A Tail-like Assembly at the Portal Vertex in Intact Herpes Simplex Type-1 Virions

PLoS Pathogens

Ryan H. Rochat¹  Wah Chiu²  Frazer J. Rixon³  Michael F. Schmid⁴  David Bhella⁴  Corey W. Hecksel⁴ 

[1] Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, United States of America;Graduate Program in Structural and Computational Biology and Molecular Biophysics, Baylor College of Medicine, Houston, Texas, United States of America;MRC-University of Glasgow Centre for Virus Research, Glasgow, United Kingdom;National Center for Macromolecular Imaging, Verna and Marrs Mclean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, United States of America

关键词: Capsids;    Virions;    Multiple alignment calculation;    Viral structure;    Caudovirales;    Eigenvectors;    Herpesviruses;    Viral genomics;   

DOI  :  10.1371/journal.ppat.1002961

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

Herpes viruses are prevalent and well characterized human pathogens. Despite extensive study, much remains to be learned about the structure of the genome packaging and release machinery in the capsids of these large and complex double-stranded DNA viruses. However, such machinery is well characterized in tailed bacteriophage, which share a common evolutionary origin with herpesvirus. In tailed bacteriophage, the genome exits from the virus particle through a portal and is transferred into the host cell by a complex apparatus (i.e. the tail) located at the portal vertex. Here we use electron cryo-tomography of human herpes simplex type-1 (HSV-1) virions to reveal a previously unsuspected feature at the portal vertex, which extends across the HSV-1 tegument layer to form a connection between the capsid and the viral membrane. The location of this assembly suggests that it plays a role in genome release into the nucleus and is also important for virion architecture.

【 授权许可】

CC BY