A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype.

@article{Qiao1999ASP,
  title={A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype.},
  author={Hui-li Qiao and R. Todd Armstrong and Grigory B. Melikyan and Fredric Cohen and Judith M White},
  journal={Molecular biology of the cell},
  year={1999},
  volume={10 8},
  pages={
          2759-69
        }
}
We showed previously that substitution of the first residue of the influenza hemagglutinin (HA) fusion peptide Gly1 with Glu abolishes fusion activity. In the present study we asked whether this striking phenotype was due to the charge or side-chain volume of the substituted Glu. To do this we generated and characterized six mutants with substitutions at position 1: Gly1 to Ala, Ser, Val, Glu, Gln, or Lys. We found the following. All mutants were expressed at the cell surface, could be cleaved… CONTINUE READING
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