The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics.

ABSTRACT: A peptide comprising no fewer than the first 20 residues of the influenza hemagglutinin HA2 subunit suffices to induce lipid mixing between the membranes of different unilamellar vesicles. This 20-residue peptide was previously reported to adopt an open "boomerang" structure that differs significantly from the closed helical-hairpin structure of a fusion peptide consisting of the first 23 residues of the HA2 sequence. This study investigates the structural and dynamic features of fusion peptides of different length and subtype. Lacking key interactions that stabilize the closed, helical-hairpin structure, the 20-residue peptide is in a dynamic equilibrium between closed and open states, adopting a ca. 11% population of the former when solubilized by DPC micelles. Peptides shorter than 20 r

SUBMITTER: Lorieau JL 

PROVIDER: S-EPMC3532579 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature