Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids

Ashley E. Reynolds, Elizabeth G. Wills, Richard J. Roller, Brent J. Ryckman, Joel D. Baines

Research output: Contribution to journalArticlepeer-review

284 Scopus citations

Abstract

The wild-type UL31, UL34, and US3 proteins localized on nuclear membranes and perinuclear virions; the US3 protein was also on cytoplasmic membranes and extranuclear virions. The UL31 and UL34 proteins were not detected in extracellular virions. US3 deletion caused (i) virion accumulation in nuclear membrane invaginations, (ii) delayed virus production onset, and (iii) reduced peak virus titers. These data support the herpes simplex virus type 1 deenvelopment-reenvelopment model of virion egress and suggest that the US3 protein plays an important, but nonessential, role in the egress pathway.

Original languageEnglish
Pages (from-to)8939-8952
Number of pages14
JournalJournal of Virology
Volume76
Issue number17
DOIs
StatePublished - 2002

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