The structure of avian polyomavirus reveals variably sized capsids, non-conserved inter-capsomere interactions, and a possible location of the minor capsid protein VP4

Peter S. Shen, Dirk Enderlein, Christian D S Nelson, Weston S. Carter, Masaaki Kawano, Li Xing, Robert D. Swenson, Norman H. Olson, Timothy S. Baker, R. Holland Cheng, Walter J. Atwood, Reimar Johne, David M. Belnap

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Avian polyomavirus (APV) causes a fatal, multi-organ disease among several bird species. Using cryogenic electron microscopy and other biochemical techniques, we investigated the structure of APV and compared it to that of mammalian polyomaviruses, particularly JC polyomavirus and simian virus 40. The structure of the pentameric major capsid protein (VP1) is mostly conserved; however, APV VP1 has a unique, truncated C-terminus that eliminates an intercapsomere-connecting β-hairpin observed in other polyomaviruses. We postulate that the terminal β-hairpin locks other polyomavirus capsids in a stable conformation and that absence of the hairpin leads to the observed capsid size variation in APV. Plug-like density features were observed at the base of the VP1 pentamers, consistent with the known location of minor capsid proteins VP2 and VP3. However, the plug density is more prominent in APV and may include VP4, a minor capsid protein unique to bird polyomaviruses.

Original languageEnglish (US)
Pages (from-to)142-152
Number of pages11
JournalVirology
Volume411
Issue number1
DOIs
StatePublished - Mar 1 2011

Fingerprint

Polyomavirus
Capsid
Capsid Proteins
Birds
JC Virus
Simian virus 40
Electron Microscopy

Keywords

  • Arginine
  • Capsomere connections
  • Cryo-electron microscopy
  • Homology model
  • Human JC polyomavirus
  • Simian virus 40
  • Size-exclusion chromatography
  • Three-dimensional reconstruction
  • Virus assembly
  • Virus structure

ASJC Scopus subject areas

  • Virology

Cite this

The structure of avian polyomavirus reveals variably sized capsids, non-conserved inter-capsomere interactions, and a possible location of the minor capsid protein VP4. / Shen, Peter S.; Enderlein, Dirk; Nelson, Christian D S; Carter, Weston S.; Kawano, Masaaki; Xing, Li; Swenson, Robert D.; Olson, Norman H.; Baker, Timothy S.; Cheng, R. Holland; Atwood, Walter J.; Johne, Reimar; Belnap, David M.

In: Virology, Vol. 411, No. 1, 01.03.2011, p. 142-152.

Research output: Contribution to journalArticle

Shen, PS, Enderlein, D, Nelson, CDS, Carter, WS, Kawano, M, Xing, L, Swenson, RD, Olson, NH, Baker, TS, Cheng, RH, Atwood, WJ, Johne, R & Belnap, DM 2011, 'The structure of avian polyomavirus reveals variably sized capsids, non-conserved inter-capsomere interactions, and a possible location of the minor capsid protein VP4', Virology, vol. 411, no. 1, pp. 142-152. https://doi.org/10.1016/j.virol.2010.12.005
Shen, Peter S. ; Enderlein, Dirk ; Nelson, Christian D S ; Carter, Weston S. ; Kawano, Masaaki ; Xing, Li ; Swenson, Robert D. ; Olson, Norman H. ; Baker, Timothy S. ; Cheng, R. Holland ; Atwood, Walter J. ; Johne, Reimar ; Belnap, David M. / The structure of avian polyomavirus reveals variably sized capsids, non-conserved inter-capsomere interactions, and a possible location of the minor capsid protein VP4. In: Virology. 2011 ; Vol. 411, No. 1. pp. 142-152.
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