Structure of the herpesvirus major capsid protein

Structure of the herpesvirus major capsid protein Herpes simplex virus‐1 (HSV‐1) virions are large, complex enveloped particles containing a proteinaceous tegument layer connected to an icosahedral capsid. The major capsid protein, VP5 (149 kDa), makes up both types of capsomere, pentons and hexons. Limited trypsin digestion of VP5 identified a single stable 65 kDa fragment which represents a proposed protein folding nucleus. We report the 2.9 Å crystal structure of this fragment and its modeling into an 8.5 Å resolution electron cryomicroscopy map of the HSV‐1 capsid. The structure, the first for any capsid protein from Herpesviridae, revealed a novel fold, placing herpesviruses outside any of the structurally linked viral groupings. Alterations in the geometrical arrangements of the VP5 subunits in the capsomeres exposes different residues, resulting in the differential association of the tegument and VP26 with the pentons and hexons, respectively. The rearrangements of VP5 subunits required to form both pentavalent and hexavalent capsomeres result in structures that exhibit very different electrostatic properties. These differences may mediate the binding and release of other structural proteins during capsid maturation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The EMBO Journal Wiley

Structure of the herpesvirus major capsid protein

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Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
0261-4189
eISSN
1460-2075
DOI
10.1093/emboj/cdg086
Publisher site
See Article on Publisher Site

Abstract

Herpes simplex virus‐1 (HSV‐1) virions are large, complex enveloped particles containing a proteinaceous tegument layer connected to an icosahedral capsid. The major capsid protein, VP5 (149 kDa), makes up both types of capsomere, pentons and hexons. Limited trypsin digestion of VP5 identified a single stable 65 kDa fragment which represents a proposed protein folding nucleus. We report the 2.9 Å crystal structure of this fragment and its modeling into an 8.5 Å resolution electron cryomicroscopy map of the HSV‐1 capsid. The structure, the first for any capsid protein from Herpesviridae, revealed a novel fold, placing herpesviruses outside any of the structurally linked viral groupings. Alterations in the geometrical arrangements of the VP5 subunits in the capsomeres exposes different residues, resulting in the differential association of the tegument and VP26 with the pentons and hexons, respectively. The rearrangements of VP5 subunits required to form both pentavalent and hexavalent capsomeres result in structures that exhibit very different electrostatic properties. These differences may mediate the binding and release of other structural proteins during capsid maturation.

Journal

The EMBO JournalWiley

Published: May 17, 2004

Keywords: ; ; ; ;

References

  • Dali: a network tool for protein structure comparison
    Holm, L; Sander, C
  • Molecular genetics of herpes simplex virus. VI. Characterization of a temperature‐sensitive mutant defective in the expression of all early viral gene products
    Knipe, DM; Batterson, W; Nosal, C; Roizman, B; Buchan, A
  • Herpes simplex virus phosphoproteins. II. Characterization of the virion protein kinase and of the polypeptides phosphorylated in the virion
    Lemaster, S; Roizman, B
  • Induced extrusion of DNA from the capsid of herpes simplex virus type 1
    Newcomb, WW; Brown, JC
  • Processing of X‐ray diffraction data collected in oscillation mode
    Otwinowski, Z; Minor, W
  • Three dimensional structure of the adenovirus major coat protein hexon
    Roberts, MM; White, JL; Grutter, MG; Burnett, RM
  • Assembly of the herpes simplex virus capsid: preformed triplexes bind to the nascent capsid
    Spencer, JV; Newcomb, WW; Thomsen, DR; Homa, FL; Brown, JC

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