Cloning, expression, and partial characterization of FBPA from Schistosoma japonicum, a molecule on that the fluke may develop nutrition competition and immune evasion from human

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• 作者：Qiping Hu ; Huiqiong Xie ; Shuyu Zhu ; Dejun Liao ; Tingzheng Zhan…
• 关键词：Schistosoma japonicum ; Fructose ; 1 ; 6 ; bisphosphate aldolase ; Cloning ; Expression ; Enzymatic kinetics ; Antigenic peptide ; Substrate inhibition
• 刊名：Parasitology Research
• 出版年：2015
• 出版时间：September 2015
• 年：2015
• 卷：114
• 期：9
• 页码：3459-3468
• 全文大小：2,119 KB
• 参考文献：Arakaki TL, Pezza JA, Cronin MA, Hopkins CE, Zimmer DB, Tolan DR, Allen KN (2004) Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function. Protein Sci 13(12):3077-4. doi:10.-110/?ps.-4915904
  Berthiaume L, Tolan DR, Sygusch J (1993) Differential usage of the carboxyl-terminal region among aldolase isozymes. J Biol Chem 268(15):10826-5PubMed
  Blostem R, Rutter WJ (1963) Comparative studies of liver and muscle aldolase. II. Immunochemical and chromatographic differentiation. J Biol Chem 238(10):3280-5
  Casazza JP, Stone SR, Fromm HJ (1979) Kinetic studies of bovine liver fructose-1,6-bisphosphatase. J Biol Chem 254(11):4661-5PubMed
  Chen J, Hu X, He S, Wang L, Hu D, Wang X, Zheng M, Yang Y, Liang C, Xu J, Yu X (2010) Expression and immune response analysis of Schistosoma japonicum VAL-1, a homologue of vespid venom allergens. Parasitol Res 106(6):1413-. doi:10.-007/?s00436-010-1817-y View Article PubMed
  Dax C, Coin?on M, Sygusch J, Blonski C (2005) Hydroxynaphthaldehyde phosphate derivatives as potent covalent Schiff base inhibitors of fructose-1,6-bisphosphate aldolase. Biochemistry 44(14):5430-3. doi:10.-021/?bi0477992 View Article PubMed
  Diao W, Zhou H, Pan W, Liu H, Shen Y, Xu Y, Li X, Cao J (2014) Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum. Parasitol Res 113(3):919-4. doi:10.-007/?s00436-013-3723-6 PubMed Central View Article PubMed
  Diaz SA, Martin SR, Grainger M, Howell SA, Green JL, Holder AA (2014) Plasmodium falciparum aldolase and the C-terminal cytoplasmic domain of certain apical organellar proteins promote actin polymerization. Mol Biochem Parasitol 197(1-2):9-4. doi:10.-016/?j.?molbiopara.-014.-9.-06 PubMed Central View Article PubMed
  Dziewulska-Szwajkowska D, Zmojdzian M, Dobryszycki P, Kochman M, Dzugaj A (2004) The interaction of FBPase with aldolase a kinetic and fluorescence investigation on chicken muscle enzymes. Comput Biochem Phys 137(1):115-9. doi:10.-016/?j.?cbpc.-003.-0.-10 View Article
  El-Dabaa E, Mei H, El-Sayed A, Karim AM, Eldesoky HM, Fahim FA, LoVerde PT, Saber MA (1998) Cloning and characterization of Schistosoma mansoni fructose-1,6-biphosphate aldolase isoenzyme. J Parasitol 84(5):954-0View Article PubMed
  Galkin A, Kulakova L, Melamud E, Li L, Wu C, Mariano P, Dunaway-Mariano D, Nash TE, Herzberg O (2007) Characterization, kinetics, and crystal structures of fructose-1,6-bisphosphate aldolase from the human parasite, Giardia lamblia. J Biol Chem 282(7):4859-7. doi:10.-074/?jbc.?M609534200 View Article PubMed
  Guillou F, Roger E, Moné Y, Rognon A, Grunau C, Théron A, Mitta G, Coustau C, Gourbal BE (2007) Excretory-secretory proteome of larval Schistosoma mansoni and Echinostoma caproni, two parasites of Biomphalaria glabrata. Mol Biochem Parasitol 155(1):45-6. doi:10.-016/?j.?molbiopara.-007.-5.-09 View Article PubMed
  Hester G, Brenner-Holzach O, Rossi FA, Struck-Donatz M, Winterhalter KH, Smit JD, Piontek K (1991) The crystal structure of fructose-1,6-biphosphate aldolase from Drosophila melanogaster at 2.5 ? resolution. FEBS Lett 292(1-2):237-2View Article PubMed
  Hurst MH, Shi YE, Lindberg R (2000) Pathology and course of natural Schistosoma japonicum infection in pigs: results of a field study in Hubei province, China. Ann Trop Med Parasitol 94(5):461-7PubMed
  Kusakabe T, Motoki K, Sugimoto Y, Takasaki Y, Hori K (1994) Human aldolase B: liver-specific properties of the isozyme depend on type B isozyme group-specific sequences. Protein Eng 7(11):1387-3. doi:10.-093/?protein/-.-1.-387 View Article PubMed
  Li Y, Sleigh AC, Williams GM, Forsyth SJ, Tanner M, McManus DP (2000a) Measuring exposure to Schistosoma japonicum in China. III. Activity diaries, snail and human infection, transmission ecology and options for control. Acta Trop 75(3):279-9. doi:10.-016/?S0001-706X(00)00056-5 View Article PubMed
  Li YS, Sleigh AC, Ross AG, Li Y, Williams GM, Tanner M, McManus DP (2000b) Two-year impact of praziquantel treatment for Schistosoma japonicum infection in China: reinfection, subclinical disease and fibrosis marker measurements. T Roy Soc TropP Med H 94(2):191-View Article
  Li YS, Sleigh AC, Ross AG, Williams GM, Tanner M, McManus DP (2000c) Epidemiology of Schistosoma japonicum in China: morbidity and strategies for control in the Dongting Lake region. Int J Parasitol 30(3):273-1View Article PubMed
  Lu G, Hu X, Peng Z, Xie H, Li Y, Wu Z, Yu X (2006) Expression and characterization of lactate dehydrogenase from Schistosoma japonicum. Parasitol Res 99(5):593-View Article PubMed
  Motoki K, Kitajima Y, Hori K (1993) Isozyme-specific modules on human aldolase A molecule: isozyme group-specific sequences 1 and 4 are required for showing characteristics as aldolase A. J Biol Chem 268(3):1677-3PubMed
  Mutapi F, Bourke C, Harcus Y, Midzi N, Mduluza T, Tu
• 作者单位：Qiping Hu (1)
  Huiqiong Xie (1)
  Shuyu Zhu (1)
  Dejun Liao (2)
  Tingzheng Zhan (2)
  Dengyu Liu (2)
  
