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-Structure paper
Title | A tail-like assembly at the portal vertex in intact herpes simplex type-1 virions. |
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Journal, issue, pages | PLoS Pathog, Vol. 8, Issue 10, Page e1002961, Year 2012 |
Publish date | Oct 4, 2012 |
Authors | Michael F Schmid / Corey W Hecksel / Ryan H Rochat / David Bhella / Wah Chiu / Frazer J Rixon / |
PubMed Abstract | 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 ...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. |
External links | PLoS Pathog / PubMed:23055933 / PubMed Central |
Methods | EM (subtomogram averaging) |
Resolution | 60.0 Å |
Structure data | EMDB-5452: EMDB-5453: |