用户名: 密码: 验证码:
L型凝集素和Toll、IMD信号通路关键因子在日本对虾先天免疫中的功能研究
详细信息    本馆镜像全文|  推荐本文 |  |   获取CNKI官网全文
摘要
免疫系统包括先天免疫和适应性免疫,无脊椎动物只有先天免疫。虽然在属于无脊椎动物的模式生物果蝇中,有关先天免疫研究的比较清楚,但是在海洋无脊椎动物中的研究有待投入更多的精力。本文以海洋无脊椎动物,日本囊对虾为研究对象,对其模式识别和免疫相关信号途径进行了研究。发现L型凝集素可能做为一种调理素辅助血细胞进行吞噬作用;Toll和IMD信号通路参与抗革兰氏阳性菌和革兰氏阴性菌的免疫应答,并且发现同一个抗菌肽可以受这两条信号通路的调控。
     (1)日本囊对虾的一种L型凝集素促进血细胞对病原菌的吞噬作用能力
     L型凝集素(L-Type Lectin, LTLs)含有糖类识别结构域,与来源于豆科植物种子的凝集素在结构上的折叠方式相似。这是一类I型跨膜蛋白,在动物中LTLs主要参与了蛋白的分泌过程,与糖蛋白的筛选、转运和靶向运输有关。最近有研究表明LTLs可能参与了脊椎动物的免疫应答,但在无脊椎动物先天免疫中的功能尚未见报道。我们从日本囊对虾(Marsupenaeus japonicus)中发现了一种L型凝集素并命名为MjLTL1,它含有一个信号肽、一个L型凝集素结构域和一个跨膜结构域。在鳗弧菌感染的对虾血细胞和肝胰腺中表达上调;在Ca2+的存在下能够凝集细菌,包括多种革兰氏阳性菌和革兰氏阴性菌。并能结合多种细菌,这种结合活性归因于MjLTL1能够结合脂多糖、脂磷壁酸和肽聚糖。MjLTL1能够帮助清除鳗弧菌。在将MjLTL1通过RNA干扰技术敲低表达后,对虾体内残留的鳗弧菌明显比对照组多。进一步的研究发现MjLTL1可能促进血细胞吞噬细菌。为了找到这一作用可能的机制,我们从对虾中克隆到一个解聚素和金属蛋白酶样蛋白(a disintegrin and metalloprotease-like protein)并命名为MjADAM。 ADAM能够水解膜蛋白从而介导一种胞外域脱落机制。研究发现它的组织分布和表达模式与MjLTL1类似。通过注射dsMjADAM将MjADAM的表达下调后,血细胞的吞噬效率降低了。之前有报道ADAM可以剪切位于细胞膜上的LTL,从而释放出游离的N端,这种机制称为胞外域脱落。我们的研究结果说明MjLTL1和MjADAM可能也存在相同的机制,MjADAM将鳗弧菌感染后从细胞质转移到细胞膜上的MjLTL1剪切从而释放出游离端,通过结合和凝集细菌促进血细胞吞噬细菌,做为一种调理素参与对虾的先天免疫。
     (2) Toll和IMD信号通路调控抗菌肽表达的机制研究
     果蝇中抗菌肽的表达主要受Toll和免疫缺陷(IMD)信号通路的调控。但在日本对虾中这两条信号通路,尤其是IMD信号通路的研究刚刚开始,并且,日本对虾中Toll和IMD信号通路各自调控哪些抗菌肽(AMPs)的表达,如何调控它们的表达:独立的还是合作,或存在其它机制还不清楚。为此,我们对日本囊对虾(M.japonicus)中两条通路的转录因子,分别命名为MjDorsal和MjRelish,和在信号转导过程中起关键作用的分子,命名为MjMyD88和MjIMD进行了研究。其中MjDorsal和MjMyD88属于Toll信号通路,而MjRelish和MjIMD属于IMD信号通路。MjDorsal含有RHD (Rel homology domain)结构域、ANK结构域和IPT (Ig-like, plexins, transcription factors)结构域;MjRelish含有一个RHD结构域和IκB样结构域(两个串联的ANK结构域);我们只得到MjMyD88的部分序列,该序列所编码的氨基酸是TIR结构域的一部分;MjIMD含有一个Death结构域。通过qRT-PCR发现MjDorsal主要分布于血细胞、鳃、胃和肠中;MjRelish主要分布于血细胞和肠中;MjMyD88主要分布于肝胰腺和鳃中;MjIMD主要分布于血细胞、肝胰腺、鳃和胃中。在鳗弧菌(Vibrio anguillarum)和金黄色葡萄球菌(Staphylococcus aureus)感染日本对虾后,这四种分子在血细胞、胃和肠中表达上调,但是上调表达的起始时间和持续时间不同。为了找到这两条信号通路所调控的抗菌肽(antimicrobial peptides AMPs),我们选择了15种AMPs做为候选效应基因进行表达模式筛选,发现其中5种AMPs:MjALF4, MjALF6, MjALF8, MjCrus12,MjLys4在感染鳗弧菌和金黄色葡萄球菌的对虾组织中会上调表达,但是表达上调时间和存在的组织不同,MjALF4, MjALF6和MjALF8在六种组织中都能都检测到;MjCrus12主要分布于鳃、胃和肠中;MjLys4主要分布于鳃和胃中。我们通过注射双链RNA(dsRNA)将MjDorsal、MjRelish、MjMyD88和MjIMD基因分别沉默后再分别感染鳗弧菌和金黄色葡萄球菌,通过qRT-PCR检测上述五种抗菌肽的表达模式,结果显示在MjDorsal (MjMyD88)干扰组并注射金黄色葡萄球菌后,这五种抗菌肽与对照组(注射dsGFP)相比,其表达量不再被革兰氏阳性菌刺激所诱导而上调,而针对鳗弧菌的感染它们的表达仍然明显上调;在MjRelish和MjIMD干扰组并注射革兰氏阴性菌鳗弧菌后,上述五种抗菌肽不再上调表达,而对金黄色葡萄球菌的感染与对照组相同依然上调表达。以上的结果表明,在日本对虾中,Toll信号通路主要被革兰氏阳性菌的感染所激活,而IMD信号通路主要被抗革兰氏阴性菌的感染所激活,调控抗菌肽的表达。同一种抗菌肽可以受不同信号途径的调控。
Immune system of vertebrates including ininnate and adaptive immunity, while the invertebrate possess innate immunity only. Although a great progresses have been made in the study of invertebrate Drosophila innate immunity, the study in marine invertebrate immunity has a long way to go. In this paper, the innate immunity of marine invertebrate, Marsupenaeus japonicus was studied, and found that an L-type lectin functions as pattern recognition receptors and is involved in hemocyte phagocytosis. Toll and IMD signaling pathway is mainly involved in the immune response aginst the Gram-positive bacteria and gram-negative bacteria, respectively.
     (1) L-type lectin from the kuruma shrimp Marsupenaeus japonicus promotes hemocyte phagocytosis
     L-type lectins (LTLs) contain a luminal carbohydrate recognition domain, which exhibits homology to leguminous lectins. These type I membrane proteins are involved in the early secretory pathway of animals, and have functions in glycoprotein sorting, trafficking and targeting. Recent studies suggest that LTLs may be involved in immune responses in vertebrates, but no functional studies have been reported. This study reports an LTL, designated as MjLTLl, from the kuruma shrimp Marsupenaeus japonicus. MjLTL consists of a signal peptide, leguminous lectin domain, and transmembrane region. It was upregulated following challenge of shrimp with Vibrio anguillarum. MjLTL1could agglutinate several bacteria with the presence of calcium, and bind to several Gram-positive and Gram-negative bacteria through lipopolysaccharide and peptidoglycan binding. MjLTL1could enhance the clearance of V. anguillarum in vivo. MjLTL1silencing by RNA interference could impair bacterial clearance ability. Further study suggested that MjLTL promoted hemocyte phagocytosis. To analyze the possible mechanism, a disintegrin and metalloprotease-like protein (MjADAM) mediating the proteolytic release of extracellular domains from the membrane-bound precursors was also studied in the shrimp. MjADAM exhibited similar tissue location and expression profiles to MjLTL1. After knockdown of MjADAM, the hemocyte phagocytosis rate also declined significantly. ADAM was reported to have an ectodomain shedding function to LTL and release the ectodomain of the lectin from cell membrane. Therefore, our results suggest that the extracellular domain of MjLTL might be released from the cell surface as a soluble protein by MjADAM, and function as an opsonin involved in the antibacterial immune responses in shrimp.
     (2) Toll and IMD pathways cooperatively mediate antibacterial immunity in Mars
     Inducible expression of antimicrobial peptide genes is regulated by the Toll and immune deficiency (IMD) pathways in Drosophila, the researchs of the two signal pathways are just beginning, especially the IMD pathway in shrimp. Our knowledge about which AMPs s are regulated by the two signal pathways, and how the two signal pathways to regulate the shrimp AMP gene, are still dimness up to date. Here we describe the functional analysis of Toll and IMD pathways in M. japonicus. We identified a Relish and Dorsal homologue, MjRelish and MjDorsal, MjMyD88and MjImd from the shrimp. MjRelish contains a conserved Rel homology domain (RHD), a signal peptide, an IκB-like domain (two ankyrin repeats) and a transmembrane domain. MjDorsal contains a RHD, and an Ig-like, plexins, transcription factors (IPT) domain. MjRelish and MjDorsal mRNAs were expressed at different levels in different tissues including hemocytes, heart, hepatopancreas, gill, stomach and intestin, the highest expression level of them are all in the hemocytes and hepatopancreas. MjRelish was up-regulated in hemocyte and hepatopancreas when shrimp were injected with V. anguillarium, it was also up-regulated in hepatopancreas when shrimp were stimulated with S. aureus. MjDorsal was up-regulated in hemocytes and hepatopancreas when shrimp were injected with V. anguillarium, or with S. aureus. Spatio-temporal expression profiles of15AMPs in M. japonicus were detected after injection of V. anguillarium or S. aureus. Five of which (MJALF4, MjALF6, MjALF8, MjCrusl2, MjLys4) were up-regulated in hemocytes of shrimp stimulated with V. anguillarium or S. aureus. After knocking down of MjRelish, or MjImd, the5AMPs were no more up-regulated in hemocytes of shrimp stimulated by V. anguillarium, but the silencing of MjRelish or MjImd had no effect on the expression of the5AMPs in hemocytes of shrimp post injection of S. aureus. After knocking down MjDorsal or MjMyD88, the5AMPs were not up-regulated in hemocytes of shrimp stimulated by S. aureus, but had no effect on expression profiles of the5AMPs in hemocytes of shrimp injected of S. aureus. These results suggested that (1) shrimp Toll pathway was activeted by Gram-positive bacteria challenge and regulated5-AMP expression. IMD pathway was activited by Gram-negtive bacteria and regulated the expression of5AMPs,(2) same AMP could be regulated by two different pathways.
