对虾抗病毒相关蛋白的分子克隆与功能研究
详细信息    本馆镜像全文|  推荐本文 |  |   获取CNKI官网全文
摘要
对虾的养殖是我国沿海地区重要的水产支柱产业。但是白斑病毒(white spot syndrome virus, WSSV)等病毒使对虾养殖业遭受了极大的损失。因此,研究对虾的抗病毒先天免疫防御机制,对于预防和控制对虾疾病具有重要意义。1.对虾TRBP和eIF6之间存在直接的相互作用,并在对虾抗病毒RNAi途径中起作用
     HIV转录激活反应RNA结合蛋白(Trans-activation response RNA-binding protein, TRBP)是一种多功能蛋白,在多种生命进程中发挥重要作用。我们从中国明对虾(Fenneropenaeus chinensis)中克隆得到三个TRBP家族成员,分别命名为Fc-TRBP1-3.我们在大肠杆菌Escherichia coli中重组表达并纯化了Fc-TRBP1,随后使用纯化的Fc-TRBP1进行对虾血细胞T7噬菌体展示文库淘选,并得到中国明对虾真核翻译起始因子(Fc-eukaryotic initiation factor 6, Fc-eIF6)的部分序列。我们克隆得到Fc-eIF6的全长cDNA序列,并在大肠杆菌中进行重组表达。利用pull down实验验证了TRBP和eIF6之间存在直接的相互作用。RT-PCR和Northern blot结果表明Fc-TRBP和Fc-eIF6在所有检测的组织中都有表达,对虾受鳗弧菌刺激后在所有组织中表达有上调趋势,在对虾受到病毒刺激时TRBP和eIF6的表达模式在不同组织中有较大差异,在血细胞中呈现下调趋势而在鳃和肠中上调。Western blot结果验证了TRBP在肝胰腺和鳃中的表达模式。注射重组TRBP蛋白可抑制WSSV在对虾体内的复制。通过这些结果可以推测TRBP和eIF6可能在抗病毒免疫中起重要作用。
     随后我们在日本囊对虾(Marsupenaeus japonicus)中克隆得到TRBP和eIF6的全长序列。我们对日本囊对虾TRBP(Mj-TRBP)的不同结构域进行重组表达。pulldown实验证明TRBP结构域B,C介导与eIF6的结合。Gel-shift结果表明TRBP结构域A对dsRNA具有很高的亲和力,而结构域B亲和力很弱,结构域C不结合dsRNA但可通过介导TRBP全长分子的二聚化提高TRBP分子的亲和力。RNAi结果表明TRBP和eIF6参与dsRNA介导的RNA沉默,沉默TRBP和eIF6均可促进WSSV的增殖。以上结果表明,TRBP和eIF6可能通过抗病毒RNA沉默参与对虾抗病毒免疫。
     2.组织蛋白酶C参与对虾的抗病毒先天免疫
     组织蛋白酶C, (Cathepsin C, Cath C)是一种溶酶体半胱氨酸蛋白酶,属于木瓜蛋白酶家族。Cath C能够激活许多糜蛋白酶样的丝氨酸蛋白酶(chymotrypsin-like serine proteases)并在免疫和炎症细胞中参与调控许多丝氨酸蛋白酶的活性。在本研究中,我们克隆了中国明对虾Cath C的cDNA全长序列,命名为Fc-Cath C。Fc-Cath C的cDNA长1445bp,包含1356的bp开放读码框(open reading frame, ORF)编码了451氨基酸长度的蛋白包括17个氨基酸的信号肽。Real time PCR结果表明Fc-Cath C mRNA在肝胰腺中转录,并在受鳗弧菌Vibrioanguillarum和白斑病毒(white spot syndrome virus, WSSV)刺激后上调。通过向对虾体内注射Cath C的抗体后,可促进WSSV的增殖以及提高对虾受病毒感染后的死亡率。我们的结果表明Fc-Cath C可能在对虾的抗病毒先天免疫中起重要的作用。
     3.翻译控制肿瘤蛋白的基因克隆及功能研究
     翻译控制肿瘤蛋白(translationally controlled tumor protein, TCTP)是一种多功能的蛋白,在许多生命过程中发挥重要的功能。我们从中国明对虾中克隆得到TCTP的cDNA全长序列命名为Fc-TCTP。Fc-TCTP cDNA长711bp,包含507 bp的开放读码框(open reading frame, ORF)编码了168氨基酸,包含一个TCTP结构域的蛋白。我们Fc-TCTP受到鳗弧菌刺激和WSSV刺激后的表达模式进行分析发现,在受到WSSV刺激后TCTP的mRNA和蛋白水平上的表达量显著上调。结果表明Fc-TCTP可能在对虾的抗病毒先天免疫中起重要的作用。
The Chinese white shrimp (Fenneropenaeus chinensis) cultivation is an important economic activity in China. However, the aquaculture of shrimp has suffered vast economic losses because of serious viral diseases such as white spot syndrome virus (WSSV). So investigating the mechanism of antiviral immunity will help us to control those viral diseases.
     1. Fc-TRBP interacts with Fc-eIF6 directly, and both are involved in the antiviral RNA interference
     The Trans-activation response RNA-binding protein (TRBP) plays an important role in many biological processes. In these studies, three new cDNAs of the TRBP family were cloned from Fenneropenaeus chinensis, and designated Fc-TRBP 1-3. Recombinant expressed Fc-TRBPl in Escherichia coli was used for panning of a T7 phage display library constructed using Chinese shrimp hepatopancreas. From this panning, eukaryotic initiation factor 6 (eIF6) was isolated and sequenced. After cloning and recombinantly expressing Fenneropenaeus chinensis-derived Fc-eIF6, the interaction between Fc-TRBP and Fc-eIF6 was confirmed using pull-down assays and far western analysis. Expression of Fc-TRBPs was detected in many tissues, with its expression level increasing in heart, gill and intestine in the early stages of infection by the white spot syndrome virus (WSSV), and increasing in most tissues following a challenge with Vibrio anguillarum. Western blot studies confirmed the increased expression of Fc-TRBP in gill after WSSV infection. The expression pattern of eIF6 was also analyzed. Infection analysis show the replication of WSSV was reduced after injection with Fc-TRBP.
