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Viral capsid mobility: A dynamic conduit for inactivation

Academic Article
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Overview

authors

  • Broo, K.
  • Wei, J.
  • Marshall, D.
  • Brown, F.
  • Smith, T. J.
  • Johnson Jr., John
  • Schneemann, Anette
  • Siuzdak, Gary

publication date

  • February 2001

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Mass spectrometry and fluorescent probes have provided direct evidence that alkylating agents permeate the protein capsid of naked viruses and chemically inactivate the nucleic acid. N-acetyl-aziridine and a fluorescent alkylating agent, dansyl sulfonate aziridine, inactivated three different viruses, flock house virus, human rhinovirus-14, and foot and mouth disease virus. Mass spectral studies as well as fluorescent probes showed that alkylation of the genome was the mechanism of inactivation. Because particle integrity was not affected by selective alkylation (as shown by electron microscopy and sucrose gradient experiments), it was reasoned that the dynamic nature of the viral capsid acts as a conduit to the interior of the particle. Potential applications include fluorescent labeling for imaging viral genomes in living cells, the sterilization of blood products, vaccine development, and viral inactivation in vivo.

subject areas

  • Animals
  • Aphthovirus
  • Aziridines
  • Capsid
  • Drosophila melanogaster
  • Mechlorethamine
  • RNA Viruses
  • Rhinovirus
  • Spectrometry, Mass, Electrospray Ionization
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Identity

PubMed Central ID

  • PMC30128

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.051598298

PubMed ID

  • 11226229
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Additional Document Info

start page

  • 2274

end page

  • 2277

volume

  • 98

issue

  • 5

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