引文
Adachi, Y., Ishii, T., Ikeda, Y., Hoshino, A., Tamura, H., Aketagawa, J., Tanaka, S., Ohno, N.,2004. Characterization of beta-glucan recognition site on C-type lectin, dectin 1. Infect Immun 72, 4159-4171.
    Adang, M.J., Spence, K.D.,1981. Surface morphology of peritrophic membrane formation in the cabbage looper, Trichoplusia ni. Cell Tissue Res 218,141-147.
    Agaisse, H., Perrimon, N.,2004. The roles of JAK/STAT signaling in Drosophila immune responses. Immunol Rev 198,72-82.
    Agaisse, H., Petersen, U.M., Boutros, M., Mathey-Prevot, B., Perrimon, N.,2003. Signaling role of hemocytes in Drosophila JAK/STAT-dependent response to septic injury. Dev Cell 5,441-450.
    Aggarwal, K., Silverman, N.,2008. Positive and negative regulation of the Drosophila immune response. BMB Rep 41,267-277.
    Ahmed, A.U., Schmidt, R.L., Park, C.H., Reed, N.R., Hesse, S.E., Thomas, C.F., Molina, J.R., Deschamps, C., Yang, P., Aubry, M.C., Tang, A.H.,2008. Effect of disrupting seven-in-absentia homolog 2 function on lung cancer cell growth. J Natl Cancer Inst 100,1606-1629.
    Ambrose, R.L., Mackenzie, J.M.,2013. ATF6 signaling is required for efficient West Nile virus replication by promoting cell survival and inhibition of innate immune responses. J Virol 87, 2206-2214.
    Andrade-Coelho, C.A., Santos-Mallet, J., Souza, N.A., Lins, U., Meirelles, M.N., Rangel, E.F.,2001. Ultrastructural features of the midgut epithelium of females Lutzomyia intermedia (Eutz & Neiva, 1912) (Diptera:Psychodidae:Phlebotominae). Mem Inst Oswaldo Cruz 96,1141-1151.
    Aono, H., Diaz, GG, Mori, K.,1994. Cytolysis of hemocytes induced by serum and plasma in three crustaceans, Panulirus japonicus, Penaeus japonicus, and Homarus americanus. Dev Comp Immunol 18,265-275.
    Arbouzova, N.I., Zeidler, M.P.,2006. JAK/STAT signalling in Drosophila:insights into conserved regulatory and cellular functions. Development 133,2605-2616.
    Arnot, C.J., Gay, N.J., Gangloff, M.,2010. Molecular mechanism that induces activatioa of Spatzle, the ligand for the Drosophila Toll receptor. J Biol Chem 285,19502-19509.
    Arts, J.A., Cornelissen, F.H., Cijsouw, T., Hermsen, T., Savelkoul, H.F., Stet, R.J.,2007. Molecular cloning and expression of a Toll receptor in the giant tiger shrimp, Penaeus monodon. Fish Shellfish Immunol 23,504-513.
    Aspan, A., Huang, T.S., Cerenius, L., Soderhall, K.,1995. cDNA cloning of prophenoloxidase from the freshwater crayfish Pacifastacus leniusculus and its activation. Proc Natl Acad Sci U S A 92, 939-943.
    Avadhanula, V., Weasner, B.P., Hardy, G.G, Kumar, J.P., Hardy, R.W.,2009. A novel system for the launch of alphavirus RNA synthesis reveals a role for the Imd pathway in arthropod antiviral response. PLoS Pathog 5, e1000582.
    Ayyar, S., Pistillo, D., Calleja, M., Brookfield, A., Gittins, K., Goldstone, C., Simpson, P.,2007. NF-kappaB/Rel-mediated regulation of the neural fate in Drosophila. PLoS One 2, el 178.
    Bachere, E., Gueguen, Y., Gonzalez, M., de Lorgeril, J., Gamier, J., Romestand, B.,2004. Insights into the anti-microbial defense of marine invertebrates:the penaeid shrimps and the oyster Crassostrea gigas. Immunol Rev 198,149-168.
    Bae, S.H., Kim, B.R., Kang, B.J., Tsutsui, N., Okutsu, T., Shinji, J., Jang, I.K., Han, C.H., Wilder, M.N., 2012. Molecular cloning of prophenoloxidase and the effects of dietary beta-glucan and rutin on immune response in hemocytes of the fleshy shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol 33,597-604.
    Baeg, G.H., Zhou, R., Perrimon, N.,2005. Genome-wide RNAi analysis of JAK/STAT signaling components in Drosophila. Genes Dev 19,1861-1870.
    Basseri, S., Austin, R.C.,2012. Endoplasmic reticulum stress and lipid metabolism:mechanisms and therapeutic potential. Biochem Res Int 2012,841362.
    Belvin, M.P., Anderson, K.V.,1996. A conserved signaling pathway:the Drosophila toll-dorsal pathway. Annu Rev Cell Dev Biol 12,393-416.
    Ben-Tekaya, H., Miura, K., Pepperkok, R., Hauri, H.P.,2005. Live imaging of bidirectional traffic from the ERGIC. J Cell Sci 118,357-367.
    Bettencourt, R., Asha, H., Dearolf, C., Ip, Y.T.,2004. Hemolymph-dependent and -independent responses in Drosophila immune tissue. J Cell Biochem 92,849-863.
    Bischoff, V., Vignal, C., Boneca, I.G, Michel, T., Hoffmann, J.A., Royet, J.,2004. Function of the drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria. Nat Immunol 5,1175-1180.
    Bitra, K., Suderman, R.J., Strand, M.R.,2012. Polydnavirus Ank proteins bind NF-kappaB homodimers and inhibit processing of Relish. PLoS Pathog 8, e1002722.
    Blobel, C.P.,2005. ADAMs:key components in EGFR signalling and development. Nat Rev Mol Cell Biol 6,32-43.
    Blohmke, C.J., Mayer, M.L., Tang, A.C., Hirschfeld, A.F., Fjell, C.D., Sze, M.A., Falsafi, R., Wang, S., Hsu, K., Chilvers, M.A., Hogg, J.C., Hancock, R.E., Turvey, S.E.,2012. Atypical activation of the unfolded protein response in cystic fibrosis airway cells contributes to p38 MAPK-mediated innate immune responses. J Immunol 189,5467-5475.
    Bolognesi, R., Ribeiro, A.F., Terra, W.R., Ferreira, C.,2001. The peritrophic membrane of Spodoptera frugiperda:secretion of peritrophins and role in immobilization and recycling digestive enzymes. Arch Insect Biochem Physiol 47,62-75.
    Brasier, A.R.,2006. The NF-kappaB regulatory network. Cardiovasc Toxicol 6,111-130.
    Brogden, K.A.,2005. Antimicrobial peptides:pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3,238-250.
    Buchon, N., Poidevin, M., Kwon, H.M., Guillou, A., Sottas, V., Lee, B.L., Lemaitre, B.,2009. A single modular serine protease integrates signals from pattern-recognition receptors upstream of the Drosophila Toll pathway. Proc Natl Acad Sci U S A 106,12442-12447.
    Busse, M.S., Arnold, C.P., Towb, P., Katrivesis, J., Wasserman, S.A.,2007. A kappaB sequence code for pathway-specific innate immune responses. EMBO J 26,3826-3835.
    Cabassi, C.S., Taddei, S., Cavirani, S., Baroni, M.C., Sansoni, P., Romani, A.A.,2013. Broad-spectrum activity of a novel antibiotic peptide against multidrug-resistant veterinary isolates. Vet J 198, 534-537.
    Cerenius, L., Bangyeekhun, E., Keyser, P., Soderhall,1., Soderhall, K.,2003. Host prophenoloxidase expression in freshwater crayfish is linked to increased resistance to the crayfish plague fungus, Aphanomyces astaci. Cell Microbiol 5,353-357.
    Cerenius, L., Lee, B.L., Soderhall, K.,2008. The proPO-system:pros and cons for its role in invertebrate immunity. Trends Immunol 29,263-271.
    Chaikeeratisak, V., Somboonwiwat, K., Wang, H.C., Lo, C.F., Tassanakajon, A.,2012. Proteomic analysis of differentially expressed proteins in the lymphoid organ of Vibrio harveyi-infected Penaeus monodon. Mol Biol Rep 39,6367-6377.
    Chaung, H.C., Huang, T.C., Yu, J.H., Wu, M.L., Chung, W.B.,2009. Immunomodulatory effects of beta-glucans on porcine alveolar macrophages and bone marrow haematopoietic cell-derived dendritic cells. Vet Immunol Immunopathol 131,147-157.
    Chen, W.Y., Ho, K.C., Leu, J.H., Liu, K.F., Wang, H.C., Kou, GH., Lo, C.F.,2008. WSSV infection activates STAT in shrimp. Dev Comp Immunol 32,1142-1150.
    Chen, Y.H., Zhao, L., Pang, L.R., Li, X.Y., Weng, S.P., He, J.G,2012. Identification and characterization of Inositol-requiring enzyme-1 and X-box binding protein 1, two proteins involved in the unfolded protein response of Litopenaeus vannamei. Dev Comp Immunol 38, 66-77.
    Choe, K.M., Werner, T., Stoven, S., Hultmark, D., Anderson, K.V.,2002. Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila. Science 296,359-362.
    Choi, J., Tanaka, K., Cao, Y, Qi, Y, Qiu, J., Liang, Y, Lee, S.Y., Stacey, G,2014. Identification of a plant receptor for extracellular ATP. Science 343,290-294.
    Copley, R.R., Totrov, M., Linnell, J., Field, S., Ragoussis, J., Udalova, I.A.,2007. Functional conservation of Rel binding sites in drosophilid genomes. Genome Res 17,1327-1335.
    Dam, T.K., Brewer, C.F.,2010. Lectins as pattern recognition molecules:the effects of epitope density in innate immunity. Glycobiology 20,270-279.
    De Gregorio, E., Spellman, P.T., Tzou, P., Rubin, GM., Lemaitre, B.,2002. The Toll and Imd pathways are the major regulators of the immune response in Drosophila. EMBO J 21,2568-2579.
    de la Vega, E., O'Leary, N.A., Shockey, J.E., Robalino, J., Payne, C., Browdy, C.L., Warr, GW., Gross, P.S.,2008. Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF):a broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection. Mol Immunol 45,1916-1925.
    DeDiego, M.L., Nieto-Torres, J.L., Jimenez-Guardeno, J.M., Regla-Nava, J.A., Alvarez, E., Oliveros, J.C., Zhao, J., Fett, C., Perlman, S., Enjuanes, L.,2011. Severe acute respiratory syndrome coronavirus envelope protein regulates cell stress response and apoptosis. PLoS Pathog 7, e1002315.
    Derksen, A.C., Granados, R.R.,1988. Alteration of a lepidopteran peritrophic membrane by baculoviruses and enhancement of viral infectivity. Virology 167,242-250.
    Desclos-Theveniau, M., Arnaud, D., Huang, T.Y., Lin, GJ., Chen, W.Y., Lin, Y.C., Zimmerli, L.,2012. The Arabidopsis lectin receptor kinase LecRK-V.5 represses stomatal immunity induced by Pseudomonas syringae pv. tomato DC3000. PLoS Pathog 8, e 1002513.
    Dimitriadis, V.K.,1985. Ultrastructural analysis of peritrophic membrane formation of Drosophila auraria larvae. J Submicrosc Cytol 17,293-297.
    Dodd, R.B., Drickamer, K.,2001. Lectin-like proteins in model organisms:implications for evolution of carbohydrate-binding activity. Glycobiology 11,71R-79R.
    Du, X.J., Wang, J.X., Liu, N., Zhao, X.F., Li, F.H., Xiang, J.H.,2006. Identification and molecular characterization of a peritrophin-like protein from fleshy prawn (Fenneropenaeus chinensis). Mol Immunol 43,1633-1644.
    El Chamy, L., Leclerc, V, Caldelari, I., Reichhart, J.M.,2008. Sensing of 'danger signals' and pathogen-associated molecular patterns defines binary signaling pathways 'upstream' of Toll. Nat Immunol 9,1165-1170.
    El Kebir, D., Jozsef, L., Pan, W., Wang, L., Filep, J.G.,2009. Bacterial DNA activates endothelial cells and promotes neutrophil adherence through TLR9 signaling. J Immunol 182,4386-4394.
    Erturk-Hasdemir, D., Broemer, M., Leulier, F., Lane, W.S., Paquette, N., Hwang, D., Kim, C.H., Stoven, S., Meier, P., Silverman, N.,2009. Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Proc Natl Acad Sci U S A 106, 9779-9784.
    Feng, N., Wang, D., Wen, R., Li, F.,2014. Functional analysis on immune deficiency (IMD) homolog gene in Chinese shrimp Fenneropenaeus chinensis. Mol Biol Rep 41,1437-1444.
    Feng, X., Krishnan, K., Richie, D.L., Aimanianda, V., Hartl, L., Grahl, N., Powers-Fletcher, M.V., Zhang, M., Fuller, K.K., Nierman, W.C., Lu, L.J., Latge, J.P., Woollett, L., Newman, S.L., Cramer, R.A., Jr., Rhodes, J.C., Askew, D.S.,2011. HacA-independent functions of the ER stress sensor IreA synergize with the canonical UPR to influence virulence traits in Aspergillus jumigatus. PLoS Pathog 7, e1002330.
    Fiedler, K., Simons, K.,1994. A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins. Cell 77,625-626.
    Fraldi, A., Zito, E., Annunziata, F., Lombardi, A., Cozzolino, M., Monti, M., Spampanato, C., Ballabio, A., Pucci, P., Sitia, R., Cosma, M.P.,2008. Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44. Hum Mol Genet 17,2610-2621.
    Gallo, C., Schiavon, F., Ballarin, L.,2011. Insight on cellular and humoral components of innate immunity in Squilla mantis (Crustacea, Stomatopoda). Fish Shellfish Immunol 31,423-431.
    Ganesan, S., Aggarwal, K., Paquette, N., Silverman, N.,2011. NF-kappaB/Rel proteins and the humoral immune responses of Drosophila melanogaster. Curr Top Microbiol Immunol 349, 25-60.
    Gendrin, M., Welchman, D.P., Poidevin, M., Herve, M., Lemaitre, B.,2009. Long-range activation of systemic immunity through peptidoglycan diffusion in Drosophila. PLoS Pathog 5, e1000694.
    Ghosh, S., May, M.J., Kopp, E.B.,1998. NF-kappa B and Rel proteins:evolutionarily conserved mediators of immune responses. Annu Rev Immunol 16,225-260.
    Gonzalez-Crespo, S., Levine, M.,1994. Related target enhancers for dorsal and NF-kappa B signaling pathways. Science 264,255-258.
    Gottar, M., Gobert, V., Matskevich, A.A., Reichhart, J.M., Wang, C., Butt, T.M., Belvin, M., HoffMann, J.A., Ferrandon, D.,2006. Dual detection of fungal infections in Drosophila via recognition of glucans and sensing of virulence factors. Cell 127,1425-1437.
    Gottar, M., Gobert, V., Michel, T., Belvin, M., Duyk, G., Hoffmann, J.A., Ferrandon, D., Royet, J., 2002. The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature 416,640-644.
    Govind, S.,2008. Innate immunity in Drosophila:Pathogens and pathways. Insect Sci 15,29-43.
    Gronholm, J., Kaustio, M., Myllymaki, H., Kallio, J., Saarikettu, J., Kronhamn, J., Valanne, S., Silvennoinen, O., Ramet, M.,2012. Not4 enhances JAK/STAT pathway-dependent gene expression in Drosophila and in human cells. FASEB J 26,1239-1250.
    Gueguen, Y., Gamier, J., Robert, L., Lefranc, M.P., Mougenot, I., de Lorgeril, J., Janech, M., Gross, P.S., Warr, G.W., Cuthbertson, B., Barracco, M.A., Bulet, P., Aumelas, A., Yang, Y., Bo, D., Xiang, J., Tassanakajon, A., Piquemal, D., Bachere, E.,2006. PenBase, the shrimp antimicrobial peptide penaeidin database:sequence-based classification and recommended nomenclature. Dev Comp Immunol 30,283-288.
    Hall, M., Wang, R., van Antwerpen, R., Sottrup-Jensen, L., Soderhall, K.,1999. The crayfish plasma clotting protein:a vitellogenin-related protein responsible for clot formation in crustacean blood. Proc Natl Acad Sci U S A 96,1965-1970.
    Han-Ching Wang, K., Tseng, C.W., Lin, H.Y., Chen, I.T., Chen, Y.H., Chen, Y.M., Chen, T.Y., Yang, H.L.,2010. RNAi knock-down of the Litopenaeus vannamei Toll gene (LvToll) significantly increases mortality and reduces bacterial clearance after challenge with Vibrio harveyi. Dev Comp Immunol 34,49-58.
    Han, F., Zhang, X.,2007. Characterization of a ras-related nuclear protein (Ran protein) up-regulated in shrimp antiviral immunity. Fish Shellfish Immunol 23,937-944.
    Hara-Kuge, S., Ohkura, T., Ideo, H., Shimada, O., Atsumi, S., Yamashita, K.,2002. Involvement of VIP36 in intracellular transport and secretion of glycoproteins in polarized Madin-Darby canine kidney (MDCK) cells. J Biol Chem 277,16332-16339.
    Harper, M.S., Granados, R.R.,1999. Peritrophic membrane structure and formation of larvalTrichoplusia niwith an investigation on the secretion patterns of a PM mucin. Tissue Cell 31, 202-211.
    Harper, M.S., Hopkins, T.L.,1997. Peritrophic membrane structure and secretion in European corn borer larvae(Ostrinia nubilalis). Tissue Cell 29,463-475.
    Harper, M.S., Hopkins, T.L., Czapla, T.H.,1998. Effect of wheat germ agglutinin on formation and structure of the peritrophic membrane in European corn borer(Ostrinia nubilalis)larvae. Tissue Cell 30,166-176.
    Hassan, I.H., Zhang, M.S., Powers, L.S., Shao, J.Q., Baltrusaitis, J., Rutkowski, D.T., Legge, K., Monick, M.M.,2012. Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway. J Biol Chem 287,4679-4689.
    Hauri, H., Appenzeller, C., Kuhn, F., Nufer, O.,2000a. Lectins and traffic in the secretory pathway. FEBS Lett 476,32-37.
    Hauri, H.P., Kappeler, F., Andersson, H., Appenzeller, C.,2000b. ERGIC-53 and traffic in the secretory pathway. J Cell Sci 113 (Pt 4),587-596.
