The synthesis of caprine arthritis-encephalitis virus structural proteins was analysed in infected cells labelled with [S]methionine and [H]glucosamine and by translation of virion RNA . Viral polypeptides were isolated from infected cell lysates or from translation products by immunoprecipitation with specific antisera and resolved by SDS-PAGE. Results indicated that the gene-encoded p28, p19 and p16 virion core proteins were formed by cleavage processing of a 55K precursor with several intermediate polypeptides. The gp135 virion surface glycoprotein, encoded by the gene, was formed by post-translational modification of a glycosylated precursor of 150K apparent . This precursor was formed by glycosylation of a 90K primary gene product.

Keyword(s): CAEV , lentivirus and structural proteins

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