ABSTRACT
Boophilus annulatus is an obligate blood feeder tick that can cause great losses in animals due to anemia and its ability to injure its host skin directly. The aim of this study was identification of cattle humoral immune response to some tick proteins during experimental infestation. Immune sera against tick were collected from experimentally infested cattle with ticks. One and two-dimensional electrophoresis and Western blotting methods were used for the detection of immunogenic proteins in larval tick extract and eight of these proteins were identified by MALDI-TOF and MALDI-TOF-TOF mass spectrometry. In non-reducing one-dimensional SDS-PAGE, some bounds between 12 to more than 250-kDa appeared. In two-dimensional SDS-PAGE, numerous spot appeared and the identified immunogenic proteins by parallel immunoblotting weighted between 14 and 97 kDa. Amino acid sequences of protein spot with 37-kDa molecular weight had identity to tropomyosin based on Mascot search in NCBI. Anti tropomyosin antibodies can be induced in experimentally infested hosts with ticks and it seems that tropomyosin can be useful for the development of anti tick vaccines.
Subject(s)
Animals , Tropomyosin/immunology , Ticks , Vaccines , Cattle , Immunity, HumoralABSTRACT
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 alfa-hélice 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.
Taenia solium paramyosin (TPmy) is a prominent 100 kDa antigen in human and porcine cysticercosis. TPmy is an α-helical coiled coil protein present in muscle and tegumentary structures of T. solium cysticerci. TPmy has the property of binding C1q resulting in inhibition of the complement cascade. TPmy probably binds C1q through its collagen-like domains and could be involved in a parasite strategy to modulate host immune response. Humoral immune response against TPmy is preferentially directed against carboxyl terminal end in humans and mice, whereas amino terminal end of TPmy preferentially induces a Th1-related cellular immune response. Protection studies in murine model of cysticercosis showed that the amino terminal end fragment of TPmy induces approximately 60% protection against an i.p. challenge with Taenia crassiceps cysts when mice are immunized with recombinant fragments of TPmy. Initial protection studies using genetic immunization showed that amino terminal end fragment of TPmy cloned into a plasmid expression vector with a cytomegalovirus promoter, together with IL-12-expressing plasmids induced 79% protection, suggesting that this kind of TPmy-immunization might result in development of a cost-effective vaccine against cysticercosis.
Subject(s)
Animals , Female , Mice , Cysticercosis/prevention & control , Cysticercosis/veterinary , Swine Diseases/prevention & control , Vaccines/immunology , Antigens, Helminth/immunology , Mice, Inbred BALB C , Taenia solium/immunology , Tropomyosin/immunologyABSTRACT
Seis pacientes que consultaron por síntomas respiratorios alérgicos (RSP y ASMA) diagnosticados por Skin prick test (SPT), fueron tratados con inmunoterapia específica (SIT) para ácaros por un lapso promedio de 23,3 meses. Tres (N2, N4 y N5) referían a su ingreso, síntomas leves a la ingesta de mariscos y se hizo SPT e IgE específica por Radio Allergo Sorbent Test (RAST) para "pool" de mariscos antes de la SIT. Ante la aparición y/o intensificación de síntomas en estos 6 pacientes por ingesta de frutos de mar luego de SIT prolongada, se realizó RAST clase 1 y 2 para N4 y N2; y N1 entre clase 0 y 1 (0,35 PRU/ml). El SPT de N2 se mantuvo positivo y el de N5 negativo, tal como antes de SIT. Sólo N4 cambió a SPT positivo al "pool" de marisco. Doce controles asintomáticos con SIT similares fueron negativos a la provocación oral, al SPT y al RAST. La presencia de un antígeno común a ambos alergenos (tropomiosina) al ser administrado en SIT para ácaros, provocaría una sensibilización nueva o aumentada en estos pacientes aunque no se pudo descartar sensibilización por ingesta habitual de mariscos
Subject(s)
Humans , Mites/immunology , Cross Reactions/immunology , Desensitization, Immunologic , Food Hypersensitivity/etiology , Shellfish/adverse effects , Food Hypersensitivity/immunology , Tropomyosin/adverse effects , Tropomyosin/immunologyABSTRACT
A Schistosoma mansoni adult worm anionic fraction (PIII) has previously been shown to protect mice against challenge infection and to reduce pulmonary and hepatic granulomatous hypersensitivity. Serum from PIII-immunized rabbit was used to screen a gt11 cDNA library from S. mansoni adult worm in order to identify antigens capable of modulating granulomatous hypersensitivity. We obtained four clones with 400 (Sm-III.11), 900 (Sm-III.16), 1100 (Sm-III.10) and 1300 (Sm-III.12) bp of length. All clone-specific antibodies were able to recognize most of the PIII components. The sequence analysis showed that these clones presented high homology with S. mansoni paramyosin (Sm-97). These findings describe a new function to this antigen with an important role in modulation of granulomatous hypersensitivity to S. mansoni eggs.