    Hedengren-Olcott, M., Olcott, M.C., Mooney, D.T., Ekengren, S., Geller, B.L., Taylor, B.J.,2004. Differential activation of the NF-kappaB-like factors Relish and Dif in Drosophila melanogaster by fungi and Gram-positive bacteria. J Biol Chem 279,21121-21127.
    Hetru, C., Hoffmann, J.A.,2009. NF-kappaB in the immune response of Drosophila. Cold Spring Harb PerspectBiol 1, a000232.
    Hoffmann, J.A., Kafatos, F.C., Janeway, C.A., Ezekowitz, R.A.,1999. Phylogenetic perspectives in innate immunity. Science 284,1313-1318.
    Honti, V., Csordas, G., Kurucz, E., Markus, R., Ando, I.,2014. The cell-mediated immunity of Drosophila melanogaster:hemocyte lineages, immune compartments, microanatomy and regulation. Dev Comp Immunol 42,47-56.
    Hou, F., He, S., Liu, Y., Zhu, X., Sun, C., Liu, X.,2014. RNAi knock-down of shrimp Litopenaeus vannamei Toll gene and immune deficiency gene reveals their difference in regulating antimicrobial peptides transcription. Dev Comp Immunol 44,255-260.
    Hou, F., Wang, X., Qian, Z., Liu, Q., Liu, Y, He, S., Mi, X., Bai, C., Sun, C., Liu, X.,2013. Identification and functional studies of Akirin, a potential positive nuclear factor of NF-kappaB signaling pathways in the Pacific white shrimp, Litopenaeus vannamei. Dev Comp Immunol 41, 703-714.
    Hou, S.X., Zheng, Z., Chen, X., Perrimon, N.,2002. The Jak/STAT pathway in model organisms: emerging roles in cell movement. Dev Cell 3,765-778.
    Hsieh, S.L., Wu, C.C., Liu, C.H., Lian, J.L.,2013. Effects of the water extract of Gynura bicolor (Roxb. & Willd.) DC on physiological and immune responses to Vibrio alginolyticus infection in white shrimp (Litopenaeus vannamei). Fish Shellfish Immunol 35,18-25.
    Hu, S., Yang, X.,2000. dFADD, a novel death domain-containing adapter protein for the Drosophila caspase DREDD. J Biol Chem 275,30761-30764.
    Hu, X., Yagi, Y, Tanji, T., Zhou, S., Ip, Y.T.,2004. Multimerization and interaction of Toll and Spatzle in Drosophila. Proc Natl Acad Sci U S A 101,9369-9374.
    Huang, F., Kao, C.Y, Wachi, S., Thai, P., Ryu, J., Wu, R.,2007. Requirement for both JAK-mediated PI3K signaling and ACT1/TRAF6/TAK1-dependent NF-kappaB activation by IL-17A in enhancing cytokine expression in human airway epithelial cells. J Immunol 179,6504-6513.
    Huang, X.D., Yin, Z.X., Jia, X.T., Liang, J.P., Ai, H.S., Yang, L.S., Liu, X., Wang, P.H., Li, S.D., Weng, S.P., Yu, X.Q., He, J.G.,2010. Identification and functional study of a shrimp Dorsal homologue. Dev Comp Immunol 34,107-113.
    Huang, X.D., Yin, Z.X., Liao, J.X., Wang, P.H., Yang, L.S., Ai, H.S., Gu, Z.H., Jia, X.T., Weng, S.P., Yu, X.Q., He, J.G.,2009. Identification and functional study of a shrimp Relish homologue. Fish Shellfish Immunol 27,230-238.
    Huh, J.R., Foe, I., Muro, I., Chen, C.H., Seol, J.H., Yoo, S.J., Guo, M., Park, J.M., Hay, B.A.,2007. The Drosophila inhibitor of apoptosis (LAP) DIAP2 is dispensable for cell survival, required for the innate immune response to gram-negative bacterial infection, and can be negatively regulated by the reaper/hid/grim family of IAP-binding apoptosis inducers. J Biol Chem 282,2056-2068.
    Hultmark, D.,2003. Drosophila immunity:paths and patterns. Curr Opin Immunol 15,12-19.
    Imler, J.L., Hoffmann, J.A.,2001. Toll receptors in innate immunity. Trends Cell Biol 11,304-311.
    Ip, Y.T., Reach, M., Engstrom, Y, Kadalayil, L., Cai, H., Gonzalez-Crespo, S., Tatei, K., Levine, M., 1993. Dif, a dorsal-related gene that mediates an immune response in Drosophila. Cell 75, 753-763.
    Itin, C, Kappeler, F., Linstedt, A.D., Hauri, H.P.,1995a. A novel endocytosis signal related to the KKXX ER-retrieval signal. EMBO J 14,2250-2256.
    Itin, C., Schindler, R., Hauri, H.P.,1995b. Targeting of protein ERGIC-53 to the ER/ERGIC/cis-Golgi recycling pathway. J Cell Biol 131,57-67.
    Iwanaga, S., Lee, B.L.,2005. Recent advances in the innate immunity of invertebrate animals. J Biochem Mol Biol 38,128-150.
    Jakovac, H., Grebic, D., Barac-Latas, V., Mrakovcic, I., Radosevic-Stasic, B.,2013. Expression pattern of the endoplasmic reticulum stress protein gp96 in monophasic and chronic relapsing form of experimental autoimmune encephalomyelitis in rats. Histol Histopathol 28,61-78.
    Jang, I.H., Chosa, N., Kim, S.H., Nam, H.J., Lemaitre, B., Ochiai, M., Kambris, Z., Brun, S., Hashimoto, C, Ashida, M., Brey, P.T., Lee, W.J.,2006. A Spatzle-processing enzyme required for toll signaling activation in Drosophila innate immunity. Dev Cell 10,45-55.
    Jiravanichpaisal, P., Lee, B.L., Soderhall, K.,2006. Cell-mediated immunity in arthropods: hematopoiesis, coagulation, melanization and opsonization. Immunobiology 211,213-236.
    Jitvaropas, R., Amparyup, P., Gross, P.S., Tassanakajon, A.,2009. Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus monodon. Comp Biochem Physiol B Biochem Mol Biol 153,236-243.
    Johansson, M.W.,1999. Cell adhesion molecules in invertebrate immunity. Dev Comp Immunol 23, 303-315.
    Kamiya, Y., Kamiya, D., Yamamoto, K., Nyfeler, B., Hauri, H.P., Kato, K.,2008. Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36. J Biol Chem 283, 1857-1861.
    Kang, C.J., Xue, J.F., Liu, N., Zhao, X.F., Wang, J.X.,2007. Characterization and expression of a new subfamily member of penaeidin antimicrobial peptides (penaeidin 5) from Fenneropenaeus chinensis. Mol Immunol 44,1535-1543.
    Kato, N., Dasgupta, R., Smartt, C.T., Christensen, B.M.,2002. Glucosamine:fructose-6-phosphate aminotransferase:gene characterization, chitin biosynthesis and peritrophic matrix formation in Aedes aegypti. Insect Mol Biol 11,207-216.
    Kawai, T., Akira, S.,2010. The role of pattern-recognition receptors in innate immunity:update on Toll-like receptors. Nat Immunol 11,373-384.
    Kerrigan, A.M., Brown, GD.,2009. C-type lectins and phagocytosis. Immunobiology 214,562-575.
    Kilpatrick, D.C.,2002. Animal lectins:a historical introduction and overview. Biochim Biophys Acta 1572,187-197.
    Kleinnijenhuis, J., Oosting, M., Joosten, L.A., Netea, M.G, Van Crevel, R.,2011. Innate immune recognition of Mycobacterium tuberculosis. Clin Dev Immunol 2011,405310.
    Kleino, A., Valanne, S., Ulvila, J., Kallio, J., Myllymaki, H., Enwald, H., Stoven, S., Poidevin, M., Ueda, R., Hultmark, D., Lemaitre, B., Ramet, M.,2005. Inhibitor of apoptosis 2 and TAK1-binding protein are components of the Drosophila Imd pathway. EMBO J 24,3423-3434.
    Krusong, K., Poolpipat, P., Supungul, P., Tassanakajon, A.,2012. A comparative study of antimicrobial properties of crustinPml and crustinPm7 from the black tiger shrimp Penaeus monodon. Dev Comp Immunol 36,208-215.
    Kuhlman, M., Joiner, K., Ezekowitz, R.A.,1989. The human mannose-binding protein functions as an opsonin. J Exp Med 169,1733-1745
    Kunsch, C., Ruben, S.M., Rosen, C.A.,1992. Selection of optimal kappa B/Rel DNA-binding motifs: interaction of both subunits of NF-kappa B with DNA is required for transcriptional activation. Mol Cell Biol 12,4412-4421.
    Kurata, S.,2010. Extracellular and intracellular pathogen recognition by Drosophila PGRP-LE and PGRP-LC. Int Immunol 22,143-148.
    Lan, J.F., Zhou, J., Zhang, X.W., Wang, Z.H., Zhao, X.F., Ren, Q., Wang, J.X.,2013. Characterization of an immune deficiency homolog (IMD) in shrimp(Fenneropenaeus chinensis) and crayfish (Procambarus clarkif). Dev Comp Immunol 41,608-617.
    Lee, S.Y., Soderhall, K.,2001. Characterization of a pattern recognition protein, a masquerade-like protein, in the freshwater crayfish Pacifastacus leniusculus. J Immunol 166,7319-7326.
    Leelatanawit, R., Klinbunga, S., Aoki, T., Hirono, I., Valyasevi, R., Menasveta, P.,2008. Suppression subtractive hybridization (SSH) for isolation and characterization of genes related to testicular development in the giant tiger shrimp Penaeus monodon. BMB Rep 41,796-802.
    Lemaitre, B., Hoffmann, J.,2007. The host defense of Drosophila melanogaster. Annu Rev Immunol 25,697-743.
    Lemaitre, B., Kromer-Metzger, E., Michaut, L., Nicolas, E., Meister, M., Georgel, P., Reichhart, J.M., Hoffmann, JA.,1995. A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense. Proc Natl Acad Sci U S A 92,9465-9469.
