Receptor-triggered membrane association of a model retroviral glycoprotein

Rachel L. Damico, Joanne Crane, Paul Bates

Research output: Contribution to journalArticlepeer-review

Abstract

Current models of retroviral entry hypothesize that interactions between the vital envelope protein and the host receptor(s) induce conformational changes in the envelope protein that activate the envelope protein and initiate fusion. We employed a liposome-binding assay to demonstrate directly and characterize the activation of a model retroviral envelope protein (EnvA) from Rous sarcoma virus (RSV). In the presence of purified vital receptor, the trimeric ectodomain of EnvA was converted from a water-soluble form to a membrane-associated form, consistent with conversion of the envelope protein to its fusogenic state. This activation was nonlinear with respect to receptor concentration, suggesting cooperativity within the trimeric envelope protein. The activated EnvA was stably associated with the target membrane through hydrophobic interactions, behaving like an intrinsic membrane protein. The ability of EnvA to associate with membrane was coincident with a loss of receptor-binding activity, suggesting that during viral entry activated EnvA dissociates from the receptor to facilitate membrane fusion. These results provide direct evidence that receptor binding triggers conversion of the EnvA protein to a membrane-binding form, illustrating that RSV is a useful model for the study of retroviral entry and activation of pH- independent fusion proteins.

Original languageEnglish (US)
Pages (from-to)2580-2585
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number5
DOIs
StatePublished - Mar 3 1998
Externally publishedYes

ASJC Scopus subject areas

  • General

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