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Published January 15, 1982 | public
Journal Article

Association of Sindbis Virion Glycoproteins and their Precursors

Abstract

We have studied the association of the Sindbis virus glycoproteins in mature virions and infected cells. The glycoproteins were cross-linked with bifunctional amino-reactive reagents (11 Å cross-linking distance), some of which could be subsequently cleaved by reduction. Using monospecific rabbit antisera against each viral envelope glycoprotein it was found that >90% of the cross-linked glycoprotein dimers from intact virions or virions solubilized with Triton X100 prior to cross-linking were heterodimers of E1 and E2. The pattern of cross-linked glycoproteins from intact virions as well as infected cells suggested that three E1-E2 dimers may be associated to form a hexameric subunit. Cross-linking of pulselabeled infected monolayers showed that PE2 was cross-linked to E1 less efficiently than was E2, suggesting that if PE2 and E1 are associated as a complex in infected cells then their conformation with respect to reactive amino groups is distinct from that of the mature virion glycoproteins. ts mutants of Sindbis virus in the complementation groups corresponding to E1 and PE2 fail to cleave PE2 at the non-permissive temperature (40 °C). In monolayers infected with these mutants or a heat-resistant variant of Sindbis virus, the glycoprotein precursors synthesized at the elevated temperature were readily cross-linked into large aggregates, indicating a temperature-sensitive tendency for the proteins to aggregate.

Additional Information

© 1982 Academic Press Inc. (London) Ltd. Received 2 July 1981. We thank Edith Lenches for preparing the CEF and BHK-21 monolayers. This work was supported by grant PCM 80-22830 from the National Science Foundation, and by grants GM06965 and AI10793 from the National Institutes of Health. One author (C.M.R.) was supported by Training grant GM 00086 from NIH.

Additional details

Created:
August 19, 2023
Modified:
October 18, 2023