    Lemaitre, B., Nicolas, E., Michaut, L., Reichhart, J.M., Hoffmann, J.A.,1996. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86,973-983.
    Lemaitre, B., Reichhart, J.M., Hoffmann, J.A.,1997. Drosophila host defense:differential induction of antimicrobial peptide genes after infection by various classes of microorganisms. Proc Natl Acad Sci U S A 94,14614-14619.
    Leulier, F., Parquet, C., Pili-Floury, S., Ryu, J.H., Caroff, M., Lee, W.J., Mengin-Lecreulx, D., Lemaitre, B.,2003. The Drosophila immune system detects bacteria through specific peptidoglycan recognition. Nat Immunol 4,478-484.
    Leulier, F., Vidal, S., Saigo, K., Ueda, R., Lemaitre, B.,2002. Inducible expression of double-stranded RNA reveals a role for dFADD in the regulation of the antibacterial response in Drosophila adults. Curr Biol 12,996-1000.
    Li, B., Gao, B., Ye, L., Han, X., Wang, W., Kong, L., Fang, X., Zeng, Y., Zheng, H., Li, S., Wu, Z., 2007. Hepatitis B virus X protein (HBx) activates ATF6 and IRE1-XBP1 pathways of unfolded protein response. Virus Res 124,44-49.
    Li, F., Wang, D., Li, S., Yan, H., Zhang, J., Wang, B., Xiang, J.,2010. A Dorsal homolog (FcDorsal) in the Chinese shrimp Fenneropenaeus chinensis is responsive to both bacteria and WSSV challenge. Dev Comp Immunol 34,874-883.
    Li, F., Xiang, J.,2013a. Recent advances in researches on the innate immunity of shrimp in China. Dev Comp Immunol 39,11-26.
    Li, F., Xiang, J.,2013b. Signaling pathways regulating innate immune responses in shrimp. Fish Shellfish Immunol 34,973-980.
    Li, F., Yan, H., Wang, D., Priya, T.A., Li, S., Wang, B., Zhang, J., Xiang, J.,2009. Identification of a novel relish homolog in Chinese shrimp Fenneropenaeus chinensis and its function in regulating the transcription of antimicrobial peptides. Dev Comp Immunol 33,1093-1101.
    Li, H.D., Liu, W.X., Michalak, M.,2011. Enhanced clathrin-dependent endocytosis in the absence of calnexin. PLoS One 6, e21678.
    Li, L., Wang, J.X., Zhao, X.F., Kang, C.J., Liu, N., Xiang, J.H., Li, F.H., Sueda, S., Kondo, H.,2005. High level expression, purification, and characterization of the shrimp antimicrobial peptide, Ch-penaeidin, in Pichia pastoris. Protein Expr Purif 39,144-151.
    Li, S., Zhang, X., Sun, Z., Li, F., Xiang, J.,2013a. Transcriptome analysis on Chinese shrimp Fenneropenaeus chinensis during WSSV acute infection. PLoS One 8, e58627.
    Li, W., Tang, X., Xing, J., Sheng, X., Zhan, W.,2014. Proteomic Analysis of Differentially Expressed Proteins in Fenneropenaeus chinensis Hemocytes upon White Spot Syndrome Virus Infection. PLoS One 9, e89962.
    Li, X.Y., Pang, L.R., Chen, Y.G., Weng, S.P., Yue, H.T., Zhang, Z.Z., Chen, Y.H., He, J.G.,2013b. Activating transcription factor 4 and X box binding protein 1 of Litopenaeus vannamei transcriptional regulated white spot syndrome virus genes Wsv023 and Wsv083. PLoS One 8, e62603.
    Liang, K.C., Suzuki, Y, Kumagai, Y, Nakai, K.,2014. Analysis of changes in transcription start site distribution by a classification approach. Gene 537,29-40.
    Ligoxygakis, P., Pelte, N., Ji, C., Leclerc, V., Duvic, B., Belvin, M., Jiang, H., Hoffmann, J.A., Reichhart, J.M.,2002. A serpin mutant links Toll activation to melanization in the host defence of Drosophila. EMBO J 21,6330-6337.
    Lin, Y.C., Chen, J.C., SN, C.M., WZ, W.M., AS, N.A.S., Cheng, S.Y., Hsu, C.H.,2012. Modulation of innate immunity and gene expressions in white shrimp Litopenaeus vannamei following long-term starvation and re-feeding. Results Immunol 2,148-156.
    Liu, W., Han, F., Zhang, X.,2009. Ran GTPase regulates hemocytic phagocytosis of shrimp by interaction with myosin. J Proteome Res 8,1198-1206.
    Lofgren, S.E., Miletti, L.C., Steindel, M., Bachere, E., Barracco, M.A.,2008. Trypanocidal and leishmanicidal activities of different antimicrobial peptides (AMPs) isolated from aquatic animals. Exp Parasitol 118,197-202.
    Luo, H., Dearolf, C.R.,2001. The JAK/STAT pathway and Drosophila development. Bioessays 23, 1138-1147.
    Luo, T., Zhang, X., Shao, Z., Xu, X.,2003. PmAV, a novel gene involved in virus resistance of shrimp Penaeus monodon. FEBS Lett 551,53-57.
    Makki, R., Meister, M., Pennetier, D., Ubeda, J.M., Braun, A., Daburon, V., Krzemien, J., Bourbon, H.M., Zhou, R., Vincent, A., Crozatier, M.,2010. A short receptor downregulates JAK/STAT signalling to control the Drosophila cellular immune response. PLoS Biol 8, e1000441.
    Manfruelli, P., Reichhart, J.M., Steward, R., Hoffmann, J.A., Lemaitre, B.,1999. A mosaic analysis in Drosophila fat body cells of the control of antimicrobial peptide genes by the Rel proteins Dorsal and DIF. EMBO J 18,3380-3391.
    Mangkalanan, S., Sanguanrat, P., Utairangsri, T., Sritunyalucksana, K., Krittanar, C.,2014. Characterization of the circulating hemocytes in mud crab (Scylla olivacea) revealed phenoloxidase activity. Dev Comp Immunol 44,116-123.
    Medzhitov, R., Janeway, C., Jr.,2000. Innate immunity. N Engl J Med 343,338-344.
    Medzhitov, R., Janeway, C.A., Jr.,1997. Innate immunity:the virtues of a nonclonal system of recognition. Cell 91,295-298.
    Meffert, M.K., Chang, J.M., Wiltgen, B.J., Fanselow, M.S., Baltimore, D.,2003. NF-kappa B functions in synaptic signaling and behavior. Nat Neurosci 6,1072-1078.
    Mekata, T., Kono, T., Yoshida, T., Sakai, M., Itami, T.,2008. Identification of cDNA encoding Toll receptor, MjToll gene from kuruma shrimp, Marsupenaeus japonicus. Fish Shellfish Immunol 24, 122-133.
    Meng, X., Khanuja, B.S., Ip, Y.T.,1999. Toll receptor-mediated Drosophila immune response requires Dif, an NF-kappaB factor. Genes Dev 13,792-797.
    Merlo, E., Freudenthal, R., Romano, A.,2002. The IkappaB kinase inhibitor sulfasalazine impairs long-term memory in the crab Chasmagnathus. Neuroscience 112,161-172.
    Merquiol, E., Uzi, D., Mueller, T., Goldenberg, D., Nahmias, Y, Xavier, R.J., Tirosh, B., Shibolet, O., 2011. HCV causes chronic endoplasmic reticulum stress leading to adaptation and interference with the unfolded protein response. PLoS One 6, e24660.
    Mialhe, E., Bachere, E., Boulo, V., Cadoret, J.P., Rousseau, C., Cedeno, V., Saraiva, E., Carrera, L., Calderon, J., Colwell, R.R.,1995. Future of biotechnology-based control of disease in marine invertebrates. Mol Mar Biol Biotechnol 4,275-283.
    Moreno, A.A., Mukhtar, M.S., Blanco, F., Boatwright, J.L., Moreno, I., Jordan, M.R., Chen, Y, Brandizzi, F., Dong, X., Orellana, A., Pajerowska-Mukhtar, K.M.,2012. IRE1/bZIP60-mediated unfolded protein response plays distinct roles in plant immunity and abiotic stress responses. PLoS One 7,e31944.
    Moskalyk, L.A., Oo, M.M., Jacobs-Lorena, M.,1996. Peritrophic matrix proteins of Anopheles gambiae and Aedes aegypti. Insect Mol Biol 5,261-268.
    Muller, P., Kuttenkeuler, D., Gesellchen, V., Zeidler, M.P., Boutros, M.,2005. Identification of JAK/STAT signalling components by genome-wide RNA interference. Nature 436,871-875.
    Muta, T., Iwanaga, S.,1996. The role of hemolymph coagulation in innate immunity. Curr Opin Immunol 8,41-47.
    Narasimhan, S., Rajeevan, N., Liu, L., Zhao, Y.O., Heisig, J., Pan, J., Eppler-Epstein, R., Deponte, K., Fish, D., Fikrig, E.,2014. Gut microbiota of the tick vector Ixodes scapularis modulate colonization of the lyme disease spirochete. Cell Host Microbe 15,58-71.
    Neve, E.P., Svensson, K., Fuxe, J., Pettersson, R.F.,2003. VIPL, a VIP36-like membrane protein with a putative function in the export of glycoproteins from the endoplasmic reticulum. Exp Cell Res 288,70-83.
    Nicolas, E., Reichhart, J.M., Hoffmann, J.A., Lemaitre, B.,1998. In vivo regulation of the IkappaB homologue cactus during the immune response of Drosophila. J Biol Chem 273,10463-10469.
    Niederreiter, L., Kaser, A.,2011. Endoplasmic reticulum stress and inflammatory bowel disease. Acta Gastroenterol Belg 74,330-333.
