Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution

Benes L. Trus, Richard S Roden, Heather L. Greenstone, Michael Vrhel, John T. Schiller, Frank P. Booy

Research output: Contribution to journalArticle

Abstract

The three-dimensional structure of bovine papillomavirus has been determined to 9 Å resolution by reconstruction of high resolution, low dose cryo-electron micrographs of quench-frozen virions. Although hexavalent and pentavalent capsomeres form star-shaped pentamers of the major capsid protein L1, they have distinct high-resolution structures. Most prominently, a 25 Å hole in the centre of hexavalent capsomeres is occluded in the pentavalent capsomeres. This raises the possibility that the L2 minor capsid protein is located in the centre of the pentavalent capsomeres. Intercapsomere connections ~10 Å in diameter were clearly resolved. These link adjacent capsomeres and are reminiscent of the helical connections that stabilize polyomavirus.

Original languageEnglish (US)
Pages (from-to)413-420
Number of pages8
JournalNature Structural Biology
Volume4
Issue number5
StatePublished - May 1997
Externally publishedYes

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Capsid
Capsid Proteins
Polyomavirus
Virion
Stars
Electrons

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution. / Trus, Benes L.; Roden, Richard S; Greenstone, Heather L.; Vrhel, Michael; Schiller, John T.; Booy, Frank P.

In: Nature Structural Biology, Vol. 4, No. 5, 05.1997, p. 413-420.

Research output: Contribution to journalArticle

Trus, Benes L. ; Roden, Richard S ; Greenstone, Heather L. ; Vrhel, Michael ; Schiller, John T. ; Booy, Frank P. / Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution. In: Nature Structural Biology. 1997 ; Vol. 4, No. 5. pp. 413-420.
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