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. 1982 Feb;79(4):968–972. doi: 10.1073/pnas.79.4.968

Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion.

J J Skehel, P M Bayley, E B Brown, S R Martin, M D Waterfield, J M White, I A Wilson, D C Wiley
PMCID: PMC345880  PMID: 6951181

Abstract

A conformational change in the hemagglutinin glycoprotein of influenza virus has been observed to occur to pH values corresponding to those optimal for the membrane fusion activity of the virus. CD, electron microscopic, and sedimentation analyses show that, in the pH range 5.2-4.9, bromelain-solubilized hemagglutinin (BHA) aggregates as protein-protein rosettes and acquires the ability to bind both lipid vesicles and nonionic detergent. Trypsin treatment of BHA in the pH 5.0-induced conformation indicates that aggregation is a property of the BHA2 component and that the conformation change also involves BHA1. The implications of these observations for the role of the glycoprotein in membrane fusion are discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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