In silico approach for the identification of immunological properties of enolase from Trypanosoma cruzi and its possible usefulness as vaccine in Chagas disease
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- 作者：Alejandro Carabarín-Lima (1) (4)
Olivia Rodríguez-Morales (1)
María Cristina González-Vázquez (2) (5)
Lidia Baylón-Pacheco (3)
Pedro A. Reyes (1)
Minerva Arce-Fonseca (1)
José Luis Rosales-Encina (3) - 刊名：Parasitology Research
- 出版年：2014
- 出版时间：March 2014
- 年：2014
- 卷：113
- 期：3
- 页码：1029-1039
- 全文大小：834 KB
- 参考文献：1. Babbitt PC, Hasson MS, Wedekind JE, Palmer DR, Barrett WC, Reed GH, Rayment I, Ringe D, Kenyon GL, Gerlt JA (1996) The enolase superfamily: a general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids. Biochemistry 35:16489-6501 g/10.1021/bi9616413" target="_blank" title="It opens in new window">CrossRef
2. Bergmann S, Rohde M, Chhatwal GS, Hammerschmidt S (2001) Alpha-enolase of / Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40:1273-287 g/10.1046/j.1365-2958.2001.02448.x" target="_blank" title="It opens in new window">CrossRef
3. Bern C, Montgomery SP (2009) An estimate of the burden of Chagas disease in the United States. Clin Infect Dis 49:e52–e54 g/10.1086/605091" target="_blank" title="It opens in new window">CrossRef
4. Brandina I, Graham J, Lemaitre-Guillier C, Entelis N, Krasheninnikov I, Sweetlove L, Tarassov I, Martin RP (2006) Enolase takes part in a macromolecular complex associated to mitochondria in yeast. Biochim Biophys Acta 1757:1217-228 g/10.1016/j.bbabio.2006.07.001" target="_blank" title="It opens in new window">CrossRef
5. Camandaroba EL, Reis EA, Goncalves MS, Reis MG, Andrade SG (2003) / Trypanosoma cruzi: susceptibility to chemotherapy with benznidazole of clones isolated from the highly resistant Colombian strain. Rev Soc Bras Med Trop 36:201-09 g/10.1590/S0037-86822003000200002" target="_blank" title="It opens in new window">CrossRef
6. Cancado JR (1999) Criteria of Chagas disease cure. Mem Inst Oswaldo Cruz 94:331-35 g/10.1590/S0074-02761999000700064" target="_blank" title="It opens in new window">CrossRef
7. Capello M, Ferri-Borgogno S, Cappello P, Novelli F (2011) Alpha-enolase: a promising therapeutic and diagnostic tumor target. FEBS J 278:1064-074 g/10.1111/j.1742-4658.2011.08025.x" target="_blank" title="It opens in new window">CrossRef
8. Carod-Artal FJ, Gascon J (2010) Chagas disease and stroke. Lancet Neurol 9:533-42 g/10.1016/S1474-4422(10)70042-9" target="_blank" title="It opens in new window">CrossRef
9. Chen N, Yuan ZG, Xu MJ, Zhou DH, Zhang XX, Zhang YZ, Wang XW, Yan C, Lin RQ, Zhu XQ (2012) / Ascaris suum enolase is a potential vaccine candidate against ascariasis. Vaccine 30:3478-482 g/10.1016/j.vaccine.2012.02.075" target="_blank" title="It opens in new window">CrossRef
10. Decker BL, Wickner WT (2006) Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast. J Biol Chem 281:14523-4528 g/10.1074/jbc.M600911200" target="_blank" title="It opens in new window">CrossRef
11. Entelis N, Brandina I, Kamenski P, Krasheninnikov IA, Martin RP, Tarassov I (2006) A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in / Saccharomyces cerevisiae. Genes Dev 20:1609-620 g/10.1101/gad.385706" target="_blank" title="It opens in new window">CrossRef
12. Etz H, Minh DB, Henics T, Dryla A, Winkler B, Triska C, Boyd AP, Sollner J, Schmidt W, Von Ahsen U, Buschle M, Gill SR, Kolonay J, Khalak H, Fraser CM, Von Gabain A, Nagy E, Meinke A (2002) Identification of in vivo expressed vaccine candidate antigens from / Staphylococcus aureus. Proc Natl Acad Sci U S A 99:6573-578 g/10.1073/pnas.092569199" target="_blank" title="It opens in new window">CrossRef
