Analysis of radioactively labelled and highly purified infectious lymphocytic choriomeningitis (LCM) virus by polyacrylamide gel electrophoresis (PAGE) revealed 12 components which, according to their apparent molecular weight and glycosylation status, were designated as p19, p25, p26, gp35, p38, gp44, gp60, p63, p77, gp85, gp130, and p200. As shown by immunoprecipitation, they all bound to rabbit anti-LCM virus antibodies. Three proteins, namely gp35 (= ‘GP-2’), gp44 (= ‘GP-1’) and p63 (= ‘NP’), had previously been described by others as major constituents of the virion. Our results confirm this and suggest that gp60, p77, gp85, and p200 are further distinct structural proteins. In contrast, p25 and p38 appear to be cleavage or degradation products of p63; p19 and p26 seem to belong to gp60, which could be the monomeric form of a dimer, gp130. Peptide mapping by limited proteolysis revealed considerable overlapping of amino acid sequences among the major glycoproteins with one peptide being common to all. From the results of PAGE performed after external labelling of intact virions, we conclude that gp44, gp60, and gp85 (but not gp35) form the surface of the virus envelope. Analytical isoelectric focusing under non-reducing conditions has shown that the major glycoproteins appeared to consist of several components with different isoelectric points.

Keyword(s): glycoproteins , LCM virus and proteins

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