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M Tesar

Publications and source records attributed to M Tesar.

20 records · Page 2Linked to original sources

Identification of foot-and-mouth disease virus replication in vaccinated cattle by antibodies to non-structural virus proteins.

Antibodies raised in cattle against foot-and-mouth disease virus by vaccination or by experimental infection were distinguished. Vaccination elicited only antibodies to virus capsid proteins and the polymerase 3D. Virus replication in cattle elicited additional antibodies directed against the non-structural proteins 2B, 2C, 3AB1, and/or 3C irrespective of prior vaccination or whether the cattle exhibited symptoms of disease. Non-permissive mice inoculated with virus responded in the same way, indicating that antibodies raised due to the transient presence of antigen are safely recognized by the method applied which was radioimmunoprecipitation. All kinds of infections were thus detected and it was possible to differentiate between cattle exposed or not exposed to challenge in the field, and further between protected animals and possible virus carriers.

Animals↗

Serological probes for some foot-and-mouth disease virus nonstructural proteins.

Foot-and-mouth disease virus (FMDV) O1 Kaufbeuren-specific cDNA fragments were subcloned into the E. coli expression vector pRIT.2T. Fusion proteins thus produced in bacteria were purified by affinity chromatography and inoculated into rabbits. Three sera thus obtained were found to be monospecific for FMDV proteins 3A, 3C, and 3D, respectively. Two others were prevalently directed against protein 2C, but in addition, either to protein 2B or to protein 3A. Five out of six mature nonstructural virus proteins can therefore be separately investigated in FMDV-infected cells, either by indirect immunofluorescence or by radioimmunoprecipitation. Immunofluorescence shows all investigated proteins to be located exclusively in the cytoplasm. One of them, protein 2C, transiently forms aggregates at the periphery of cells. Radioimmunoprecipitation confirmed current knowledge on maturation of FMDV proteins. It was further used to characterize postinfectional sera with regard to FMDV-specific antibodies. Cattle and guinea pig were found to have responded differently to FMDV nonstructural antigens. Furthermore, antigenicity of yet to be described FMDV polypeptides was observed in the guinea pig.

Animals↗