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Journal of Virology, December 2001, p. 11863-11867, Vol. 75, No. 23
Verna and Marrs McLean Department of
Biochemistry, Baylor College of Medicine,1 and
Department of Pathology and Laboratory Medicine, University of
Texas-Houston Medical School,3 Houston, Texas
77030, and MRC Virology Unit, Institute of Virology, Glasgow
G11 5JR, United Kingdom2
Received 7 June 2001/Accepted 10 July 2001
Examination of the three-dimensional structure of intact herpes
simplex virus type 1 (HSV-1) virions had revealed that the icosahedrally symmetrical interaction between the tegument and capsid
involves the pentons but not the hexons (Z. H. Zhou, D. H. Chen, J. Jakana, F. J. Rixon, and W. Chiu, J. Virol.
73:3210-3218, 1999). To account for this, we postulated that the
presence of the small capsid protein, VP26, on top of the hexons was
masking potential binding sites and preventing tegument attachment. We have now tested this hypothesis by determining the structure of virions
lacking VP26. Apart from the obvious absence of VP26 from the capsids,
the structures of the VP26 minus and wild-type virions were essentially
identical. Notably, they showed the same tegument attachment patterns,
thereby demonstrating that VP26 is not responsible for the divergent
tegument binding properties of pentons and hexons.
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.23.11863-11867.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
The Pattern of Tegument-Capsid Interaction in the
Herpes Simplex Virus Type 1 Virion Is Not Influenced by the Small
Hexon-Associated Protein VP26
*
Corresponding author. Mailing address: MRC Virology
Unit, Institute of Virology, Church Street, Glasgow, United Kingdom,
G11 5JR. Phone: 44141 330 4025. Fax: 44141 337 2236. E-mail:
f.rixon{at}vir.gla.ac.uk.
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