Thesis
ESTUDIO E IDENTIFICACIÓN DE ANTÍGENOS VACUNALES DE Clostridium chauvoei
Autor
IBT. MARTÍNEZ GÓMEZ., ELIAN MIREILLE
Institución
Resumen
Diseases caused by Clostridium bacteria cause major economic losses in our country, and important institutions affecting livestock. In these diseases, severe necrotic processes are generated and / or sudden death, for bacterial growth and overproduction of toxins caused by physical trauma to the animal or by a change in diet. In our resea rch group we work on the design of new generation vaccines, among others, against clostridial myositis, where in a previous paper we obtained the recombinant flagellin of Clostridium chauvoei, which showed that it alone does not awakens a protective immune response in experimental animals. For this reason, the general objective of this work was to study the antigenic mosaic of C. chauvoei to identify potential vaccine antigens, using bioinformatic strategies and techniques to identify immunogenic molecules, such as Western Blot technique. Strains were studied from veterinary clinical isolates of Puebla and Veracruz, and with these strains we found five antigenic proteins whose molecular weights were 57, 49, 39, 25 and 15 kDa, which could then be evaluated as vaccine antigens. At the same time, we conducted a bioinformatic analysis of sialidase Nana C. chauvoei, because of its relevance in the pathogenesis of the disease. This was performed by homology modeling, using the structures of Nani and NanJ sialidase of Clostridium perfringens as templates, once counting on the structure, were determined which residues of the catalytic site of this enzyme could mutate, for decreased its catalytic ability and retained three-dimensional structure, resulting a mutant in residues R650T and D382H. In conclusion, we identified five potential vaccine candidates for C. chauvoei in strains of Black leg cases in Mexico. We performed in silico analysis of sialidase Nana resulting three-dimensional structure and the prediction of an active site mutant, which retained the structure of the wild sialidase and decreased interactions with the substrate.