     Then we show that the double strand RNA bind domain (dsRBD) B and C of TRBP homologue from Marsupenaeus japonicus (Mj-TRBP) mediated the interaction of TRBP and eIF6. Gel-shift assays reveal the N-terminal dsRBD of Mj-TRBP binds to double strand RNA (dsRNA) with a high affinity, while TRBP might be homo-dimerized by the C-terminal region and increase the affinity to dsRNA. RNAi against either Mj-TRBP or Mj-eIF6 impairs the dsRNA induced sequence-specific RNAi pathway and facilitates the proliferation of WSSV. These results indicate that TRBP and eIF6 may be components of the RNA-induced silencing complex (RISC), and thereby play a crucial role in the anti-viral defense response of shrimp.
     2. Cathepsin C is involved in the innate antiviral immunity.
     Cathepsin C (Cath C) is a lysosomal cysteine protease that belongs to the papain superfamily. Cath C is capable of activating many chymotrypsin-like serine proteases and is reported to be a central coordinator for the activation of many serine proteinases in immune and inflammatory cells. In this study, Cath C cDNA was cloned from Fenneropenaeus chinensis (Fc). The complete cDNA of Fc-Cath C in Chinese white shrimp was found to be 1445-base pairs (bp) long. It contained an open reading frame (ORF) 1356-bp long and encoded a 451-amino acid residue protein, including a 17-amino acid residue signal peptide. Real-time PCR analysis results indicated that Fc-Cath C mRNA was transcribed in the hepatopancreas and upregulated after stimulation by the Vibrio anguillarum and the white spot syndrome viruses (WSSVs). Replication of the WSSV increased after the injection of Fc-Cath C antiserum. These results imply that Fc-Cath C might play an important role in the antiviral immune response of shrimp.
     3. Molecular cloning and function analysis of TCTP
     The translationally controlled tumor protein (TCTP) is a multi-functioning protein that performs vital roles, particularly in various complicated life processes. In this study, a new TCTP cDNA was cloned from Fenneropenaeus chinensis and hence was designated as Fc-TCTP. Its length is 711 bp, and it is characterized by 507-bp open reading frame (ORF) that encodes a deduced 168-amino acid protein, including a TCTP domain. Moreover, this study analyzed the expression patterns of this gene when it responds to infection specifically with Vibrio anguillarum and the white spot syndrome virus (WSSV). Based on the results, Fc-TCTP was present in all the analyzed tissues. Additionally, Fc-TCTP's expression level decreased after having been infected by bacteria, but was upregulated in the hepatopancreas after having been exposed to WSSV. Likewise, the Fc-TCTP protein was upregulated during its exposure to the virus. These results suggest that Fc-TCTP could well be involved in the antiviral response in F. chinensis.
引文
Akk, A. M., Simmons, P. M., Chan, H. W., Agapov, E., Holtzman, M. J., Grayson, M. H. and Pham, C. T. (2008). Dipeptidyl peptidase I-dependent neutrophil recruitment modulates the inflammatory response to Sendai virus infection. J Immunol 180,3535-42.
    Aliyari, R., Wu, Q., Li, H. W., Wang, X. H., Li, F., Green, L. D., Han, C. S., Li, W. X. and Ding, S. W. (2008). Mechanism of induction and suppression of antiviral immunity directed by virus-derived small RNAs in Drosophila. Cell Host Microbe 4,387-97.
    Andersson, M. G., Haasnoot, P. C., Xu, N., Berenjian, S., Berkhout, B. and Akusjarvi, G. (2005). Suppression of RNA interference by adenovirus virus-associated RNA. J Virol 79,9556-65.
    Bangrak, P., Graidist, P., Chotigeat, W. and Phongdara, A. (2004). Molecular cloning and expression of a mammalian homologue of a translationally controlled tumor protein (TCTP) gene from Penaeus monodon shrimp. JBiotechnol 108,219-26.
    Bannwarth, S., Talakoub, L., Letourneur, F., Duarte, M., Purcell, D. F., Hiscott, J. and Gatignol, A. (2001). Organization of the human tarbp2 gene reveals two promoters that are repressed in an astrocytic cell line. JBiol Chem 276,48803-13.
    Bartel, D. P. (2004). MicroRNAs:genomics, biogenesis, mechanism, and function. Cell 116,281-97. Baulcombe, D. (2004). RNA silencing in plants. Nature 431,356-63.
    Benkirane, M., Neuveut, C., Chun, R. F., Smith, S. M., Samuel, C. E., Gatignol, A. and Jeang, K. T. (1997). Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. Embo J 16,611-24.
    Bennasser, Y., Le, S. Y., Benkirane, M. and Jeang, K. T. (2005). Evidence that HIV-1 encodes an siRNA and a suppressor of RNA silencing. Immunity 22,607-19.
    Bennasser, Y., Yeung, M. L. and Jeang, K. T. (2006). HIV-1 TAR RNA subverts RNA interference in transfected cells through sequestration of TAR RNA-binding protein, TRBP. J Biol Chem 281, 27674-8.
    Benndorf, R., Nurnberg, P. and Bielka, H. (1988). Growth phase-dependent proteins of the Ehrlich ascites tumor analyzed by one- and two-dimensional electrophoresis. Exp Cell Res 174,130-8.
    Bentwich, I. (2005). Prediction and validation of microRNAs and their targets. FEBS Lett 579, 5904-10.
    Bentwich, I., Avniel, A., Karov, Y., Aharonov, R., Gilad, S., Barad, O., Barzilai, A., Einat, P., Einav, U., Meiri, E. et al. (2005). Identification of hundreds of conserved and nonconserved human microRNAs. Nat Genet 37,766-70.
    Bernstein, E., Caudy, A. A., Hammond, S. M. and Hannon, G J. (2001). Role for a bidentate ribonuclease in the initiation step of RNA interference. Nature 409,363-6.
    Bheekha-Escura, R., MacGlashan, D. W., Langdon, J. M. and MacDonald, S. M. (2000). Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line, AML14-3D10. Blood 96,2191-8.
    Bini, L., Heid, H., Liberatori, S., Geier, G, Pallini, V. and Zwilling, R. (1997). Two-dimensional gel electrophoresis of Caenorhabditis clegans homogenates and identification of protein spots by microsequencing. Electrophoresis 18,557-62.
    Bohm, H., Benndorf, R., Gaestel, M., Gross, B., Nurnberg, P., Kraft, R., Otto, A. and Bielka, H. (1989). The growth-related protein P23 of the Ehrlich ascites tumor:translational control, cloning and primary structure. Biochem Int 19,277-86.
    Bommer, U. A., Borovjagin, A. V., Greagg, M. A., Jeffrey, I. W., Russell, P., Laing, K. G., Lee, M. and Clemens, M. J. (2002). The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKR. RNA 8,478-96.
