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.
Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Manidipa
M
Banerjee
Reza
R
Khayat
Hanna E
HE
Walukiewicz
Amy L
AL
Odegard
Anette
A
Schneemann
John E
JE
Johnson
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