2004, Número 2
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Gac Med Mex 2004; 140 (2)
Hacia el desarrollo de una vacuna en contra de la cisticercosis porcina basada en la paramiosina de Taenia solium
Solís CF, Vázquez-Talavera J, Laclette JP
Idioma: Español
Referencias bibliográficas: 44
Paginas: 129-138
Archivo PDF: 791.38 Kb.
RESUMEN
La paramiosina de Taenia solium (TPmy) es un antígeno
inmunodominante de la cisticercosis humana y porcina. Se
trata de una proteína de 100 kDa con una estructura alfahélice
superenrollada asociada al músculo y a estructuras
tegumentarias del cisticerco. La TPmy tiene la propiedad
de unirse al C1q e inhibir la cascada del complemento. La
TPmy probablemente se une al C1q a través sus dominios
tipo colágena y podría estar relacionada con una estrategia
parasitaria para modular la respuesta inmune del huésped.
En el hombre y en el ratón, la respuesta inmune humoral en
contra de la TPmy está preferentemente dirigida hacia el extremo
carboxilo terminal mientras que el extremo amino terminal
de la TPmy induce una respuesta protectora celular de tipo Th1.
Ensayos de protección en el modelo murino de cisticercosis en
ratones inmunizados con fragmentos recombinantes de TPmy
revelaron que el extremo amino terminal induce alrededor de
60% de protección en contra de un reto intraperitoneal con
cisticercos de Taenia crassiceps. Ensayos preliminares de
protección por inmunización génica revelaron que el extremo
amino terminal de la TPmy clonado en un vector plasmídico
con un promotor de citomegalovirus induce alrededor de
79% de protección, junto con plásmidos para la expresión de
IL-12, sugiriendo que este tipo de inmunización con TPmy
puede resultar en el desarrollo de una vacuna eficaz y económica
en contra de la cisticercosis.
REFERENCIAS (EN ESTE ARTÍCULO)
Flisser A, Woodhouse E, Larralde C. Human cysticercosis: antigens, antibodies and non-responders. Clin Exp Immunol 1980;39:27-37.
Espinoza B, Ruiz-Palacios G, Tovar A, et al. Characterization by enzymelinked immunosorbent assay of the humoral immune response in patients with neurocysticercosis and its application in immunodiagnosis. J Clin Microbiol 1986;24:536-541.
Guerra G, Flisser A, Cañedo L, Laclette JP. Biochemical and immunological characterization of antigen B purified from cysticerci of Taenia solium. Cysticercosis: present state of knowledge and perspectives (edited by Flisser et al.). New York: Academic Press; 1982. p. 437-452.
Plancarte A, Flisser A, Larralde C. Fibronectin-like properties of antigen B from cysticerci of Taenia solium. 1982: In: Flisser A. et al.editors Cysticercosis: present state of knowledge and perspectives. New York: Academic Press.: 1982. p. 453-464.
Laclette JP, Alagón A, Willms K, Torre-Blanco A. Purification of antigen B from Taenia solium cysticerci by affinity to mammalian collagen. J Parasitol 1990;76:273-275.
Laclette JP, Merchant MT, Willms K. Histological and ultrastructural localization of antigen B in the metacestode of Taenia solium. J Parasitology 1987;73:121-129.
Lumsden RD. Histological studies on the absortive surface of cestode. II. The synthesis and intracellular transport of protein in the strobilar integument. Zeitschr Parasitenk 1966;28:1-13.
Trimble J, Lumsden RD. Cytochemical characterization of tegument membrane associated carbohydrates in Taenia crassiceps larvae. J Parasitol 1975;61:665-667.
Laclette JP, Rodríguez M, Landa A, Arcos L, de Alba P, Mancilla R, Willms K. The coexistence of Taenia solium cysticerci and the pig: role of antigen B. Acta Leidensis 1989;57:115-122.
Laclette JP, Skelly P, Merchant M, Shoemaker CB. Aldehyde fixation dramatically alters the immunolocalization pattern of paramyosin in helminth parasites. Exp Parasitol 1995;81:140-144.
