PRODUCTION AND PURIFICATION OF RECOMBINANT PROTEIN HN OF THE PORCINE RUBULAVIRUS AS A CANDIDATE FOR AN IMMUNOGEN IN PIGS Rocío Lara-Romero1, José Luis Cerriteño-Sánchez4, Sandra Cuevas-Romero3, Humberto Ramírez-Mendoza2, Eliseo Hernandez1, Susana Mendoza1. 1 2 FES-Cuautitlán. UNAM. México. Facultad de Medicina Veterinaria y Zootecnia. UNAM. México. 3CENID-Microbiología Animal. INIFAP. México. 4Benémerita Universidad Autónoma de Puebla. México.
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Introduction In 1980, the pig farms located in La Piedad, Michoacan, México a new Paramyxoviridae was isolated and latter classified as porcine Rubulavirus (PorPV) and the disease was named Blue Eye Syndrome. There are more than 16 million pigs in at least one third of them are affected. The disease is concentrated in the central states of México. In newborn pigs, 19% of the animals are born dead or mummified and of those born alive; up to 50% are killed by the PorPV. The virus is an RNA one that codifies six structural proteins (NP, L, M, F HN and P). The most immunogenic of the proteins is HN which is capable of eliciting neutralizing antibodies. In SDS-PAGE, it has a MW of 60 kDa. Our aim was to purify a high amount of a previously developed bacterial clone with the recombinant protein and evaluate it as a candidate immunogen for pigs.
Table 1. Amount (ug/ul) of inclusion bodies obtained from two strains of E. coli. By the Student T test it was determined that the highest producer of intracellular inclusion bodies was the E. coli BL21 strain (P=
