Atomic model of the papillomavirus capsid

Atomic model of the papillomavirus capsid Papillomaviruses propagate in differentiating skin cells, and certain types are responsible for the onset of cervical cancer. We have combined image reconstructions from electron cryomicroscopy (cryoEM) of bovine papillomavirus at 9 Å resolution with coordinates from the crystal structure of small virus‐like particles of the human papillomavirus type 16 L1 protein to generate an atomic model of the virion. The overall fit of the L1 model into the cryoEM map is excellent, but residues 402–446 in the ‘C‐terminal arm’ must be rebuilt. We propose a detailed model for the structure of this arm, based on two constraints: the presence of an intermolecular disulfide bond linking residues 175 and 428, and the clear identification of a feature in the image reconstruction corresponding to an α‐helix near the C‐terminus of L1. We have confirmed the presence of the disulfide bond by mass spectrometry. Our ‘invading arm’ model shows that papilloma‐ and polyomaviruses have a conserved capsid architecture. Most of the rebuilt C‐terminal arm is exposed on the viral surface; it is likely to have a role in infection and in immunogenicity. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The EMBO Journal Wiley

Atomic model of the papillomavirus capsid

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Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
0261-4189
eISSN
1460-2075
DOI
10.1093/emboj/cdf494
Publisher site
See Article on Publisher Site

Abstract

Papillomaviruses propagate in differentiating skin cells, and certain types are responsible for the onset of cervical cancer. We have combined image reconstructions from electron cryomicroscopy (cryoEM) of bovine papillomavirus at 9 Å resolution with coordinates from the crystal structure of small virus‐like particles of the human papillomavirus type 16 L1 protein to generate an atomic model of the virion. The overall fit of the L1 model into the cryoEM map is excellent, but residues 402–446 in the ‘C‐terminal arm’ must be rebuilt. We propose a detailed model for the structure of this arm, based on two constraints: the presence of an intermolecular disulfide bond linking residues 175 and 428, and the clear identification of a feature in the image reconstruction corresponding to an α‐helix near the C‐terminus of L1. We have confirmed the presence of the disulfide bond by mass spectrometry. Our ‘invading arm’ model shows that papilloma‐ and polyomaviruses have a conserved capsid architecture. Most of the rebuilt C‐terminal arm is exposed on the viral surface; it is likely to have a role in infection and in immunogenicity.

Journal

The EMBO JournalWiley

Published: Apr 16, 2003

Keywords: ; ; ; ;

References

  • Conserved features in papillomavirus and polyomavirus capsids
    Belnap, DM; Olson, NH; Cladel, NM; Newcomb, WW; Brown, JC; Kreider, JW; Christensen, ND; Baker, TS
  • Papillomavirus capsid protein expression in Escherichia coli: purification and assembly of HPV11 and HPV16 L1
    Chen, XS; Casini, G; Harrison, SC; Garcea, RL
  • Site‐directed mutation affecting polyomavirus capsid self‐assembly in vitro
    Garcea, RL; Salunke, DM; Caspar, DL
  • Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometric observation of a peptide triplet induced by thermal cleavage of cystine
    Kim, JS; Kim, HJ

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