Laclette JP, Landa A, Arcos L, Willms K, Davis, AE, Shoemaker CB. Paramyosin is the Schistosoma mansoni (Trematoda) homologue of antigen B from Taenia solium (Cestoda). Mol Biochem Parasitol 1991;44:287-295.
Landa A, Laclette JP, Nicholson-Weller A, Shoemaker CB. Taenia solium paramyosin (AgB): cDNA cloning and recombinant expression of collagen binding and complement inhibitor activity. Mol Biochem Parasitol 1993;60:343-347
Vargas-Parada L, Laclette JP. Gene structure of Taenia solium paramyosin. Parasitol Res 2003;89:375-378.
Cohen C, Parry DA, α-Helical coiled coils and bundles: how to design an α-helical protein. Prot Struct Funct Genet 1990;7:1-15.
Laclette JP, Shoemaker CB, Richter D, Arcos L, Pante N, Cohen C, Bing D, Nicholson-Weller A. Paramyosin inhibits complement C1. J Immunol 1992;148:124-128.
Kalinna B, McManus DP. An IgG (Fc gamma)-binding protein of Taenia crassiceps (Cestoda) exhibits sequence homology and antigenic similarity with schistosome paramyosin. Parasitology 1993;106:289-296.
Pearce EJ, James SL, Hieny S, Lanar DE, Sher A. Induction of protective immunity against Schistosoma mansoni by vaccination with schistosome paramyosin (Sm97), a nonsurface parasite antigen. Proc Natl Acad Sci USA 1988;85:5678-5682.
Flanigan TP, King CH, Lett RR, Nanduri J, Mahmoud AA. Induction of resistance to Schistosoma mansoni infection in mice by purified parasite paramyosin. J Clin Invest 1989;83:1010-1014.
Richter D, Incani RN, Harn DA. Isotype responses to candidate vaccine antigens in protective sera obtained from mice vaccinated with irradiated cercariae of Schistosoma mansoni. Infect Immun 1993;61:3003-3011.
Richter D, Reynolds SR, Harn DA. Candidate vaccine antigens that stimulate the cellular immune response of mice vaccinated with irradiated cercariae of Schistosoma mansoni. J Immunol 1993;151:256-265.
Yang W, Waine GJ, McManus DP. Antibodies to Schistosoma japonicum (Asian bloodfluke) paramyosin induced by nucleic acid vaccination. Biochem. Biophys. Res Commun 1995; 212:1029-1039.
McManus DP, Wong JY, Zhou J, Cai C, Zeng Q, Smyth D, Li Y, Kalinna BH, Duke MJ, Yi X. Recombinant paramyosin (rec-Sj-97) tested for immunogenicity and vaccine efficacy against Schistosoma japonicum in mice and water buffaloes. Vaccine 2001;20:870-878.
Nanduri J, Kazura JW. Paramyosin-enhanced clearance of Brugia malayi microfilaremia in mice. J Immunol 1999;143:3359-3363.
Li BW, Chandrashekar R, Weil GJ. Vaccination with recombinant filarial paramyosin induces partial immunity to Brugia malayi infection in birds. J Immunol 1993;150:1881-1885.
Nara T, Matsumoto N, Janecharut T, Matsuda H, Yamamoto K, Irimura T, Nakamura K, Aikawa M, Oswald I, Sher A, Kita K, Kojima S. Demonstration of the target molecule of a protective IgE antibody in secretory glands of Schistosoma japonicum larvae. Int Immunol 1994;6:963-971.
Correa-Oliveira R, Pearce EJ, Oliveira GC, et al. The human immune response to defined immunogens of Schistosoma mansoni: elevated antibody levels to paramyosin in stool-negative individuals from two endemic areas in Brazil. Trans Roy Soc Trop Med Hyg 1989;83:798-804.
Conraths FJ, Harnett MJ, Worms, MJ, Parkhouse RM. Immunological crossreaction between an Onchocercha paramyosin-like molecule and a microfilaria surface antigen. Trop Med Parasitol 1992;43:135-138.