13. Feo S, Arcuri D, Piddini E, Passantino R, Giallongo A (2000) ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1). FEBS Lett 473:47-2 g/10.1016/S0014-5793(00)01494-0" target="_blank" title="It opens in new window">CrossRef
14. Ferguson DJ, Parmley SF, Tomavo S (2002) Evidence for nuclear localisation of two stage-specific isoenzymes of enolase in / Toxoplasma gondii correlates with active parasite replication. Int J Parasitol 32:1399-410 g/10.1016/S0020-7519(02)00129-7" target="_blank" title="It opens in new window">CrossRef
15. Gan W, Zhao G, Xu H, Wu W, Du W, Huang J, Yu X, Hu X (2010) Reverse vaccinology approach identify an / Echinococcus granulosus tegumental membrane protein enolase as vaccine candidate. Parasitol Res 106:873-82 g/10.1007/s00436-010-1729-x" target="_blank" title="It opens in new window">CrossRef
16. Guzman-Bracho C (2001) Epidemiology of Chagas disease in Mexico: an update. Trends Parasitol 17:372-76 g/10.1016/S1471-4922(01)01952-3" target="_blank" title="It opens in new window">CrossRef
17. He Y, Xiang Z (2013) Databases and / in silico tools for vaccine design. Methods Mol Biol 993:115-27 g/10.1007/978-1-62703-342-8_8" target="_blank" title="It opens in new window">CrossRef
18. Labbe M, Peroval M, Bourdieu C, Girard-Misguich F, Pery P (2006) / Eimeria tenella enolase and pyruvate kinase: a likely role in glycolysis and in others functions. Int J Parasitol 36:1443-452 g/10.1016/j.ijpara.2006.08.011" target="_blank" title="It opens in new window">CrossRef
19. Lee H, Guo Y, Ohta M, Xiong L, Stevenson B, Zhu JK (2002) LOS2, a genetic locus required for cold-responsive gene transcription encodes a bi-functional enolase. EMBO J 21:2692-702 g/10.1093/emboj/21.11.2692" target="_blank" title="It opens in new window">CrossRef
20. Li W, Hu X, Zhang X, Ge Y, Zhao S, Hu Y, Ashman RB (2011) Immunisation with the glycolytic enzyme enolase confers effective protection against / Candida albicans infection in mice. Vaccine 29:5526-533 g/10.1016/j.vaccine.2011.05.030" target="_blank" title="It opens in new window">CrossRef
21. Li Y, Xu H, Chen J, Gan W, Wu W, Wu W, Hu X (2012) Gene cloning, expression, and localization of antigen 5 in the life cycle of / Echinococcus granulosus. Parasitol Res 110:2315-323 g/10.1007/s00436-011-2766-9" target="_blank" title="It opens in new window">CrossRef
22. Liu L, Cheng G, Wang C, Pan X, Cong Y, Pan Q, Wang J, Zheng F, Hu F, Tang J (2009) Identification and experimental verification of protective antigens against / Streptococcus suis serotype 2 based on genome sequence analysis. Curr Microbiol 58:11-7 g/10.1007/s00284-008-9258-x" target="_blank" title="It opens in new window">CrossRef
23. Maione D, Margarit I, Rinaudo CD, Masignani V, Mora M, Scarselli M, Tettelin H, Brettoni C, Iacobini ET, Rosini R, D’Agostino N, Miorin L, Buccato S, Mariani M, Galli G, Nogarotto R, Nardi-Dei V, Vegni F, Fraser C, Mancuso G, Teti G, Madoff LC, Paoletti LC, Rappuoli R, Kasper DL, Telford JL, Grandi G (2005) Identification of a universal Group B streptococcus vaccine by multiple genome screen. Science 309:148-50 g/10.1126/science.1109869" target="_blank" title="It opens in new window">CrossRef
24. Moncayo A (2003) Chagas disease: current epidemiological trends after the interruption of vectorial and transfusional transmission in the Southern Cone countries. Mem Inst Oswaldo Cruz 98:577-91 g/10.1590/S0074-02762003000500001" target="_blank" title="It opens in new window">CrossRef
25. Moncayo A, Silveira AC (2009) Current epidemiological trends for Chagas disease in Latin America and future challenges in epidemiology, surveillance and health policy. Mem Inst Oswaldo Cruz 104:17-0 g/10.1590/S0074-02762009000900005" target="_blank" title="It opens in new window">CrossRef
