Abstract:
:The major outer capsid protein, VP5, of five US bluetongue viruses, was found to be glycosylated. Enzymatic removal of the carbohydrate moiety did not affect the electrophoretic mobility of VP5 in SDS-PAGE, indicating the presence of only short and possibly unbranched oligosaccharide chains. The surface accessibilities and immunogenic specificities of two conformational-dependent antigenic epitopes on VP5 of BTV were not affected by deglycosylation. Selective binding of those lectins which have well-defined sugar specificities suggests that the potential short N-linked carbohydrate chain present on BTV VP5 might be composed of sialic acid alpha(2-6)-N-acetylgalactosamine-beta(1-3)-galactose-beta(1-4)-N- acetylglucosamine-beta(1-2)-mannose-N-acetylglucosamine-Asn. In accordance with the standard nomenclature, BTV-VP5 should now be termed GP5 due to the presence of the carbohydrate moiety.
journal_name
Virologyjournal_title
Virologyauthors
Yang YY,Li JKdoi
10.1016/s0042-6822(83)90000-4subject
Has Abstractpub_date
1993-05-01 00:00:00pages
350-4issue
1eissn
0042-6822issn
1096-0341journal_volume
194pub_type
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