    Novak, M.L., Thorp, E.B.,2013. Shedding light on impaired efferocytosis and nonresolving inflammation. Circ Res 113,9-12.
    Nufer, O., Mitrovic, S., Hauri, H.P.,2003. Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum protein. J Biol Chem 278,15886-15896.
    Olsen, L.R., Dessen, A., Gupta, D., Sabesan, S., Sacchettini, J.C., Brewer, C.F.,1997. X-ray crystallographic studies of unique cross-linked lattices between four isomeric biantennary oligosaccharides and soybean agglutinin. Biochemistry 36,15073-15080.
    Pal, S., Wu, J., Wu, L.P.,2008. Microarray analyses reveal distinct roles for Rel proteins in the Drosophila immune response. Dev Comp Immunol 32,50-60.
    Pal, S., Wu, L.P.,2009. Pattern recognition receptors in the fly:lessons we can learn from the Drosophila melanogaster immune system. Fly (Austin) 3,121-129.
    Pan, C.Y., Peng, K.C., Lin, C.H., Chen, J.Y.,2011. Transgenic expression of tilapia hepcidin 1-5 and shrimp chelonianin in zebrafish and their resistance to bacterial pathogens. Fish Shellfish Immunol 31,275-285.
    Pan, D., He, N., Yang, Z., Liu, H., Xu, X.,2005. Differential gene expression profile in hepatopancreas of WSSV-resistant shrimp (Penaeus japonicus) by suppression subtractive hybridization. Dev Comp Immunol 29,103-112.
    Parry, G.C., Mackman, N.,1994. A set of inducible genes expressed by activated human monocytic and endothelial cells contain kappa B-like sites that specifically bind c-Rel-p65 heterodimers. J Biol Chem 269,20823-20825.
    Pietrocola, F., Izzo, V, Niso-Santano, M., Vacchelli, E., Galluzzi, L., Maiuri, M.C., Kroemer, G,2013. Regulation of autophagy by stress-responsive transcription factors. Semin Cancer Biol 23, 310-322.
    Platzer-Schultz, I., Welsch, U.,1969. [Formation and fine structure of the peritrophic membrane in larvae of Chironomus strenzkei Fittkau (Diptera)]. Z Zellforsch Mikrosk Anat 100,594-605.
    Ponprateep, S., Tassanakajon, A., Rimphanitchayakit, V,2011. A Kazal type serine proteinase SPIPm2 from the black tiger shrimp Penaeus monodon is capable of neutralization and protection of hemocytes from the white spot syndrome virus. Fish Shellfish Immunol 31,1179-1185.
    Qin, S.Y., Kawasaki, N., Hu, D., Tozawa, H., Matsumoto, N., Yamamoto, K.,2012. Subcellular localization of ERGIC-53 under endoplasmic reticulum stress condition. Glycobiology 22, 1709-1720.
    Rahnamaeian, M., Vilcinskas, A.,2012. Defense gene expression is potentiated in transgenic barley expressing antifungal peptide Metchnikowin throughout powdery mildew challenge. J Plant Res 125,115-124.
    Ramet, M., Manfruelli, P., Pearson, A., Mathey-Prevot, B., Ezekowitz, R.A.,2002. Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature 416, 644-648.
    Ramirez, J.L., Dimopoulos, G.,2010. The Toll immune signaling pathway control conserved anti-dengue defenses across diverse Ae. aegypti strains and against multiple dengue virus serotypes. Dev Comp Immunol 34,625-629.
    Rath, E., Haller, D.,2012. Unfolded protein responses in the intestinal epithelium:sensors for the microbial and metabolic environment. J Clin Gastroenterol 46 Suppl, S3-5.
    Rayms-Keller, A., Olson, K.E., McGaw, M., Oray, C., Carlson, J.O., Beaty, B.J.,1998. Effect of heavy metals on Aedes aegypti (Diptera:Culicidae) larvae. Ecotoxicol Environ Saf 39,41-47.
    Reiterer, V., Nyfeler, B., Hauri, H.P.,2010. Role of the lectin VIP36 in post-ER quality control of human alphal-antitrypsin. Traffic 11,1044-1055.
    Rijiravanich, A., Browdy, C.L., Withyachumnarnkul, B.,2008. Knocking down caspase-3 by RNAi reduces mortality in Pacific white shrimp Penaeus (Litopenaeus) vannamei challenged with a low dose of white-spot syndrome virus. Fish Shellfish Immunol 24,308-313.
    Rini, J.M.,1995a. Lectin structure. Annu Rev Biophys Biomol Struct 24,551-577.
    Rini, J.M.,1995b. X-ray crystal structures of animal lectins. Curr Opin Struct Biol 5,617-621.
    Rodriguez, J., Boulo, V., Mialhe, E., Bachere, E.,1995. Characterisation of shrimp haemocytes and plasma components by monoclonal antibodies. J Cell Sci 108 (Pt 3),1043-1050.
    Rubinstein, N., Ilarregui, J.M., Toscano, M.A., Rabinovich, GA.,2004. The role of galectins in the initiation, amplification and resolution of the inflammatory response. Tissue Antigens 64,1-12.
    Rus, F., Flatt, T., Tong, M., Aggarwal, K., Okuda, K., Kleino, A., Yates, E., Tatar, M., Silverman, N., 2013. Ecdysone triggered PGRP-LC expression controls Drosophila innate immunity. EMBO J 32,1626-1638.
    Rutschmann, S., Jung, A.C., Hetru, C., Reichhart, J.M., Hoffmann, J.A., Ferrandon, D.,2000. The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila. Immunity 12,569-580.
    Rutschmann, S., Kilinc, A., Ferrandon, D.,2002. Cutting edge:the toll pathway is required for resistance to gram-positive bacterial infections in Drosophila. J Immunol 168,1542-1546.
    Ryerse, J.S., Purcell, J.P., Sammons, R.D., Lavrik, P.B.,1992. Peritrophic membrane structure and formation in the larva of a math, Heliothis. Tissue Cell 24,751-771.
    Sabin, L.R., Hanna, S.L., Cherry, S.,2010. Innate antiviral immunity in Drosophila. Curr Opin Immunol 22,4-9.
    Sato, S., St-Pierre, C., Bhaumik, P., Nieminen, J.,2009. Galectins in innate immunity:dual functions of host soluble beta-galactoside-binding lectins as damage-associated molecular patterns (DAMPs) and as receptors for pathogen-associated molecular patterns (PAMPs). Immunol Rev 230, 172-187.
    Satoh, T., Suzuki, K., Yamaguchi, T., Kato, K.,2014. Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36. PLoS One 9, e87963.
    Schallus, T., Jaeckh, C., Feher, K., Palma, A.S., Liu, Y., Simpson, J.C., Mackeen, M., Stier, G., Gibson, T.J., Feizi, T., Pieler, T., Muhle-Goll, C.,2008. Malectin:a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Mol Biol Cell 19,3404-3414.
    Seetharaman, J., Kanigsberg, A., Slaaby, R., Leffler, H., Barondes, S.H., Rini, J.M.,1998. X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution. J Biol Chem 273,13047-13052.
    Sen, R., Baltimore, D.,1986. Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 46,705-716.
    Seto, Y., Tamura, K.,2013. Extensive differences in antifungal immune response in two Drosophila species revealed by comparative transcriptome analysis. Int J Genomics 2013,542139.
    Shaposhnikov, M., Latkin, D., Plyusnina, E., Shilova, L., Danilov, A., Popov, S., Zhavoronkov, A., Ovodov, Y., Moskalev, A.,2014. The effects of pectins on life span and stress resistance in Drosophila melanogaster. Biogerontology 15,113-127.
    Sharon, N., Lis, H.,1990. Legume lectins--a large family of homologous proteins. FASEB J 4, 3198-3208.
    Sharon, N., Lis, H.,2004. History of lectins:from hemagglutinins to biological recognition molecules. Glycobiology 14,53R-62R.
    Shen, Z., Jacobs-Lorena, M.,1998. A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression, and characterization. J Biol Chem 273, 17665-17670.
    Shi, X., Chamankhah, M., Visal-Shah, S., Hemmingsen, S.M., Erlandson, M., Braun, L., Alting-Mees, M., Khachatourians, GG, O'Grady, M., Hegedus, D.D.,2004. Modeling the structure of the type I peritrophic matrix:characterization of a Mamestra configurata intestinal mucin and a novel peritrophin containing 19 chitin binding domains. Insect Biochem Mol Biol 34,1101-1115.
    Shi, X.Z., Zhang, R.R., Jia, Y.P., Zhao, X.F., Yu, X.Q., Wang, J.X.,2009. Identification and molecular characterization of a Spatzle-like protein from Chinese shrimp (Fenneropenaeus chinensis). Fish Shellfish Immunol 27,610-617.
    Shimada, O., Hara-Kuge, S., Yamashita, K., Tosaka-Shimada, H., Yanchao, L., Yongnan, L., Atsumi, S., Ishikawa, H.,2003. Clusters of VIP-36-positive vesicles between endoplasmic reticulum and Golgi apparatus in GH3 cells. Cell Struct Funct 28,155-163.
    Shirakabe, K., Hattori, S., Seiki, M., Koyasu, S., Okada, Y.,2011. VIP36 protein is a target of ectodomain shedding and regulates phagocytosis in macrophage Raw 264.7 cells. J Biol Chem 286,43154-43163.
    Silverman, N., Paquette, N., Aggarwal, K.,2009. Specificity and signaling in the Drosophila immune response. Invertebrate Surviv J 6,163-174.
    Silverman, N., Zhou, R., Erlich, R.L., Hunter, M., Bernstein, E., Schneider, D., Maniatis, T.,2003. Immune activation of NF-kappaB and JNK requires Drosophila TAK1. J Biol Chem 278, 48928-48934.
    Silverman, N., Zhou, R., Stoven, S., Pandey, N., Hultmark, D., Maniatis, T.,2000. A Drosophila IkappaB kinase complex required for Relish cleavage and antibacterial immunity. Genes Dev 14, 2461-2471.
