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.
Electron cryotomography reveals the portal in the herpesvirus capsid. Publishing Authors By Initials
Electron cryotomography reveals the portal in the herpesvirus capsid. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Journal of virology
VOLUME: 81
Page Numbers: 2065-8
Journal Abbreviation: J. Virol.
ISSN: 0022-538X
DAY: 6
MONTH: 12
YEAR: 2006
Electron cryotomography reveals the portal in the herpesvirus capsid. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 113724
Electron cryotomography reveals the portal in the herpesvirus capsid. Keywords Mesh Terms:
KEYWORDS: Urea
MESH TERMS: chemistry
Chemical & Substance for Abstract: Electron cryotomography reveals the portal in the herpesvirus capsid. Information
Substance Name: Urea
Registry Number: 57-13-6
Grant and Affiliation Information for Electron cryotomography reveals the portal in the herpesvirus capsid.
AFFILIATION: 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, USA.
Country: United States
AGENCY: United States NIAID
GRANT: R01AI38469
ACRONYM: AI
MEDLINETA: J Virol
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