    Bommer, U. A., Lazaris-Karatzas, A., De Benedetti, A., Nurnberg, P., Benndorf, R., Bielka, H. and Sonenberg, N. (1994). Translational regulation of the mammalian growth-related protein P23: involvement of eIF-4E. Cell Mol Biol Res 40,633-41.
    Bondebjerg, J., Fuglsang, H., Valeur, K. R., Kaznelson, D. W., Hansen, J. A., Pedersen, R. O., Krogh, B. O., Jensen, B. S., Lauritzen, C., Petersen, G et al. (2005). Novel semicarbazide-derived inhibitors of human dipeptidyl peptidase I (hDPPI). Bioorg Med Chem 13,4408-24.
    Brodersen, P. and Voinnet, O. (2006). The diversity of RNA silencing pathways in plants. Trends Genet 22,268-80.
    Brown, G R., McGuire, M. J. and Thiele, D. L. (1993). Dipeptidyl peptidase I is enriched in granules of in vitro-and in vivo-activated cytotoxic T lymphocytes. J Immunol 150,4733-42.
    Bruce, C. and Taylor, W. H. (1996). Plasma histamine in patients with tropical disorders and acute asthma who exhibit eosinophilia. Ann Clin Biochem 33 (Pt 3),249-52.
    Brummelkamp, T. R., Bernards, R. and Agami, R. (2002). A system for stable expression of short interfering RNAs in mammalian cells. Science 296,550-3.
    Bucher, E., Hemmes, H., de Haan, P., Goldbach, R. and Prins, M. (2004). The influenza A virus NS1 protein binds small interfering RNAs and suppresses RNA silencing in plants. J Gen Virol 85, 983-91.
    Cans, C., Passer, B. J., Shalak, V., Nancy-Portebois, V., Crible, V., Amzallag, N., Allanic, D., Tufino, R., Argentini, M., Moras, D. et al. (2003). Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A. Proc Natl Acad Sci USA 100,13892-7.
    Capodici, J., Kariko, K. and Weissman, D. (2002). Inhibition of HIV-1 infection by small interfering RNA-mediated RNA interference. J Immunol 169,5196-201.
    Carmell, M. A., Xuan, Z., Zhang, M. Q. and Hannon, G J. (2002). The Argonaute family:tentacles that reach into RNAi, developmental control, stem cell maintenance, and tumorigenesis. Genes Dev 16, 2733-42.
    Ceci, M., Gaviraghi, C., Gorrini, C., Sala, L. A., Offenhauser, N., Marchisio, P. C. and Biffo, S. (2003). Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly. Nature 426, 579-84.
    Chang, K. Y. and Ramos, A. (2005). The double-stranded RNA-binding motif, a versatile macromolecular docking platform. FEBS J 272,2109-17.
    Chendrimada, T. P., Finn, K. J., Ji, X., Baillat, D., Gregory, R. I., Liebhaber, S. A., Pasquinelli, A. E. and Shiekhattar, R. (2007). MicroRNA silencing through RISC recruitment of eIF6. Nature 447, 823-8.
    Chendrimada, T. P., Gregory, R. I., Kumaraswamy, E., Norman, J., Cooch, N., Nishikura, K. and Shiekhattar, R. (2005). TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing. Nature 436,740-4.
    Chien, C. Y., Tejero, R., Huang, Y., Zimmerman, D. E., Rios, C. B., Krug, R. M. and Montelione, G. T. (1997). A novel RNA-binding motif in influenza A virus non-structural protein 1. Nat Struct Biol 4,891-5.
    Chitpatima, S. T., Makrides, S., Bandyopadhyay, R. and Brawerman, G (1988). Nucleotide sequence of a major messenger RNA for a 21 kilodalton polypeptide that is under translational control in mouse tumor cells. Nucleic Acids Res 16,2350.
    Christodoulopoulos, P., Cameron, L., Durham, S. and Hamid, Q. (2000). Molecular pathology of allergic disease. Ⅱ:Upper airway disease. JAllergy Clin Immunol 105,211-23.
    Chung, K. F. and Adcock, I. M. (2001). Pathophysiological mechanisms of asthma. Application of cell and molecular biology techniques. Mol Biotechnol 18,213-32.
    Collins, R. E. and Cheng, X. (2005). Structural domains in RNAi. FEBSLett 579,5841-9.
    Corbeau, P. (2008). Interfering RNA and HIV:reciprocal interferences. PLoS Pathog 4, e1000162.
    Cosentino, G. P., Venkatesan, S., Serluca, F. C., Green, S. R., Mathews, M. B. and Sonenberg, N. (1995). Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo-and heterodimers in vivo. Proc Natl Acad Sci USA 92,9445-9.
    D'Agrosa, R. M. and Callahan, J. W. (1988). In vitro activation of neuraminidase in the beta-galactosidase-neuraminidase-protective protein complex by cathepsin C. Biochem Biophys Res Commun 157,770-5.
    Daher, A., Laraki, G, Singh, M., Melendez-Pena, C. E., Bannwarth, S., Peters, A. H., Meurs, E. F., Braun, R. E., Patel, R. C. and Gatignol, A. (2009). TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress. Mol Cell Biol 29,254-65.
    Daher, A., Longuet, M., Dorin, D., Bois, F., Segeral, E., Bannwarth, S., Battisti, P. L., Pureell, D. F., Benarous, R., Vaquero, C. et al. (2001). Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression. J Biol Chem 276,33899-905.
    Daniels, S. M., Melendez-Pena, C. E., Scarborough, R. J., Daher, A., Christensen, H. S., El Far, M., Purcell, D. F., Laine, S. and Gatignol, A. (2009). Characterization of the TRBP domain required for dicer interaction and function in RNA interference. BMC Mol Biol 10,38.
    Das, A. T., Brummelkamp, T. R., Westerhout, E. M., Vink, M., Madiredjo, M., Bernards, R. and Berkhout, B. (2004). Human immunodeficiency virus type 1 escapes from RNA interference-mediated inhibition. J Virol 78,2601-5.
    Daviet, L., Erard, M., Dorin, D., Duarte, M., Vaquero, C. and Gatignol, A. (2000). Analysis of a binding difference between the two dsRNA-binding domains in TRBP reveals the modular function of a KR-helix motif. EurJ Biochem 267,2419-31.
    Denli, A. M., Tops, B. B., Plasterk, R. H., Ketting, R. F. and Hannon, G J. (2004). Processing of primary microRNAs by the Microprocessor complex. Nature 432,231-5.
    Dhar, A. K., Roux, M. M. and Klimpel, K. R. (2001). Detection and quantification of infectious hypodermal and hematopoietic necrosis virus and white spot virus in shrimp using real-time quantitative PCR and SYBR Green chemistry. J Clin Microbiol 39,2835-45.
    Ding, S. W. and Voinnet, O. (2007). Antiviral immunity directed by small RNAs. Cell 130,413-26.
    Dorin, D., Bonnet, M. C., Bannwarth, S., Gatignol, A., Meurs, E. F. and Vaquero, C. (2003). The TAR RNA-binding protein, TRBP, stimulates the expression of TAR-containing RNAs in vitro and in vivo independently of its ability to inhibit the dsRNA-dependent kinase PKR. J Biol Chem 278, 4440-8.
    Doughty, M. J. and Gruenstein, E. I. (1987). Cell growth and substrate effects on characteristics of a lysosomal enzyme (cathepsin C) in Duchenne muscular dystrophy fibroblasts. Biochem Cell Biol 65, 617-25.
    Duarte, M., Graham, K., Daher, A., Battisti, P. L., Bannwarth, S., Segeral, E., Jeang, K. T. and Gatignol, A. (2000). Characterization of TRBP1 and TRBP2. Stable stem-loop structure at the 5'end of TRBP2 mRNA resembles HIV-1 TAR and.is not found in its processed pseudogene. J Biomed Sci 7, 494-506.
    Dunoyer, P. and Voinnet, O. (2005). The complex interplay between plant viruses and host RNA-silencing pathways. Curr Opin Plant Biol 8,415-23.
    Eamens, A. L., Smith, N. A., Curtin, S. J., Wang, M. B. and Waterhouse, P. M. (2009). The Arabidopsis thaliana double-stranded RNA binding protein DRB 1 directs guide strand selection from microRN A duplexes. RNA 15,2219-35.
    Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K. and Tuschl, T. (2001). Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411,494-8.
    Enwonwu, C. O., Afolabi, B. M., Salako, L. O., Idigbe, E. O. and Bashirelah, N. (2000). Increased plasma levels of histidine and histamine in falciparum malaria:relevance to severity of infection. J Neural Transm 107,1273-87.
    Erard, M., Barker, D. G, Amalric, F., Jeang, K. T. and Gatignol, A. (1998). An Arg/Lys-rich core peptide mimics TRBP binding to the HIV-1 TAR RNA upper-stem/loop. J Mol Biol 279,1085-99.
    Filipowicz, W. (2005). RNAi:the nuts and bolts of the RISC machine. Cell 122,17-20.
    Filipowicz, W., Jaskiewicz, L., Kolb, F. A. and Pillai, R. S. (2005). Post-transcriptional gene silencing by siRNAs and miRNAs. Curr Opin Struct Biol 15,331-41.
    Fire, A., Xu, S., Montgomery, M. K., Kostas, S. A., Driver, S. E. and Mello, C. C. (1998). Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 391, 806-11.
    Forstemann, K., Tomari, Y., Du, T., Vagin, V. V., Denli, A. M., Bratu, D. P., Klattenhoff, C., Theurkauf, W. E. and Zamore, P. D. (2005). Normal microRNA maturation and germ-line stem cell maintenance requires Loquacious, a double-stranded RNA-binding domain protein. PLoS Biol 3, e236.
    Gachet, Y., Tournier, S., Lee, M., Lazaris-Karatzas, A., Poulton, T. and Bommer, U. A. (1999). The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle. J Cell Sci 112 (Pt 8),1257-71.
    Galiana-Arnoux, D., Dostert, C., Schneemann, A., Hoffmann, J. A. and Imler, J. L. (2006). Essential function in vivo for Dicer-2 in host defense against RNA viruses in drosophila. Nat Immunol 7,590-7.
    Garcia-Sastre, A. (2002). Mechanisms of inhibition of the host interferon alpha/beta-mediated antiviral responses by viruses. Microbes Infect 4,647-55.
    Gatignol, A., Buckler-White, A., Berkhout, B. and Jeang, K. T. (1991). Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR. Science 251,1597-600.
    Gatignol, A., Buckler, C. and Jeang, K. T. (1993). Relatedness of an RNA-binding motif in human immunodeficiency virus type 1 TAR RNA-binding protein TRBP to human Pl/dsI kinase and Drosophila staufen. Mol Cell Biol 13,2193-202.
    Gatignol, A., Laine, S. and Clerzius, G. (2005). Dual role of TRBP in HIV replication and RNA interference:viral diversion of a cellular pathway or evasion from antiviral immunity? Retrovirology 2, 65.
    Gitlin, L., Stone, J. K. and Andino, R. (2005). Poliovirus escape from RNA interference:short interfering RNA-target recognition and implications for therapeutic approaches. J Virol 79,1027-35.
    Gnanasekar, M., Rao, K. V., Chen, L., Narayanan, R. B., Geetha, M., Scott, A. L., Ramaswamy, K. and Kaliraj, P. (2002). Molecular characterization of a calcium binding translationally controlled
    tumor protein homologue from the filarial parasites Brugia malayi and Wuchereria bancrofti. Mol Biochem Parasitol 121,107-18.
    Grebenjuk, V. A., Kuusksalu, A., Kelve, M., Schutze, J., Schroder, H. C. and Muller, W. E. (2002). Induction of (2'-5')oligoadenylate synthetase in the marine sponges Suberites domuncula and Geodia cydonium by the bacterial endotoxin lipopolysaccharide. Eur J Biochem 269,1382-92.
    Gregory, R. I., Chendrimada, T. P., Cooch, N. and Shiekhattar, R. (2005). Human RISC couples microRNA biogenesis and posttranscriptional gene silencing. Cell 123,631-40.
    Gregory, R. I., Yan, K. P., Amuthan, G., Chendrimada, T., Doratotaj, B., Cooch, N. and Shiekhattar, R. (2004). The Microprocessor complex mediates the genesis of microRNAs. Nature 432, 235-40.
    Grishok, A. (2005). RNAi mechanisms in Caenorhabditis elegans. FEBS Lett 579,5932-9.
    Gross, B., Gaestel, M., Bohm, H. and Bielka, H. (1989). cDNA sequence coding for a translationally controlled human tumor protein. Nucleic Acids Res 17,8367.
    Gross, P. S., Bartlett, T. C., Browdy, C. L., Chapman, R. W. and Warr, G. W. (2001). Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp, L. setiferus. Dev Comp Immunol 25, 565-77.
    Guo, S. and Kemphues, K. J. (1995). par-1, a gene required for establishing polarity in C. elegans embryos, encodes a putative Ser/Thr kinase that is asymmetrically distributed. Cell 81,611-20.