    Sim, S., Dimopoulos, G,2010. Dengue virus inhibits immune responses in Aedes aegypti cells. PLoS One 5, e10678.
    Singh, P., Chien, C.C., Mishra, S., Tsai, C.H., Zimmerli, L.,2012. The Arabidopsis LECTIN RECEPTOR KINASE-VI.2 is a functional protein kinase and is dispensable for basal resistance to Botrytis cinerea. Plant Signal Behav 8.
    Singh, P., Zimmerli, L.,2013. Lectin receptor kinases in plant innate immunity. Front Plant Sci 4,124.
    Small, C., Ramroop, J., Otazo, M., Huang, L.H., Saleque, S., Govind, S.,2013. An Unexpected Link Between Notch Signaling and ROS in Restricting the Differentiation of Hematopoietic Progenitors in Drosophila. Genetics.
    Somboonwiwat, K., Bachere, E., Rimphanitchayakit, V., Tassanakajon, A.,2008. Localization of anti-lipopolysaccharide factor (ALFPm3) in tissues of the black tiger shrimp, Penaeus monodon, and characterization of its binding properties. Dev Comp Immunol 32,1170-1176.
    Somboonwiwat, K., Chaikeeratisak, V., Wang, H.C., Fang Lo, C., Tassanakajon, A.,2010. Proteomic analysis of differentially expressed proteins in Penaeus monodon hemocytes after Vibrio harveyi infection. Proteome Sci 8,39.
    Somnuk, S., Tassanakajon, A., Rimphanitchayakit, V.,2012. Gene expression and characterization of a serine proteinase inhibitor PmSERPIN8 from the black tiger shrimp Penaeus monodon. Fish Shellfish Immunol 33,332-341.
    Souza-Neto, J.A., Sim, S., Dimopoulos, G,2009. An evolutionary conserved function of the JAK-STAT pathway in anti-dengue defense. Proc Natl Acad Sci U S A 106,17841-17846.
    Srinivas, V.R., Reddy, G.B., Ahmad, N., Swaminathan, C.P., Mitra, N., Surolia, A.,2001. Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization. Biochim Biophys Acta 1527,102-111.
    Stein, D., Goltz, J.S., Jurcsak, J., Stevens, L.,1998. The Dorsal-related immunity factor (Dif) can define the dorsal-ventral axis of polarity in the Drosophila embryo. Development 125, 2159-2169.
    Steiner, H., Hultmark, D., Engstrom, A., Bennich, H., Boman, H.G.,1981. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292,246-248.
    Stuart, L.M., Ezekowitz, R.A.,2008. Phagocytosis and comparative innate immunity:learning on the fly. Nat Rev Immunol 8,131-141.
    Su, W., Liu, Y., Xia, Y., Hong, Z., Li, J.,2012. The Arabidopsis homolog of the mammalian OS-9 protein plays a key role in the endoplasmic reticulum-associated degradation of misfolded receptor-like kinases. Mol Plant 5,929-940.
    Sugumaran, M., Nellaiappan, K., Valivittan, K.,2000. A new mechanism for the control of phenoloxidase activity:inhibition and complex formation with quinone isomerase. Arch Biochem Biophys 379,252-260.
    Sun, C., Shao, H.L., Zhang, X.W., Zhao, X.F., Wang, J.X.,2011. Molecular cloning and expression analysis of signal transducer and activator of transcription (STAT) from the Chinese white shrimp Fenneropenaeus chinensis. Mol Biol Rep 38,5313-5319.
    Taengchaiyaphum, S., Havanapan, P.O., Roytrakul, S., Lo, C.F., Sritunyalucksana, K., Krittanai, C., 2013. Phosphorylation is required for myosin regulatory light chain (PmMRLC) to control yellow head virus infection in shrimp hemocytes. Fish Shellfish Immunol 34,1042-1049.
    Tanaka, H., Matsuki, H., Furukawa, S., Sagisaka, A., Kotani, E., Mori, H., Yamakawa, M.,2007. Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori. Biochim Biophys Acta 1769,559-568.
    Tanji, T., Yun, E.Y., Ip, Y.T.,2010. Heterodimers of NF-kappaB transcription factors DIF and Relish regulate antimicrobial peptide genes in Drosophila. Proc Natl Acad Sci U S A 107,14715-14720.
    Tauszig-Delamasure, S., Bilak, H., Capovilla, M., Hoffmann, J.A., Imler, J.L.,2002. Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections. Nat Immunol 3,91-97.
    Tellam, R.L., Eisemann, C.H., Vuocolo, T., Casu, R., Jarrney, J., Bowles, V., Pearson, R.,2001. Role of oligosaccharides in the immune response of sheep vaccinated with Lucilia cuprina larval glycoprotein, peritrophin-95. Int J Parasitol 31,798-809.
    Tellam, R.L., Vuocolo, T., Eisemann, C., Briscoe, S., Riding, G, Elvin, C., Pearson, R.,2003. Identification of an immuno-protective mucin-like protein, peritrophin-55, from the peritrophic matrix of Lucilia cuprina larvae. Insect Biochem Mol Biol 33,239-252.
    Terahara, K., Takahashi, K.G, Nakamura, A., Osada, M., Yoda, M., Hiroi, T., Hirasawa, M., Mori, K., 2006. Differences in integrin-dependent phagocytosis among three hemocyte subpopulations of the Pacific oyster "Crassostrea gigas". Dev Comp Immunol 30,667-683.
    Tian, B., Brasier, A.R.,2003. Identification of a nuclear factor kappa B-dependent gene network. Recent Prog Horm Res 58,95-130.
    Tsai, C.W., McGraw, E.A., Ammar, E.D., Dietzgen, R.G, Hogenhout, S.A.,2008. Drosophila melanogaster mounts a unique immune response to the Rhabdovirus sigma virus. Appl Environ Microbiol 74,3251-3256.
    Tseng, I.T., Chen, J.C.,2004. The immune response of white shrimp Litopenaeus vannamei and its susceptibility to Vibrio alginolyticus under nitrite stress. Fish Shellfish Immunol 17,325-333.
    Vallet-Gely, I., Lemaitre, B., Boccard, F.,2008. Bacterial strategies to overcome insect defences. Nat Rev Microbiol 6,302-313.
    van Beuningen, H.M., de Vries-van Melle, M.L., Vitters, E.L., Schreurs, W., van den Berg, W.B., van Osch, GP., van der Kraan, P.M.,2014. Inhibition of TAK1 and/or JAK can rescue impaired chondrogenic differentiation of human mesenchymal stem cells in osteoarthritis-like conditions. Tissue Eng Part A.
    van de Braak, C.B., Botterblom, M.H., Huisman, E.A., Rombout, J.H., van der Knaap, W.P.,2002a. Preliminary study on haemocyte response to white spot syndrome virus infection in black tiger shrimp Penaeus monodon. Dis Aquat Organ 51,149-155.
    van de Braak, C.B., Botterblom, M.H., Liu, W., Taverne, N., van der Knaap, W.P., Rombout, J.H., 2002b. The role of the haematopoietic tissue in haemocyte production and maturation in the black tiger shrimp(Penaeus monodon). Fish Shellfish Immunol 12,253-272.
    Vazquez, L., Alpuche, J., Maldonado, G, Agundis, C., Pereyra-Morales, A., Zenteno, E.,2009. Review: Immunity mechanisms in crustaceans. Innate Immun 15,179-188.
    Venegas, C.A., Nonaka, L., Mushiake, K., Nishizawa, T., Murog, K.,2000. Quasi-immune response of Penaeus japonicus to penaeid rod-shaped DNA virus (PRDV). Dis Aquat Organ 42,83-89.
    Verchot, J.,2014. The ER quality control and ER associated degradation machineries are vital for viral pathogenesis. Front Plant Sci 5,66.
    Verma, P., Tapadia, M.G.,2012. Immune response and anti-microbial peptides expression in Malpighian tubules of Drosophila melanogaster is under developmental regulation. PLoS One 7, e40714.
    Vidal, S., Khush, R.S., Leulier, F., Tzou, P., Nakamura, M., Lemaitre, B.,2001. Mutations in the Drosophila dTAKl gene reveal a conserved function for MAPKKKs in the control of rel/NF-kappaB-dependent innate immune responses. Genes Dev 15,1900-1912.
    Vuocolo, T., Eisemann, C.H., Pearson, R.D., Willadsen, P., Tellam, R.L.,2001. Identification and molecular characterisation of a peritrophin gene, peritrophin-48, from the myiasis fly Chrysomya bezziana. Insect Biochem Mol Biol 31,919-932.
    Walter, P., Ron, D.,2011. The unfolded protein response:from stress pathway to homeostatic regulation. Science 334,1081-1086.
    Wang, J., Kang, R., Huang, H., Xi, X., Wang, B., Zhao, Z.,2014. Hepatitis C virus core protein activates autophagy through EIF2AK3 and ATF6 UPR pathway-mediated MAP1LC3B and ATG12 expression. Autophagy 10.
    Wang, L., Li, F., Wang, B., Xiang, J.,2012a. Structure and partial protein profiles of the peritrophic membrane (PM) from the gut of the shrimp Litopenaeus vannamei. Fish Shellfish Immunol 33, 1285-1291.
    Wang, M., Ye, R., Barron, E., Baumeister, P., Mao, C., Luo, S., Fu, Y., Luo, B., Dubeau, L., Hinton, D.R., Lee, A.S.,2010. Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis. Cell Death Differ 17,488-498.
    Wang, P., Granados, R.R.,2001. Molecular structure of the peritrophic membrane (PM):identification of potential PM target sites for insect control. Arch Insect Biochem Physiol 47,110-118.
    Wang, PH., Gu, Z.H., Huang, X.D., Liu, B.D., Deng, X.X., Ai, H.S., Wang, J., Yin, Z.X, Weng, S.P., Yu, X.Q., He, J.G,2009a. An immune deficiency homolog from the white shrimp; Litopenaeus vannamei, activates antimicrobial peptide genes. Mol Immunol 46,1897-1904.
