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J Gen Virol 69 (1988), 675-681; DOI 10.1099/0022-1317-69-3-675
© 1988 Society for General Microbiology

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Precursor Polypeptides of Caprine Arthritis-Encephalitis Lentivirus Structural Proteins

William P. Cheevers1, Theresa A. Stem1, Donald P. Knowles2 and Travis C. McGuire1

1 Department of Veterinary Microbiology and Pathology
and2 U.S. Department of Agriculture, Animal Disease Research Unit, Washington State University, Pullman, Washington 99164, U.S.A.

The synthesis of caprine arthritis-encephalitis virus structural proteins was analysed in infected cells labelled with [35S]methionine and [3H]glucosamine and by translation of virion RNA in vitro. Viral polypeptides were isolated from infected cell lysates or from in vitro translation products by immunoprecipitation with specific antisera and resolved by SDS-PAGE. Results indicated that the gag gene-encoded p28, p19 and p16 virion core proteins were formed by cleavage processing of a 55K Mr precursor with several intermediate polypeptides. The gp135 virion surface glycoprotein, encoded by the env gene, was formed by post-translational modification of a glycosylated precursor of 150K apparent Mr. This precursor was formed by glycosylation of a 90K primary env gene product.

Keywords: CAEV, lentivirus, structural proteins

Received 15 September 1987; accepted 18 November 1987.


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Monoclonal Antibodies to Conformational Epitopes of the Surface Glycoprotein of Caprine Arthritis-Encephalitis Virus: Potential Application to Competitive-Inhibition Enzyme-Linked Immunosorbent Assay for Detecting Antibodies in Goat Sera
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