Vázquez-Talavera J, Solís CF, Terrazas LI, Laclette JP. Characterization and protective potential of the immune response to Taenia solium paramyosin in a murine model of cysticercosis. Infect Immun 2001;69(9):5412-5416.
Sciutto E, Fragoso G, Trueba L, Lemus D, Montoya RM, Díaz ML, Govezensky T, Lomeli C, Tapia G, Larralde C. Cysticercosis vaccine: cross protecting immunity with Taenia solium antigens against experimental murine Taenia crassiceps cysticercosis. Parasite Immunol 1990;12:687-696.
Vázquez-Talavera J, Solís CF, Medina-Escutia E, López ZM, Proaño J, Correa D, Laclette JP. Human T and B cell epitope mapping of Taenia solium paramyosin. Parasite Immunol 2001;23:575-579.
Laemmli UK. Cleavage of structural proteins during assembly of the head of the bacteriophage T4. Nature 1970;227:680-685.
Tang DC, DeVit M, Johnston SA. Genetic immunization is a simple method for eliciting an immune response. Nature 1992;356:152-154.
Whitton JL, Rodríguez F, Zhang J, Hassett DE. DNA immunization: mechanistic studies. Vaccine 1999:(17);1612-1619.
Flo J, Pérez AB, Tisminetzky S, Baralle F. Superiority of intramuscular route and full length glycoprotein D for DNA vaccination against herpes simplex 2. Enhancement of protection by the co-delivery of the GM-CSF gene. Vaccine 2000;3242-3253.
Nara T, Tanabe K, Mahakunkijcharoen Y, Osada Y, Matsumoto N, Kita K, Kojima S. The B cell epitope of paramyosin recognized by a protective monoclonal IgE antibody to Schistosoma japonicum. Vaccine 1997;15:79-84.
Abraham R, Singh A, Mukhopadhyah SK, Basu V, Bal V, S. Rath. Modulation of immunogenicity and antigenicity of proteins by myelinization to target scavenger receptors on macrophages. J Immunol 1995;154:1-8.
Sciutto E, Fragoso G, Baca M, De la Cruz V, Lemus L, Lamoyi E. Depressed T-cell proliferation associated with susceptibility to experimental Taenia crassiceps infection. Infect Immun 1995;63:2277-2281.
Villa OF, Kuhn RE. Mice infected with the larvae of Taenia crassiceps exhibit a Th2-like immune response with concomitant anergy and down regulation of Th1-associated phenomena. Parasitology 1996;112:561-570.
Terrazas LI, Cruz M, Rodríguez-Sosa M, Bojalil R, García-Tamayo FY, Larralde C. Th1-type cytokines improve resistance to murine cysticercosis caused by Taenia crassiceps. Parasitol Res 1999;85:135-141.
Sher A, Pearce E, Hieny S, James S. Induction of protective immunity against Schistosoma mansoni by a nonliving vaccine. IV. Fractionation and antigenic properties of a soluble adult worm immunoprophylactic activity. J Immunol 1986;136:3878-3883.
Kojima S, Janecharut H, Hata H, Niimura Y. Role of a mouse monoclonal IgE antibody in passive transfer of immunity to Schistosoma mansoni infection. Mem Inst Oswaldo Cruz Rio J 1987;82:237-241.
Chen H, Nara T, Zeng X, Satoh M, Wu G, Jiang W, Yi F, Kojima S, Zhang S, Hirayama K. Vaccination of domestic pig with recombinant paramyosin. against Schistosoma japonicum in China. Vaccine 2000;18:2142-2146.
Nanduri J, Kazura JW. Paramyosin-enhanced clearance of Brugia malayi microfilaremia in mice. J Immunol 1989;143:3359-3363.
Wisnewski AV, Kresina TF. Induction of protective immunity to schistosomiasis with immunologically cross-reactive Lumbricus molecules. Int J Parasitol 1995;25:503-510.