Tissue-spanning redox gradient-dependent assembly of native human papillomavirus type 16 virions

J Virol. 2009 Oct;83(20):10515-26. doi: 10.1128/JVI.00731-09. Epub 2009 Aug 5.

Abstract

Papillomavirus capsids are composed of 72 pentamers reinforced through inter- and intrapentameric disulfide bonds. Recent research suggests that virus-like particles and pseudovirions (PsV) can undergo a redox-dependent conformational change involving disulfide interactions. We present here evidence that native virions exploit a tissue-spanning redox gradient that facilitates assembly events in the context of the complete papillomavirus life cycle. DNA encapsidation and infectivity titers are redox dependent in that they can be temporally modulated via treatment of organotypic cultures with oxidized glutathione. These data provide evidence that papillomavirus assembly and maturation is redox-dependent, utilizing multiple steps within both suprabasal and cornified layers.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Capsid / metabolism*
  • Capsid / physiology
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism
  • Cell Line
  • DNA, Viral / genetics
  • DNA, Viral / metabolism
  • Electroporation
  • Glutathione / metabolism
  • Glutathione / pharmacology
  • Human papillomavirus 16 / genetics
  • Human papillomavirus 16 / metabolism*
  • Human papillomavirus 16 / pathogenicity
  • Humans
  • Keratinocytes / metabolism*
  • Keratinocytes / virology
  • Mutagenesis, Site-Directed
  • Organ Culture Techniques
  • Oxidation-Reduction
  • Virion / genetics
  • Virion / metabolism*
  • Virion / pathogenicity
  • Virus Assembly*

Substances

  • Capsid Proteins
  • DNA, Viral
  • Glutathione