Open AccessSide Chain Packing below the Fusion Peptide Strongly Modulates Triggering of the Hendra Virus F Protein
Author(s) -
Everett Clinton Smith,
Rebecca Ellis Dutch
Publication year - 2010
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01108-10
Subject(s) - hendra virus , heptad repeat , biology , lipid bilayer fusion , peptide , asparagine , histidine , fusion protein , mutant , microbiology and biotechnology , fusion , virus , cell fusion , biophysics , biochemistry , peptide sequence , amino acid , virology , cell , ebola virus , gene , recombinant dna , linguistics , philosophy
Triggering of the Hendra virus fusion (F) protein is required to initiate the conformational changes which drive membrane fusion, but the factors which control triggering remain poorly understood. Mutation of a histidine predicted to lie near the fusion peptide to alanine greatly reduced fusion despite wild-type cell surface expression levels, while asparagine substitution resulted in a moderate restoration in fusion levels. Slowed kinetics of six-helix bundle formation, as judged by sensitivity to heptad repeat B-derived peptides, was observed for all H372 mutants. These data suggest that side chain packing beneath the fusion peptide is an important regulator of Hendra virus F triggering.