Journal
JOURNAL OF VIROLOGY
Volume 79, Issue 18, Pages 12065-12076Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.79.18.12065-12076.2005
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Funding
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI030557, R37AI030557] Funding Source: NIH RePORTER
- NIAID NIH HHS [R01 AI030557, R37 AI030557, AI30557] Funding Source: Medline
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Influenza virus hemagglutinin (RA)-mediated membrane fusion is initiated by a conformational change that releases a V-shaped hydrophobic fusion domain, the fusion peptide, into the lipid bilayer of the target membrane. The most N-terminal residue of this domain, a glycine, is highly conserved and is particularly critical for HA function; G1S and G1N mutant HAs cause hemifusion and abolish fusion, respectively. We have determined the atomic resolution structures of the G1S and GIN mutant fusion domains in membrane environments. G1S forms a V with a disrupted glycine edge on its N-terminal arm and G1V adopts a slightly tilted linear helical structure in membranes. Abolishment of the kink in G1V results in reduced hydrophobic penetration of the lipid bilayer and an increased propensity to form P-structures at the membrane surface. These results underline the functional importance of the kink in the fusion peptide and suggest a structural role for the N-terminal glycine ridge in viral membrane fusion.
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