Electron cryotomography reveals the portal in the herpesvirus capsid

被引：70

作者：

Chang, Juan T.

Schmid, Michael F.

Rixon, Frazer J.

Chiu, Wah ^{[1
]}

机构：

[1] Baylor Coll Med, Grad Program Struct & Computat Biol & Mol Biophys, Natl Ctr Macromol Imaging, Verna & Marrs Mclean Dept Biochem & Mol Biol, Houston, TX 77030 USA

[2] Univ Glasgow, Inst Virol, MRC, Glasgow G11 5JR, Lanark, Scotland

来源：

JOURNAL OF VIROLOGY | 2007年 / 81卷 / 04期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1128/JVI.02053-06

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：2065 / 2068

页数：4

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