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Identification of epitope(s) on the internal virion proteins of rinderpest virus which are absent from peste des petits ruminants virus

Identifieur interne : 002666 ( Main/Exploration ); précédent : 002665; suivant : 002667

Identification of epitope(s) on the internal virion proteins of rinderpest virus which are absent from peste des petits ruminants virus

Auteurs : Kenneth C. Mccullough [Royaume-Uni, Suisse] ; Timothy U. Obi [Royaume-Uni, Nigeria] ; Hooshmand Shesberadaran [Royaume-Uni, Suède]

Source :

RBID : ISTEX:2C3FDC90196920057E59E5E581BF243E566F7FCA

Abstract

Monoclonal antibodies (MAb) raised against the RBOK vaccine strain of rinderpest virus were characterized by radio-immunoprecipitation (RIPA) and in the indirect ELISA using measles (MV), distemper (CDV), rinderpest (RPV) and peste des petits ruminants viruses (PPRV). Those found to be specific for the matrix (M) protein and the nucleocapsid (N) protein could be classified into different groups on the basis of the anti-morbillivirus MAb classification scheme: a number of these MAb showed a selective recognition of RPV, measles virus and distemper virus, or of different isolates of rinderpest virus, demonstrating that greater inter-isolate variation occurs than was apparent from analyses using polyclonal antisera. One group of anti-F protein MAb (group F1) reacted with all isolates of both RPV and PPRV. A second group of anti-N protein MAb (group N1/A) reacted with all RPV isolates, but not with the PPRV isolates. Furthermore, these group N1/A antibodies reacted strongly with RPV isolates which were upon original isolation of high pathogenicity, but had a weaker reaction against the isolates of this virus which were of low pathogenicity. Thus, MAb against RPV, in particular those against the N protein offered a potential superior to that of molecular analyses for “isolate fingerprinting”, the differentiation of RPV from PPRV and the discrimination between rinderpest viruses which had been, upon isolation, of either high or low pathogenicity.

Url:
DOI: 10.1016/0378-1135(91)90025-B


Affiliations:


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