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Dissecting the functional domains of a nonenveloped virus membrane penetration peptide

Academic Article
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Overview

authors

  • Banerjee, M.
  • Khayat, R.
  • Walukiewicz, H. E.
  • Odegard, A. L.
  • Schneemann, Anette
  • Johnson Jr., John

publication date

  • July 2009

journal

  • Journal of Virology  Journal

abstract

  • 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.

subject areas

  • Capsid Proteins
  • Cell Membrane
  • Mutation
  • Nodaviridae
  • Protein Structure, Tertiary
  • Virus Internalization
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Identity

PubMed Central ID

  • PMC2698515

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.02299-08

PubMed ID

  • 19369344
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Additional Document Info

start page

  • 6929

end page

  • 6933

volume

  • 83

issue

  • 13

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