Influence of membrane composition on the binding and folding of a membrane lytic peptide from the non-enveloped flock house virus.

ABSTRACT: Using a combination of coarse-grained and atomistic molecular dynamics simulations we have investigated the membrane binding and folding properties of the membrane lytic peptide of Flock House virus (FHV). FHV is an animal virus and an excellent model system for studying cell entry mechanisms in non-enveloped viruses. FHV undergoes a maturation event where the 44 C-terminal amino acids are cleaved from the major capsid protein, forming the membrane lytic (γ) peptides. Under acidic conditions, γ is released from the capsid interior allowing the peptides to bind and disrupt membranes. The first 21 N-terminal residues of γ, termed γ₁, have been resolved in the FHV capsid structure and γ₁ has been the subject of in vitro studies. γ₁ is structurally dynamic as i

SUBMITTER: Nangia S 

PROVIDER: S-EPMC5482360 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature