Dissecting the functional domains of a nonenveloped virus membrane penetration peptide.
Recent studies have established that several nonenveloped viruses utilize virus-encoded lytic peptides for host membrane disruption. We investigated this mechanism with the "gamma" peptide of the insect virus Flock House virus (FHV). We demonstrate that the C terminus of gamma is essential for membrane disruption in vitro and the rescue of immature virus infectivity in vivo, and the amphipathic N terminus of gamma alone is not sufficient. We also show that deletion of the C-terminal domain disrupts icosahedral ordering of the amphipathic helices of gamma in the virus. Our results have broad implications for understanding membrane lysis during nonenveloped virus entry.
Banerjee
Manidipa
M
Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Khayat
Reza
R
Walukiewicz
Hanna E
HE
Odegard
Amy L
AL
Schneemann
Anette
A
Johnson
John E
JE
D036022:Capsid Proteins / Q000235:genetics*; D002462:Cell Membrane / Q000821:virology*; D009154:Mutation; D030381:Nodaviridae / Q000235:genetics / Q000502:physiology*; D017434:Protein Structure, Tertiary; D053586:Virus Internalization
D036022:Capsid Proteins