Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity
AUTOR(ES)
Steinhauer, David A.
FONTE
The National Academy of Sciences of the USA
RESUMO
Amino acid substitutions widely distributed throughout the influenza hemagglutinin (HA) influence the pH of its membrane fusion activity. We have combined a number of these substitutions in double mutants and determined the effects on the pH of fusion and on the pH at which the refolding of HA required for fusion occurs. By analyzing combinations of mutations in three regions of the metastable neutral-pH HA that are rearranged at fusion pH we obtain evidence for both additive and nonadditive effects and for an apparent order of dominance in the effects of amino acid substitutions in particular regions on the pH of fusion. We conclude that there are at least three components in the structural transition required for membrane fusion activity and consider possible pathways for the transition in relation to the known differences between neutral and fusion pH HA structures.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=24013Documentos Relacionados
- Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin.
- Conformational Intermediates and Fusion Activity of Influenza Virus Hemagglutinin
- Oligosaccharides in the stem region maintain the influenza virus hemagglutinin in the metastable form required for fusion activity.
- Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density.
- Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatment.