PMID: 3753607Jan 1, 1986Paper

Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus

The Journal of Cell Biology
M J GethingJ M White

Abstract

Oligonucleotide-directed mutagenesis of a cDNA encoding the hemagglutinin of influenza virus has been used to introduce single base changes into the sequence that codes for the conserved apolar "fusion peptide" at the amino-terminus of the HA2 subunit. The mutant sequences replaced the wild-type gene in SV40-HA recombinant virus vectors, and the altered HA proteins were expressed in simian cells. Three mutants have been constructed that introduce single, nonconservative amino acid changes in the fusion peptide, and three fusion phenotypes were observed: substitution of glutamic acid for the glycine residue at the amino-terminus of HA2 abolished all fusion activity; substitution of glutamic acid for the glycine residue at position 4 in HA2 raised the threshold pH and decreased the efficiency of fusion; and, finally, extension of the hydrophobic stretch by replacement of the glutamic acid at position 11 with glycine yielded a mutant protein that induced fusion of erythrocytes with cells with the same efficiency and pH profile as the wild-type protein. However, the ability of this mutant to induce polykaryon formation was greatly impaired. Nevertheless, all the mutant proteins underwent a pH-dependent conformational change and bou...Continue Reading

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Citations

Aug 2, 2014·Proceedings of the National Academy of Sciences of the United States of America·Xingcheng LinJosé N Onuchic
Aug 1, 1996·The Journal of Cell Biology·M KielianW A Duffus
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Feb 5, 2008·Colloids and Surfaces. B, Biointerfaces·Shinpei Ohki, Klaus Arnold

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