volume 66, issue 8, P4940-4950 1992
DOI: 10.1128/jvi.66.8.4940-4950.1992
View full text
|
|
Share
G W Kemble, D L Bodian, J Rosé, I A Wilson, J M White

Abstract: At a low pH, the influenza virus hemagglutinin (HA) undergoes conformational changes that promote membrane fusion. While the critical role of fusion peptide release from the trimer interface has been demonstrated previously, the role of globular head dissociation in the overall fusion mechanism remains unclear. To investigate this question, we have analyzed in detail the fusion activity and low pH-induced conformational changes of a mutant, Cys-HA, in which the globular head domains are locked together by engi…

expand abstract