Peptides Interfering 3A Protein Dimerization Decrease FMDV Multiplication

• DOI: 10.1371/journal.pone.0141415
• Publication Date: 2015-10-27T18:45:31Z
• Authors: Mónica González-M...; Ángela Vázquez-Calvo; Beatriz G. de la ...; Javier Valle; David Andreu; Francisco Sobrino
• Keywords: Viral protein

Nonstructural protein 3A is involved in relevant functions foot-and-mouth disease virus (FMDV) replication. FMDV can form homodimers and preservation of the two hydrophobic α-helices (α1 α2) that stabilize dimer interface essential for In this work, small peptides mimicking residues were used to interfere with dimerization thus gain insight on its biological function. The α1, α2 spanning α-helices, α12, impaired vitro formation a peptide containing effect being higher α12. To assess inhibition cultured cells, interfering N-terminally fused heptaarginine (R7) sequence favor their intracellular translocation. Thus, when R7, interference (100 μM) able inhibit transiently expressed 3A, inhibitions found α1 impairment exerted by correlated significant, specific reductions viral yield recovered from peptide-treated infected cells. case, was only producing significant at concentrations lower than 100 μM. constitute tool understand structure-function relationship point as potential antiviral target.