Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers
- PMID: 12083843
- DOI: 10.1006/viro.2002.1429
Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers
Abstract
Rabies virus-induced membrane fusion is triggered at low pH and is mediated by the trimeric viral glycoprotein (G). G assumes three conformations: the native state (N) detected above pH 7; the activated state (A), which initiates the fusion process; and the fusion-inactive conformation (I) observed after prolonged incubation at low pH. Differently from other viral fusogenic glycoproteins, G in the I state recovers its native conformation when reincubated above pH 7. Here, we demonstrate that there is a thermodynamic equilibrium between the different states of G between pH 6 and pH 7.5. The study of this equilibrium at various pH values indicated that the conformational change toward I is induced by the protonation of at least three residues per trimer. Finally, studies on the mechanism leading to low pH induced fusion inactivation indicated that a large number of G molecules is required for stable hydrophobic interaction of the virus with the target membrane.
(c) 2002 Elsevier Science (USA).
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