    Gupta, V., Huang, X. and Patel, R. C. (2003). The carboxy-terminal, M3 motifs of PACT and TRBP have opposite effects on PKR activity. Virology 315,283-91.
    Haase, A. D., Jaskiewicz, L., Zhang, H., Laine, S., Sack, R., Gatignol, A. and Filipowicz, W. (2005). TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing. EMBO Rep 6,961-7.
    Hamilton, A. J. and Baulcombe, D. C. (1999). A species of small antisense RNA in posttranscriptional gene silencing in plants. Science 286,950-2.
    Hammond, S. M. (2005). Dicing and slicing:the core machinery of the RNA interference pathway. FEBS Lett 579,5822-9.
    Hammond, S. M., Caudy, A. A. and Hannon, G. J. (2001). Post-transcriptional gene silencing by double-stranded RNA. Nat Rev Genet 2,110-9.
    Han, J., Lee, Y., Yeom, K. H., Kim, Y. K., Jin, H. and Kim, V. N. (2004). The Drosha-DGCR8 complex in primary microRNA processing. Genes Dev 18,3016-27.
    Hannon, G. J. and Rossi, J. J. (2004). Unlocking the potential of the human genome with RNA interference. Nature 431,371-8.
    He, L. and Hannon, G. J. (2004). MicroRNAs:small RNAs with a big role in gene regulation. Nat Rev Genet 5,522-31.
    He, N., Qin, Q. and Xu, X. (2005). Differential profile of genes expressed in hemocytes of White Spot Syndrome Virus-resistant shrimp (Penaeus japonicus) by combining suppression subtractive hybridization and differential hybridization. Antiviral Res 66,39-45.
    Hitti, E. G, Sallacz, N. B., Schoft, V. K. and Jantsch, M. F. (2004). Oligomerization activity of a double-stranded RNA-binding domain. FEBS Lett 574,25-30.
    Hoa, N. T., Keene, K. M., Olson, K. E. and Zheng, L. (2003). Characterization of RNA interference in an Anopheles gambiae cell line. Insect Biochem Mol Biol 33,949-57.
    Hudig, D., Allison, N. J., Pickett, T. M., Winkler, U., Kam, C. M. and Powers, J. C. (1991). The function of lymphocyte proteases. Inhibition and restoration of granule-mediated lysis with isocoumarin serine protease inhibitors.,J Immunol 147,1360-8.
    Hunter, C. P. (1999). Genetics:a touch of elegance with RNAi. Curr Biol 9, R440-2.
    Ishidoh, K., Muno, D., Sato, N. and Kominami, E. (1991). Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a cysteine proteinase with an extremely long propeptide. J Biol Chem 266, 16312-7.
    Jacobs, B. L. and Langland, J. O. (1996). When two strands are better than one:the mediators and modulators of the cellular responses to double-stranded RNA. Virology 219,339-49.
    Jung, J., Kim, M., Kim, M. J., Kim, J., Moon, J., Lim, J. S. and Lee, K. (2004). Translationally controlled tumor protein interacts with the third cytoplasmic domain of Na,K-ATPase alpha subunit and inhibits the pump activity in HeLa cells. J Biol Chem 279,49868-75.
    Kang, H. S., Lee, M. J., Song, H., Han, S. H., Kim, Y. M., Im, J. Y. and Choi, I. (2001). Molecular identification of IgE-dependent histamine-releasing factor as a B cell growth factor. J Immunol 166, 6545-54.
    Keene, K. M., Foy, B. D., Sanchez-Vargas, I., Beaty, B. J., Blair, C. D. and Olson, K. E. (2004). RNA interference acts as a natural antiviral response to O'nyong-nyong virus (Alphavirus; Togaviridae) infection of Anopheles gambiae. Proc Natl Acad Sci USA 101,17240-5.
    Kim, D. H., Villeneuve, L. M., Morris, K. V. and Rossi, J. J. (2006). Argonaute-1 directs siRNA-mediated transcriptional gene silencing in human cells. Nat Struct Mol Biol 13,793-7.
    Kim, M., Jung, Y., Lee, K. and Kim, C. (2000). Identification of the calcium binding sites in translationally controlled tumor protein. Arch Pharm Res 23,633-6.
    Kominami, E., Ishido, K., Muno, D. and Sato, N. (1992). The primary structure and tissue distribution of cathepsin C. Biol Chem Hoppe Seyler 373,367-73.
    Laraki, G., Clerzius, G., Daher, A., Melendez-Pena, C., Daniels, S. and Gatignol, A. (2008). Interactions between the double-stranded RNA-binding proteins TRBP and PACT define the Medipal domain that mediates protein-protein interactions. RNA Biol 5,92-103.
    Le Page, C., Genin, P., Baines, M. G., and Hiscott, J. (2000). Interferon activation and innate immunity. Rev Immunogenet 2,374-86.
    Lecellier, C. H., Dunoyer, P., Arar, K., Lehmann-Che, J., Eyquem, S., Himber, C., Saib, A. and Voinnet, O. (2005). A cellular microRNA mediates antiviral defense in human cells. Science 308, 557-60.
    Lee, J. Y., Kim, H., Ryu, C. H., Kim, J. Y., Choi, B. H., Lim, Y., Huh, P. W., Kim, Y. H., Lee, K. H., Jun, T. Y. et al. (2004). Merlin, a tumor suppressor, interacts with transactivation-responsive RNA-binding protein and inhibits its oncogenic activity. J Biol Chem 279,30265-73.
    Lee, Y., Hur, I., Park, S. Y., Kim, Y. K., Suh, M. R. and Kim, V. N. (2006). The role of PACT in the RNA silencing pathway. Embo J 25,522-32.
    Li, H., Li, W. X. and Ding, S. W. (2002). Induction and suppression of RNA silencing by an animal virus. Science 296,1319-21.
    Li, H. W. and Ding, S. W. (2005). Antiviral silencing in animals. FEBS Lett 579,5965-73.
    Li, W. X., Li, H., Lu, R., Li, F., Dus, M., Atkinson, P., Brydon, E. W., Johnson, K. L., Garcia-Sastre, A., Ball, L. A. et al. (2004). Interferon antagonist proteins of influenza and vaccinia viruses are suppressors of RNA silencing. Proc Natl Acad Sci U S A 101,1350-5.
    Lichner, Z., Silhavy, D. and Burgyan, J. (2003). Double-stranded RNA-binding proteins could suppress RNA interference-mediated antiviral defences. J Gen Virol 84,975-80.
    Liu, H., Jiravanichpaisal, P., Soderhall, I., Cerenius, L. and Soderhall, K. (2006). Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus. J Virol 80,10365-71.
    Liu, H., Peng, H. W., Cheng, Y. S., Yuan, H. S. and Yang-Yen, H. F. (2005a). Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP. Mol Cell Biol 25,3117-26.
    Liu, J., Lynch, P. A., Chien, C. Y., Montelione, G. T., Krug, R. M. and Berman, H. M. (1997). Crystal structure of the unique RNA-binding domain of the influenza virus NS1 protein. Nat Struct Biol 4,896-9.
    Liu, J., Valencia-Sanchez, M. A., Hannon, G J. and Parker, R. (2005b). MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies. Nat Cell Biol 7,719-23.
    Liu, Q., Rand, T. A., Kalidas, S., Du, F., Kim, H. E., Smith, D. P. and Wang, X. (2003). R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway. Science 301,1921-5.
    Lu, R., Maduro, M., Li, F., Li, H. W., Broitman-Maduro, G., Li, W. X. and Ding, S. W. (2005). Animal virus replication and RNAi-mediated antiviral silencing in Caenorhabditis elegans. Nature 436, 1040-3.
    Lu, S. and Cullen, B. R. (2004). Adenovirus VA1 noncoding RNA can inhibit small interfering RNA and MicroRNA biogenesis. J Virol 78,12868-76.
    Lynch, G. W. and Pfueller, S. L. (1988). Thrombin-independent activation of platelet factor XIII by endogenous platelet acid protease. Thromb Haemost 59,372-7.
    MacDonald, S. M., Bhisutthibhan, J., Shapiro, T. A., Rogerson, S. J., Taylor, T. E., Tembo, M., Langdon, J. M. and Meshnick, S. R. (2001). Immune mimicry in malaria:Plasmodium falciparum secretes a functional histamine-releasing factor homolog in vitro and in vivo. Proc Natl Acad Sci U S A 98,10829-32.
    MacDonald, S. M., Rafnar, T., Langdon, J. and Lichtenstein, L. M. (1995). Molecular identification of an IgE-dependent histamine-releasing factor. Science 269,688-90.
    MacRae, I. J., Ma, E., Zhou, M., Robinson, C. V. and Doudna, J. A. (2008). In vitro reconstitution of the human RISC-loading complex. Proc Natl Acad Sci U S A 105,512-7.
    Majde, J. A. (2000). Viral double-stranded RNA, cytokines, and the flu. J Interferon Cytokine Res 20, 259-72.
    Maniataki, E. and Mourelatos, Z. (2005). A human, ATP-independent, RISC assembly machine fueled by pre-miRNA. Genes Dev 19,2979-90.
    Mathews, M. B. and Shenk, T. (1991). Adenovirus virus-associated RNA and translation control. J Virol 65,5657-62.
    Matzke, M. A. and Birchler, J. A. (2005). RNAi-mediated pathways in the nucleus. Nat Rev Genet 6, 24-35.
    McDonald, J. K., Zeitman, B. B. and Ellis, S. (1972). Detection of a Iysosomal carboxypeptidase and a Iysosomal dipeptidase in highly-purified dipeptidyl aminopeptidase I (cathepsin C) and the elimination of their activities from preparations used to sequence peptides. Biochem Biophys Res Commun 46,62-70.
    McEuen, A. R., Ashworth, D. M. and Walls, A. F. (1998). The conversion of recombinant human mast cell prochymase to enzymatically active chymase by dipeptidyl peptidase I is inhibited by heparin and histamine. Eur J Biochem 253,300-8.
    McGuire, M. J., Lipsky, P. E. and Thiele, D. L. (1993). Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I. J Biol Chem 268,2458-67.
    McGuire, M. J., Lipsky, P. E. and Thiele, D. L. (1997).Cloning and characterization of the cDNA encoding mouse dipeptidyl peptidase I (cathepsin C). Biochim Biophys Acta 1351,267-73.
    Molnar, A., Csorba, T., Lakatos, L., Varallyay, E., Lacomme, C. and Burgyan, J. (2005). Plant virus-derived small interfering RNAs originate predominantly from highly structured single-stranded viral RNAs. J Virol 79,7812-8.
    Napoli, C., Lemieux, C. and Jorgensen, R. (1990). Introduction of a Chimeric Chalcone Synthase Gene into Petunia Results in Reversible Co-Suppression of Homologous Genes in trans. Plant Cell 2, 279-289.
    Nielsen, H. V., Johnsen, A. H., Sanchez, J. C., Hochstrasser, D. F. and Schiotz, P. O. (1998). Identification of a basophil leukocyte interleukin-3-regulated protein that is identical to IgE-dependent histamine-releasing factor. Allergy 53,642-52.
    Novina, C. D., Murray, M. F., Dykxhoorn, D. M., Beresford, P. J., Riess, J., Lee, S. K., Collman, R. G, Lieberman, J., Shankar, P. and Sharp, P. A. (2002). siRNA-directed inhibition of HIV-1 infection. Nat Med 8,681-6.
    Ong, C. L., Thorpe, J. C., Gorry, P. R., Bannwarth, S., Jaworowski, A., Howard, J. L., Chung, S., Campbell, S., Christensen, H. S., Clerzius, G et al. (2005). Low TRBP levels support an innate human immunodeficiency virus type 1 resistance in astrocytes by enhancing the PKR antiviral response. J Virol 79,12763-72.
    Pan, D., He, N., Yang, Z., Liu, H. and Xu, X. (2005). Differential gene expression profile in hepatopancreas of WSSV-resistant shrimp (Penaeus japonicus) by suppression subtractive hybridization. Dev Comp Immunol 29,103-12.
    Park, H., Davies, M. V., Langland, J. O., Chang, H. W., Nam, Y. S., Tartaglia, J., Paoletti, E., Jacobs, B. L., Kaufman, R. J. and Venkatesan, S. (1994). TAR RNA-binding protein is an inhibitor of the interferon-induced protein kinase PKR. Proc Natl Acad Sci U S A 91,4713-7.
    Parker, G S., Eckert, D. M. and Bass, B. L. (2006). RDE-4 preferentially binds long dsRNA and its dimerization is necessary for cleavage of dsRNA to siRNA. RNA 12,807-18.
    Parker, G S., Maity, T. S. and Bass, B. L. (2008). dsRNA binding properties of RDE-4 and TRBP reflect their distinct roles in RNAi. J Mol Biol 384,967-79.
    Partidos, C. D., Hoebeke, J., Moreau, E., Chaloin, O., Tunis, M., Belliard, G, Briand, J. P., Desgranges, C. and Muller, S. (2005). The binding affinity of double-stranded RNA motifs to HIV-1 Tat protein affects transactivation and the neutralizing capacity of anti-Tat antibodies elicited after intranasal immunization. Eur J Immunol 35,1521-9.
    Pay, A., Heberle-Bors, E. and Hirt, H. (1992). An alfalfa cDNA encodes a protein with homology to translationally controlled human tumor protein. Plant Mol Biol 19,501-3.
    Pelisson, A., Sarot, E., Payen-Groschene, G. and Bucheton, A. (2007). A novel repeat-associated small interfering RNA-mediated silencing pathway downregulates complementary sense gypsy transcripts in somatic cells of the Drosophila ovary. J Virol 81,1951-60.
    Qiu, G. F., Yamano, K. and Unuma, T. (2005). Cathepsin C transcripts are differentially expressed in the final stages of oocyte maturation in kuruma prawn Marsupenaeus japonicus. Comp Biochem Physiol B Biochem Mol Biol 140,171-81.
    Qiu, L., Jiang, S., Huang, J., Wang, W., Zhang, D., Wu, Q. and Yang, K. (2008). Molecular cloning and mRNA expression of cathepsin C gene in black tiger shrimp (Penaeus monodon). Comp Biochem Physiol A Mol Integr Physiol 150,320-5.
    Rana, T. M. (2007). Illuminating the silence:understanding the structure and function of small RNAs. Nat Rev Mol Cell Biol 8,23-36.
    Robalino, J., Bartlett, T., Shepard, E., Prior, S., Jaramillo, G., Scura, E., Chapman, R. W., Gross, P. S., Browdy, C. L. and Warr, G. W. (2005). Double-stranded RNA induces sequence-specific antiviral silencing in addition to nonspecific immunity in a marine shrimp:convergence of RNA interference and innate immunity in the invertebrate antiviral response? J Virol 79,13561-71.
    Robalino, J., Bartlett, T. C., Chapman, R. W., Gross, P. S., Browdy, C. L. and Warr, G., W. (2007). Double-stranded RNA and antiviral immunity in marine shrimp:inducible host mechanisms and evidence for the evolution of viral counter-responses. Dev Comp Immunol 31,539-47.
    Robalino, J., Browdy, C. L., Prior, S., Metz, A., Parnell, P., Gross, P. and Warr, G. (2004). Induction of antiviral immunity by double-stranded RNA in a marine invertebrate. J Virol 78,10442-8. Robb, G. B. and Rana, T. M. (2007). RNA helicase A interacts with RISC in human cells and functions in RISC loading. Mol Cell 26,523-37.
    Rojtinnakorn, J., Hirono, I., Itami, T., Takahashi, Y. and Aoki, T. (2002). Gene expression in haemocytes of kuruma prawn, Penaeus japonicus, in response to infection with WSSV by EST approach. Fish Shellfish Immunol 13,69-83.
    Rossi, J. J. (2005). Mammalian Dicer finds a partner. EMBO Rep 6,927-9.
    Roux, M. M., Pain, A., Klimpel, K. R. and Dhar, A. K. (2002). The lipopolysaccharide and beta-1,3-glucan binding protein gene is upregulated in white spot virus-infected shrimp (Penaeus stylirostris). J Virol 76,7140-9.
    Saito, K., Ishizuka, A., Siomi, H. and Siomi, M. C. (2005). Processing of pre-microRNAs by the Dicer-1-Loquacious complex in Drosophila cells. PLoS Biol 3, e235.
    Sanchez, J. C, Schaller, D., Ravier, F., Golaz, O., Jaccoud, S., Belet, M., Wilkins, M. R., James, R., Deshusses, J. and Hochstrasser, D. (1997). Translationally controlled tumor protein:a protein identified in several nontumoral cells including erythrocytes. Electrophoresis 18,150-5.
    Sasaki, T., Shiohama, A., Minoshima, S. and Shimizu, N. (2003). Identification of eight members of the Argonaute family in the human genome small star, filled. Genomics 82,323-30.
    Saunders, L. R. and Barber, G. N. (2003). The dsRNA binding protein family:critical roles, diverse cellular functions. FASEB J17,961-83.
    Schroeder, J. T., Lichtenstein, L. M. and MacDonald, S. M. (1996). An immunoglobulin E-dependent recombinant histamine-releasing factor induces interleukin-4 secretion from human basophils. JExp Med 183,1265-70.
    Schroeder, J. T., Lichtenstein, L. M. and MacDonald, S. M. (1997). Recombinant histamine-releasing factor enhances IgE-dependent IL-4 and IL-13 secretion by human basophils. J Immunol 159,447-52.
    Schulenburg, H., Boehnisch, C. and Michiels, N. K. (2007). How do invertebrates generate a highly specific innate immune response? Mol Immunol 44,3338-44.
    Sen, G. L. and Blau, H. M. (2005). Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies. Nat Cell Biol 7,633-6.
    Smyth, M. J., McGuire, M. J. and Thia, K. Y. (1995). Expression of recombinant human granzyme B. A processing and activation role for dipeptidyl peptidase I. J Immunol 154,6299-305.
    Soldan, S. S., Plassmeyer, M. L., Matukonis, M. K. and Gonzalez-Scarano, F. (2005). La Crosse virus nonstructural protein NSs counteracts the effects of short interfering RNA.J Virol 79,234-44.
    Sturzenbaum, S. R., Kille, P. and Morgan, A. J. (1998). Identification of heavy metal induced changes in the expression patterns of the translationally controlled tumour protein (TCTP) in the earthworm Lumbricus rubellusl. Biochim Biophys Acta 1398,294-304.
    Sullivan, C. S. and Ganem, D. (2005). A virus-encoded inhibitor that blocks RNA interference in mammalian cells. J Virol 79,7371-9.
    Tabara, H., Sarkissian, M., Kelly, W. G., Fleenor, J., Grishok, A., Timmons, L., Fire, A. and Mello, C. C. (1999). The rde-1 gene, RNA interference, and transposon silencing in C. elegans. Cell 99, 123-32.
    Tahbaz, N., Kolb, F. A., Zhang, H., Jaronczyk, K., Filipowicz, W. and Hobman, T. C. (2004). Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer. EMBO Rep 5,189-94.
    Teshima, S., Rokutan, K., Nikawa, T. and Kishi, K. (1998). Macrophage colony-stimulating factor stimulates synthesis and secretion of a mouse homolog of a human IgE-dependent histamine-releasing factor by macrophages in vitro and in vivo. J Immunol 161,6356-66.
    Thaw, P., Baxter, N. J., Hounslow, A. M., Price, C., Waltho, J. P. and Craven, C. J. (2001). Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones. Nat Struct Biol 8,701-4.
    Thiele, D. L., McGuire, M. J. and Lipsky, P. E. (1997). A selective inhibitor of dipeptidyl peptidase I impairs generation of CD8+ T cell cytotoxic effector function. J Immunol 158,5200-10.
    Thiele, H., Berger, M., Skalweit, A. and Thiele, B. J. (2000). Expression of the gene and processed pseudogenes encoding the human and rabbit translationally controlled tumour protein (TCTP). Eur J Biochem 267,5473-81.
    Thomas, G. and Luther, H. (1981). Transcriptional and translational control of cytoplasmic proteins after serum stimulation of quiescent Swiss 3T3 cells. Proc Natl Acad Sci USA 78,5712-6.
    Timmons, L., Court, D. L. and Fire, A. (2001). Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans. Gene 263,103-12.
    Tirasophon, W., Roshorm, Y. and Panyim, S. (2005). Silencing of yellow head virus replication in penaeid shrimp cells by dsRNA. Biochem Biophys Res Commun 334,102-7.
    Tolia, N. H. and Joshua-Tor, L. (2007). Slicer and the argonautes. Nat Chem Biol 3,36-43.
    Tomari, Y., Matranga, C., Haley, B., Martinez, N. and Zamore, P. D. (2004). A protein sensor for siRNA asymmetry. Science 306,1377-80.
    Tomari, Y. and Zamore, P. D. (2005). Perspective:machines for RNAi. Genes Dev 19,517-29.
    Tuynder, M., Fiucci, G., Prieur, S., Lespagnol, A., Geant, A., Beaucourt, S., Duflaut, D., Besse, S., Susini, L., Cavarelli, J. et al. (2004). Translationally controlled tumor protein is a target of tumor reversion. Proc Natl Acad Sci USA 101,15364-9.
    van Rij, R. P., Saleh, M. C., Berry, B., Foo, C., Houk, A., Antoniewski, C. and Andino, R. (2006). The RNA silencing endonuclease Argonaute 2 mediates specific antiviral immunity in Drosophila melanogaster. Genes Dev 20,2985-95.
    Vargason, J. M., Szittya, G., Burgyan, J. and Hall, T. M. (2003). Size selective recognition of siRNA by an RNA silencing suppressor. Cell 115,799-811.
    Vastenhouw, N. L. and Plasterk, R. H. (2004). RNAi protects the Caenorhabditis elegans germline against transposition. Trends Genet 20,314-9.
    Voinnet, O. (2005a). Induction and suppression of RNA silencing:insights from viral infections. Nat Rev Genet 6,206-20.
    Voinnet, O. (2005b). Non-cell autonomous RNA silencing. FEBSLett 579,5858-71.
    Wang, H. W., Noland, C., Siridechadilok, B., Taylor, D. W., Ma, E., Felderer, K., Doudna, J. A. and Nogales, E. (2009a). Structural insights into RNA processing by the human RISC-loading complex. Nat Struct Mol Biol 16,1148-53.
    Wang, S., Liu, N., Chen, A. J., Zhao, X. F. and Wang, J. X. (2009b). TRBP homolog interacts with eukaryotic initiation factor 6 (eIF6) in Fenneropenaeus chinensis. J Immunol 182,5250-8.
    Wang, Y. G., Hassan, M. D., Shariff, M., Zamri, S. M. and Chen, X. (1999). Histopathology and cytopathology of white spot syndrome virus (WSSV) in cultured Penaeus monodon from peninsular Malaysia with emphasis on pathogenesis and the mechanism of white spot formation. Dis Aquat Organ 39,1-11.
    Wassenegger, M., Heimes, S., Riedel, L. and Sanger, H. L. (1994). RNA-directed de novo methylation of genomic sequences in plants. Cell 76,567-76.
    Wassenegger, M. and Krczal, G. (2006). Nomenclature and functions of RNA-directed RNA polymerases. Trends Plant Sci 11,142-51.
    Weber, F., Wagner, V., Rasmussen, S. B., Hartmann, R. and Paludan, S. R. (2006). Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses. J Virol 80,5059-64.
    Westerhout, E. M., Ooms, M., Vink, M., Das, A. T. and Berkhout, B. (2005). HIV-1 can escape from RNA interference by evolving an alternative structure in its RNA genome. Nucleic Acids Res 33, 796-804.
    Wianny, F. and Zernicka-Goetz, M. (2000). Specific interference with gene function by double-stranded RNA in early mouse development. Nat Cell Biol 2,70-5.
    Wolters, P. J., Raymond, W. W., Blount, J. L. and Caughey, G. H. (1998). Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I. J Biol Chem 273,15514-20.
    Xu, A., Bellamy, A. R. and Taylor, J. A. (1999). Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level. Biochem J 342 Pt 3,683-9.
    Ye, K., Malinina, L. and Patel, D. J. (2003). Recognition of small interfering RNA by a viral suppressor of RNA silencing. Nature 426,874-8.
    Yenofsky, R., Cereghini, S., Krowczynska, A. and Brawerman, G. (1983). Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide. Mol Cell Biol 3,1197-203.
    Yeung, M. L., Bennasser, Y., Le, S. Y. and Jeang, K. T. (2005). siRNA, miRNA and HIV:promises and challenges. Cell Res 15,935-46.
    Yodmuang, S., Tirasophon, W., Roshorm, Y., Chinnirunvong, W. and Panyim, S. (2006). YHV-protease dsRNA inhibits YHV replication in Penaeus monodon and prevents mortality. Biochem Biophys Res Commun 341,351-6.
    Zamore, P. D. (2007). RNA silencing:genomic defence with a slice of pi. Nature 446,864-5.
    Zamore, P. D., Tuschl, T., Sharp, P. A. and Bartel, D. P. (2000). RNAi:double-stranded RNA directs the ATP-dependent cleavage of mRNA at 21 to 23 nucleotide intervals. Cell 101,25-33.
    Zhang, D., Li, F., Weidner, D., Mnjoyan, Z. H. and Fujise, K. (2002). Physical and functional interaction between myeloid cell leukemia 1 protein (MCL1) and Fortilin. The potential role of MCL1 as a fortilin chaperone. J Biol Chem 277,37430-8.
    Zhong, J., Peters, A. H., Lee, K. and Braun, R. E. (1999). A double-stranded RNA binding protein required for activation of repressed messages in mammalian germ cells. Nat Genet 22,171-4.

© 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