PMID:24189547

Citation	Largo, E, Gladue, DP, Huarte, N, Borca, MV and Nieva, JL (2014) Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function. Antiviral Res. 101:30-6
Abstract	Viroporins are small integral membrane proteins functional in viral assembly and egress by promoting permeabilization. Blocking of viroporin function therefore constitutes a target for antiviral development. Classical swine fever virus (CSFV) protein p7 has been recently regarded as a class II viroporin. Here, we sought to establish the determinants of the CSFV p7 permeabilizing activity in a minimal model system. Assessment of an overlapping peptide library mapped the porating domain to the C-terminal hydrophobic stretch (residues 39-67). Pore-opening dependence on pH or sensitivity to channel blockers observed for the full protein required the inclusion of a preceding polar sequence (residues 33-38). Effects of lipid composition and structural data further support that the resulting peptide (residues 33-67), may comprise a bona fide surrogate to assay p7 activity in model membranes. Our observations imply that CSFV p7 relies on genus-specific structures-mechanisms to perform its viroporin function.
Links	PubMed Online version:10.1016/j.antiviral.2013.10.015
Keywords	Antiviral Agents/metabolism; DNA Mutational Analysis; Host-Pathogen Interactions; Membrane Proteins/genetics; Membrane Proteins/metabolism; Models, Biological; Models, Molecular; Pestivirus/genetics; Pestivirus/physiology; Viral Proteins/genetics; Viral Proteins/metabolism; Virus Assembly; Virus Release
edit table

Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
CSFVA:POLG	involved_in	GO:0039707: pore formation by virus in membrane of host cell	ECO:0000314: direct assay evidence used in manual assertion		P		Seeded From UniProt

References

See Help:References for how to manage references in GONUTS.