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Journal of Virology, July 2009, p. 6929-6933, Vol. 83, No. 13
0022-538X/09/$08.00+0 doi:10.1128/JVI.02299-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037,1 Department of Chemistry and Biochemistry, University of California—San Diego, La Jolla, California 920932
Received 3 November 2008/ Accepted 9 April 2009
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.
Published ahead of print on 15 April 2009.
# Present address: Department of Cell and Developmental Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801.
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