    Wang, P.H., Gu, Z.H., Wan, D.H., Zhang, M.Y., Weng, S.P., Yu, X.Q., He, J.G,2011. The shrimp NF-kappaB pathway is activated by white spot syndrome virus (WSSV) 449 to facilitate the expression of WSSV069 (iel), WSSV303 and WSSV371. PLoS One 6, e24773.
    Wang, P.H., Liang, J.P., Gu, Z.H., Wan, D.H., Weng, S.P., Yu, X.Q., He, J.G,2012b. Molecular cloning, characterization and expression analysis of two novel Tolls (LvTol12 and LvTol13) and three putative Spatzle-like Toll ligands (LvSpzl-3) from Litopenaeus vannamei. Dev Comp Immunol 36,359-371.
    Wang, P.H., Wan, D.H., Pang, L.R., Gu, Z.H., Qiu, W., Weng, S.P., Yu, X.Q., He, J.G,2012c. Molecular cloning, characterization and expression analysis of the tumor necrosis factor (TNF) superfamily gene, TNF receptor superfamily gene and lipopolysaccharide-induced TNF-alpha factor (LITAF) gene from Litopenaeus vannamei. Dev Comp Immunol 36,39-50.
    Wang, X.W., Wang, J.X.,2013a. Diversity and multiple functions of lectins in shrimp immunity. Dev Comp Immunol 39,27-38.
    Wang, X.W., Wang, J.X.,2013b. Pattern recognition receptors acting in innate immune system of shrimp against pathogen infections. Fish Shellfish Immunol 34,981-989.
    Wang, X.W., Zhang, X.W., Xu, W.T., Zhao, X.F., Wang, J.X.,2009b. A novel C-type lectin (FcLec4) facilitates the clearance of Vibrio anguillarum in vivo in Chinese white shrimp. Dev Comp Immunol 33,1039-1047.
    Weber, A.N., Tauszig-Delamasure, S., Hoffmann, J.A., Lelievre, E., Gascan, H., Ray, K.P., Morse, M.A., Imler, J.L., Gay, N.J.,2003. Binding of the Drosophila cytokine Spatzle to Toll is direct and establishes signaling. Nat Immunol 4,794-800.
    Wen, R., Li, F., Sun, Z., Li, S., Xiang, J.,2013. Shrimp MyD88 responsive to bacteria and white spot syndrome virus. Fish Shellfish Immunol 34,574-581.
    Wijffels, G., Hughes, S., Gough, J., Allen, J., Don, A., Marshall, K., Kay, B., Kemp, D.,1999. Peritrophins of adult dipteran ectoparasites and their evaluation as vaccine antigens. Int J Parasitol 29,1363-1377.
    Wiklund, M.L., Steinert, S., Junell, A., Hultmark, D., Stoven, S.,2009. The N-terminal half of the Drosophila Rel/NF-kappaB factor Relish, REL-68, constitutively activates transcription of specific Relish target genes. Dev Comp Immunol 33,690-696.
    Williams, D.B.,2006. Beyond lectins:the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J Cell Sci 119,615-623.
    Wongprasert, K., Sangsuriya, P., Phongdara, A., Senapin, S.,2007. Cloning and characterization of a caspase gene from black tiger shrimp (Penaeus monodon)-infected with white spot syndrome virus (WSSV). J Biotechnol 131,9-19.
    Wu, C., Soderhall, K., Soderhall, I.,2011a. Two novel ficolin-like proteins act as pattern recognition receptors for invading pathogens in the freshwater crayfish Pacifastacus leniusculus. Proteomics 11,2249-2264.
    Wu, J., Ruas, J.L., Estall, J.L., Rasbach, K.A., Choi, J.H., Ye, L., Bostrom, P., Tyra, H.M., Crawford, R.W., Campbell, K.P., Rutkowski, D.T., Kaufman, R.J., Spiegelman, B.M.,2011b. The unfolded protein response mediates adaptation to exercise in skeletal muscle through a PGC-lalpha/ATF6alpha complex. Cell Metab 13,160-169.
    Wu, W., Zong, R., Xu, J., Zhang, X.,2008. Antiviral phagocytosis is regulated by a novel Rab-dependent complex in shrimp penaeus japonicus. J Proteome Res 7,424-431.
    Xi, Z., Ramirez, J.L., Dimopoulos, G,2008. The Aedes aegypti toll pathway controls dengue virus infection. PLoS Pathog 4, e1000098.
    Xian, J.A., Guo, H., Li, B., Miao, Y.T., Ye, J.M., Zhang, S.P., Pan, X.B., Ye, C.X., Wang, A.L., Hao, X.M.,2013. Measurement of intracellular nitric oxide (NO) production in shrimp haemocytes by flow cytometry. Fish Shellfish Immunol.
    Xie, Y, Li, F., Wang, B., Li, S., Wang, D., Jiang, H., Zhang, C, Yu, K., Xiang, J.,2010. Screening of genes related to ovary development in Chinese shrimp Fenneropenaeus chinensis by suppression subtractive hybridization. Comp Biochem Physiol Part D Genomics Proteomics 5,98-104.
    Xu, J., Han, F., Zhang, X.,2007. Silencing shrimp white spot syndrome virus (WSSV) genes by siRNA. Antiviral Res 73,126-131.
    Xu, S., Wang, L., Wang, X.W., Zhao, Y.R., Bi, W.J., Zhao, X.F., Wang, J.X.,2014.1-Type lectin from the kuruma shrimp Marsupenaeus japonicus promotes hemocyte phagocytosis. Dev Comp Immunol.
    Xu, T., Liu, W., Luo, J., Li, C., Ba, X., Ampah, K.K., Wang, X., Jiang, Y, Zeng, X.,2013. Lipid Raft is required for PSGL-1 ligation induced HL-60 cell adhesion on ICAM-1. PLoS One 8, e81807.
    Yang, C., Zhang, J., Li, F., Ma, H., Zhang, Q., Jose Priya, T.A., Zhang, X., Xiang, J.,2008. A Toll receptor from Chinese shrimp Fenneropenaeus chinensis is responsive to Vibrio anguillarum infection. Fish Shellfish Immunol 24,564-574.
    Yang, L.S., Yin, Z.X., Liao, J.X., Huang, X.D., Guo, C.J., Weng, S.P., Chan, S.M., Yu, X.Q., He, J.G., 2007. A Toll receptor in shrimp. Mol Immunol 44,1999-2008.
    Yeh, S.T., Li, C.C., Tsui, W.C., Lin, Y.C., Chen, J.C.,2010. The protective immunity of white shrimp Litopenaeus vannamei that had been immersed in the hot-water extract of Gracilaria tenuistipitata and subjected to combined stresses of Vibrio alginolyticus injection and temperature change. Fish Shellfish Immunol 29,271-278.
    Yerushalmi, L., Lascourreges, J.F., Rhofir, C., Guiot, S.R.,2001a. Detection of intermediate metabolites of benzene biodegradation under microaerophilic conditions. Biodegradation 12, 379-391.
    Yerushalmi, N., Keppler-Hafkemeyer, A., Vasmatzis, G., Liu, X.F., Olsson, P., Bera, T.K., Duray, P., Lee, B., Pastan, I.,2001b. ERGL, a novel gene related to ERGIC-53 that is highly expressed in normal and neoplastic prostate and several other tissues. Gene 265,55-60.
    Yoshida, H., Kinoshita, K., Ashida, M.,1996. Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori. J Biol Chem 271,13854-13860.
    Yu, C., Achazi, K., Niedrig, M.,2013. Tick-bome encephalitis virus triggers inositol-requiring enzyme 1 (IRE1) and transcription factor 6 (ATF6) pathways of unfolded protein response. Virus Res 178, 471-477.
    Yu, X.Q., Gan, H., Kanost, M.R.,1999. Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase. Insect Biochem Mol Biol 29, 585-597.
    Zambon, R.A., Nandakumar, M., Vakharia, V.N., Wu, L.P.,2005. The Toll pathway is important for an antiviral response in Drosophila. Proc Natl Acad Sci U S A 102,7257-7262.
    Zhang, H., Peatman, E., Liu, H., Feng, T., Chen, L., Liu, Z.,2012a. Molecular characterization of three L-type lectin genes from channel catfish, Ictalurus punctatus and their responses to Edwardsiella ictaluri challenge. Fish Shellfish Immunol 32,598-608.
    Zhang, S., Li, C.Z., Yan, H., Qiu, W., Chen, Y.G., Wang, P.H., Weng, S.P., He, J.G,2012b. Identification and function of myeloid differentiation factor 88 (MyD88) in Litopenaeus vannamei. PLoS One 7, e47038.
    Zhang, X.W., Xu, W.T., Wang, X.W., Mu, Y, Zhao, X.F., Yu, X.Q., Wang, J.X.,2009. A novel C-type lectin with two CRD domains from Chinese shrimp Fenneropenaeus chinensis functions as a pattern recognition protein. Mol Immunol 46,1626-1637.
    Zhang, Z., Zhan, W., Xue, Y, Xing, J.,2004. Antigenic cross-reactivity of crustacean haemocytes using monoclonal antibodies produced against haemocytes of shrimp(Litopenaeus yannamei). Fish Shellfish Immunol 16,71-73.
    Zhou, R., Silverman, N., Hong, M., Liao, D.S., Chung, Y, Chen, Z.J., Maniatis, T.,2005. The role of ubiquitination in Drosophila innate immunity. J Biol Chem 280,34048-34055.
    Zong, R., Wu, W., Xu, J., Zhang, X.,2008. Regulation of phagocytosis against bacterium by Rab GTPase in shrimp Marsupenaeus japonicus. Fish Shellfish Immunol 25,258-263.

© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号

地址:北京市海淀区学院路29号 邮编:100083

电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700