A tail-like assembly at the portal vertex in intact herpes simplex type-1 virions.
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.
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.
Michael F
MF
Schmid
Corey W
CW
Hecksel
Ryan H
RH
Rochat
David
D
Bhella
Wah
W
Chiu
Frazer J
FJ
Rixon
D000818:Animals; D001435:Bacteriophages; D002213:Capsid / Q000737:chemistry / Q000378:metabolism*; D006224:Cricetinae; D020285:Cryoelectron Microscopy; D055032:Electron Microscope Tomography; D018259:Herpesvirus 1, Human / Q000235:genetics* / Q000378:metabolism / Q000648:ultrastructure*; D006801:Humans; D014771:Virion / Q000378:metabolism / Q000648:ultrastructure*; D053586:Virus Internalization