Abstract
Herpes simplex virus type 1 (HSV-1) is a structurally complex enveloped dsDNA virus that has evolved to replicate in human neurons and epithelia. Viral gene expression, DNA replication, capsid assembly, and genome packaging take place in the infected cell nucleus, which mature nucleocapsids exit by envelopment at the inner nuclear membrane then de-envelopment into the cytoplasm. Once in the cytoplasm, capsids travel along microtubules to reach, dock, and envelope at cytoplasmic organelles. This generates mature infectious HSV-1 particles that must then be sorted to the termini of sensory neurons, or to epithelial cell junctions, for spread to uninfected cells. The focus of this review is upon our current understanding of the viral and cellular molecular machinery that enables HSV-1 to travel within infected cells during egress and to manipulate cellular organelles to construct its envelope.
Highlights
Herpes simplex virus types 1 and 2 (HSV-1 and HSV-2) and varicella zoster virus (VZV) are human pathogens of the subfamily Alphaherpesvirinae that replicate in peripheral tissues invade the nervous system to establish latency [1,2,3,4,5]
We found that loss of UL36p reduced the efficiency with which membrane-associated Herpes simplex virus type 1 (HSV-1) capsids were able to engage with the endosomal sorting complex required for transport (ESCRT) apparatus by approximately 70%, suggesting that UL36p plays an important role in recruitment of capsids to the site of ESCRT-III/vacuolar protein sorting 4 (Vps4) deposition [59]
HSV-1 capsid trafficking, envelopment and transport, and sorting of enveloped virions in the infected cell cytoplasm can often seem a process of bewildering complexity, and many fundamental questions concerning the biology of this virus remain unanswered
Summary
Herpes simplex virus types 1 and 2 (HSV-1 and HSV-2) and varicella zoster virus (VZV) are human pathogens of the subfamily Alphaherpesvirinae that replicate in peripheral tissues invade the nervous system to establish latency [1,2,3,4,5]. Sorting of virions into or along axons It is not clear whether inner tegument proteins are added to the HSV-1 capsid while it resides in the nucleoplasm, or only after emergence into the cytosol. Both UL36p and UL37p localize at least in part to the interior of the nucleus [101,102,103], but immunoblot analysis has led to differing conclusions concerning whether UL36p and UL37p are bound to nuclear capsids [53,104,105,106]. If a similar mechanism operates for HSV-1 antibody-based detection of UL36p on nuclear capsids would yield variable results, depending upon whether the relevant epitope is present within the capsid-bound UL36p fragment
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