A Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading.

ABSTRACT: Synthetic peptides derived from the heptad repeat (HR) of fusion (F) proteins can be used as dominant negative inhibitors to inhibit the fusion mechanism of class I viral F proteins. Here, we have performed a stapled-peptide scan across the HR2 domain of the respiratory syncytial virus (RSV) F protein with the aim to identify a minimal domain capable of disrupting the formation of the postfusion six-helix bundle required for viral cell entry. Constraining the peptides with a single staple was not sufficient to inhibit RSV infection. However, the insertion of double staples led to the identification of novel short stapled peptides that display nanomolar potency in HEp-2 cells and are exceptionally robust to proteolytic degradation. By replacing each amino acid of the peptides by an alanine,

SUBMITTER: Gaillard V 

PROVIDER: S-EPMC5365662 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature