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Journal of Virology, February 2007, p. 2065-2068, Vol. 81, No. 4
0022-538X/07/$08.00+0     doi:10.1128/JVI.02053-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Electron Cryotomography Reveals the Portal in the Herpesvirus Capsid{triangledown}

Juan T. Chang,1 Michael F. Schmid,1 Frazer J. Rixon,2 and Wah Chiu1*

Graduate Program in Structural and Computational Biology and Molecular Biophysics, National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030,1 MRC Institute of Virology, University of Glasgow, Glasgow G11 5JR, United Kingdom2

Received 19 September 2006/ Accepted 22 November 2006

Herpes simplex virus type 1 is a human pathogen responsible for a range of illnesses from cold sores to encephalitis. The icosahedral capsid has a portal at one fivefold vertex which, by analogy to portal-containing phages, is believed to mediate genome entry and exit. We used electron cryotomography to determine the structure of capsids lacking pentons. The portal vertex appears different from pentons, being located partially inside the capsid shell, a position equivalent to that of bacteriophage portals. Such similarity in portal organization supports the idea of the evolutionary relatedness of these viruses.

* Corresponding author. Mailing address: Graduate Program in Structural and Computational Biology and Molecular Biophysics, National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030. Phone: (713) 798-6985. Fax: (713) 798-8682. E-mail: wah{at}bcm.edu.

{triangledown} Published ahead of print on 6 December 2006.

Journal of Virology, February 2007, p. 2065-2068, Vol. 81, No. 4
0022-538X/07/$08.00+0     doi:10.1128/JVI.02053-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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