  1. Department of Cell Biology and Genetics, School of Preclinical Medicine, Guangxi Medical University, Nanning, 530021, People’s Republic of China
  2. Department of Parasitology, School of Preclinical Medicine, Guangxi Medical University, 22 Shuangyong Road, Nanning, 530021, People’s Republic of China
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Biomedicine
  Medical Microbiology
  Microbiology
  Immunology
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1432-1955

文摘

Carbohydrate metabolism is the most important physiological process for Schistosoma japonicum which resides in host. However, as a key glycolytic enzyme in carbohydrate metabolism, fructose-1,6-bisphosphate aldolase (FBPA), there is no study on its enzymatic kinetics and antigenic peptides. Here, we report the gene cloning, expression, purification, and kinetics of the FBPA from S. japonicum (sjFBPA). After cloning, sjFBPA gene was introduced into pET-28a and transformed BL21, and a soluble His6-sjFBPA was expressed and purified successfully at the expected molecular mass of ~45?kDa. We first reported that the diversities in IGS regions and the features of residues position 346 and 357-62 of sjFBPA may be conferred either through conformational changes influencing easily the active site from a distance and/or causing the C-terminal region to interact directly with the active site, which lead His6-sjFBPA to exhibit a higher specific activity of 197.43 units/mg and degrades FBP with a typical substrate inhibition model and a higher efficiency of k cat --261.3/s and K m --.061?μM than human aldolases, which might be the strategy that S. japonicum gaining energy and surviving in its environment with low concentration of carbohydrate, and benefitting to get more metabolic substances for parasites in nutrition competition with their host. sjFBPA exhibits a high similarity of 81.46?% with that of hosts, especially in antigenic peptide regions, and 14 of 15 antigenic peptides of sjFBPA were conserved to those of human aldolase A, B, and/or C with high identity (17, 16, or 16 antigenic peptides, respectively), which may result in a molecular mimicry of FBPA with that of host, and an immune evasion from their hosts. This work would supply an experimental base for using FBPA to prevent the schistosomiasis in the future.