26. Montigiani S, Falugi F, Scarselli M, Finco O, Petracca R, Galli G, Mariani M, Manetti R, Agnusdei M, Cevenini R, Donati M, Nogarotto R, Norais N, Garaguso I, Nuti S, Saletti G, Rosa D, Ratti G, Grandi G (2002) Genomic approach for analysis of surface proteins in / Chlamydia pneumoniae. Infect Immun 70:368-79 g/10.1128/IAI.70.1.368-379.2002" target="_blank" title="It opens in new window">CrossRef
27. Mundodi V, Kucknoor AS, Alderete JF (2008) Immunogenic and plasminogen-binding surface-associated alpha-enolase of / Trichomonas vaginalis. Infect Immun 76:523-31 g/10.1128/IAI.01352-07" target="_blank" title="It opens in new window">CrossRef
28. Nakada T, Nagano I, Wu Z, Takahashi Y (2005) Molecular cloning and functional expression of enolase from / Trichinella spiralis. Parasitol Res 96:354-60 g/10.1007/s00436-005-1365-z" target="_blank" title="It opens in new window">CrossRef
29. Pal-Bhowmick I, Mehta M, Coppens I, Sharma S, Jarori GK (2007) Protective properties and surface localization of / Plasmodium falciparum enolase. Infect Immun 75:5500-508 g/10.1128/IAI.00551-07" target="_blank" title="It opens in new window">CrossRef
30. Pancholi V (2001) Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci 58:902-20 g/10.1007/PL00000910" target="_blank" title="It opens in new window">CrossRef
31. Pancholi V, Chhatwal GS (2003) Housekeeping enzymes as virulence factors for pathogens. Int J Med Microbiol 293:391-01 g/10.1078/1438-4221-00283" target="_blank" title="It opens in new window">CrossRef
32. Pancholi V, Fischetti VA (1998) Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 273:14503-4515 g/10.1074/jbc.273.23.14503" target="_blank" title="It opens in new window">CrossRef
33. Piast M, Kustrzeba-Wojcicka I, Matusiewicz M, Banas T (2005) Molecular evolution of enolase. Acta Biochim Pol 52:507-13
34. Rodriguez E, Romaris F, Lorenzo S, Moreno J, Bonay P, Ubeira FM, Garate T (2006) A recombinant enolase from / Anisakis simplex is differentially recognized in natural human and mouse experimental infections. Med Microbiol Immunol 195:1-0 g/10.1007/s00430-005-0236-7" target="_blank" title="It opens in new window">CrossRef
35. Schmunis GA (2007) Epidemiology of Chagas disease in non-endemic countries: the role of international migration. Mem Inst Oswaldo Cruz 102:75-5 g/10.1590/S0074-02762007005000093" target="_blank" title="It opens in new window">CrossRef
36. Sotillo J, Valero ML, Sánchez Del Pino MM, Fried B, Esteban JG, Marcilla A, Toledo R (2010) Excretory/secretory proteome of the adult stage of / Echinostoma caproni. Parasitol Res 107:691-97 g/10.1007/s00436-010-1923-x" target="_blank" title="It opens in new window">CrossRef
37. Subramanian A, Miller DM (2000) Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene. J Biol Chem 275:5958-965 g/10.1074/jbc.275.8.5958" target="_blank" title="It opens in new window">CrossRef
38. Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28:2731-739 g/10.1093/molbev/msr121" target="_blank" title="It opens in new window">CrossRef
39. Torre-Escudero E, Manzano-Roman R, Perez-Sanchez R, Siles-Lucas M, Oleaga A (2010) Cloning and characterization of a plasminogen-binding surface-associated enolase from / Schistosoma bovis. Vet Parasitol 173:76-4 g/10.1016/j.vetpar.2010.06.011" target="_blank" title="It opens in new window">CrossRef
40. Vanegas G, Quinones W, Carrasco-Lopez C, Concepcion JL, Albericio F, Avilan L (2007) Enolase as a plasminogen binding protein in / Leishmania mexicana. Parasitol Res 101:1511-516 g/10.1007/s00436-007-0668-7" target="_blank" title="It opens in new window">CrossRef
41. Voelker R (2009) A century after Chagas disease discovery, hurdles to tackling the infection remain. JAMA 302:1045-047 g/10.1001/jama.2009.1269" target="_blank" title="It opens in new window">CrossRef
42. Wang X, Chen W, Hu F, Deng C, Zhou C, Lv X, Fan Y, Men J, Huang Y, Sun J, Hu D, Chen J, Yang Y, Liang C, Zheng H, Hu X, Xu J, Wu Z, Yu X (2011) / Clonorchis sinensis enolase: identification and biochemical characterization of a glycolytic enzyme from excretory/secretory products. Mol Biochem Parasitol 177:135-42 g/10.1016/j.molbiopara.2011.02.011" target="_blank" title="It opens in new window">CrossRef
43. WHO (2006) Report of the scientific working group on Chagas disease. UNDP/World Bank/WHO
44. WHO (2010) Chagas disease: control and elimination. UNDP/World Bank/WHO
45. Wilkins JC, Homer KA, Beighton D (2002) Analysis of / Streptococcus mutans proteins modulated by culture under acidic conditions. Appl Environ Microbiol 68:2382-390 g/10.1128/AEM.68.5.2382-2390.2002" target="_blank" title="It opens in new window">CrossRef
46. Wilson AP, Thelen JJ, Lakritz J, Brown CR, Marsh AE (2004) The identification of a sequence related to apicomplexan enolase from / Sarcocystis neurona. Parasitol Res 94:354-60 g/10.1007/s00436-004-1224-3" target="_blank" title="It opens in new window">CrossRef
47. Wizemann TM, Heinrichs JH, Adamou JE, Erwin AL, Kunsch C, Choi GH, Barash SC, Rosen CA, Masure HR, Tuomanen E, Gayle A, Brewah YA, Walsh W, Barren P, Lathigra R, Hanson M, Langermann S, Johnson S, Koenig S (2001) Use of a whole genome approach to identify vaccine molecules affording protection against / Streptococcus pneumoniae infection. Infect Immun 69:1593-598 g/10.1128/IAI.69.3.1593-1598.2001" target="_blank" title="It opens in new window">CrossRef
48. Yang J, Qiu C, Xia Y, Yao L, Fu Z, Yuan C, Feng X, Lin J (2010) Molecular cloning and functional characterization / of Schistosoma japonicum enolase which is highly expressed at the schistosomulum stage. Parasitol Res 107:667-77 g/10.1007/s00436-010-1913-z" target="_blank" title="It opens in new window">CrossRef - 作者单位：Alejandro Carabarín-Lima (1) (4)
Olivia Rodríguez-Morales (1)
María Cristina González-Vázquez (2) (5)
Lidia Baylón-Pacheco (3)
Pedro A. Reyes (1)
Minerva Arce-Fonseca (1)
José Luis Rosales-Encina (3)
1. Departamento de Biología Molecular, Instituto Nacional de Cardiología “Ignacio Chávez- Juan Badiano No. 1, Col. Sección XVI, Tlalpan, C.P. 14080, México, D. F., México
4. Centro de Investigaciones en Ciencias Microbiológicas, Benemérita Universidad Autónoma de Puebla, Puebla, 72550, México
2. Departamento de Biología Celular, Centro de Investigación y de Estudios Avanzados del I.P.N., México, D.F., 07360, México
5. Laboratorio de Neuroendocrinología, Instituto de Fisiología, Benemérita Universidad Autónoma de Puebla, Puebla, 72570, México
3. Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del I.P.N., México, D.F., 07360, México - ISSN：1432-1955
文摘
Nowadays, Chagas disease is a major health problem in Latin America that has been disseminated also into non-endemic countries. Currently, a vaccine against Chagas disease does not exist. In the present study, the gene encoding Trypanosoma cruzi enolase (TcENO) was amplified, cloned, and sequenced and the recombinant protein was purified. We used in silico and an experimental assay to investigate the immunological role of TcENO. The in silico assays showed that TcENO sequence contains characteristic motifs of enolase; additionally, a transmembranal region was identified, and this could indicate the potential membrane localization of TcENO. Moreover, both B lymphocyte and cytotoxic T lymphocytes (CTL) predicted epitopes were localized; these results suggest the possibility that TcENO can develop both humoral and cellular immune responses. Furthermore, the presence of antibodies was verified by western blot assays, showing that the purified recombinant protein was detected by sera from experimentally infected mice and sera of patients with Chagas disease. These results indicate that TcENO is immunogenic and could be used as a vaccine candidate.