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Ultrastructural Localization of the Herpes Simplex Virus Type 1 UL31, UL34, and US3 Proteins Suggests Specific Roles in Primary Envelopment and Egress of Nucleocapsids
Journal article   Open access   Peer reviewed

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 and Joel D Baines
Journal of virology, Vol.76(17), pp.8939-8952
09/2002
DOI: 10.1128/JVI.76.17.8939-8952.2002
PMCID: PMC136992
PMID: 12163613
url
https://doi.org/10.1128/JVI.76.17.8939-8952.2002View
Published (Version of record) Open Access

Abstract

The wild-type U L 31, U L 34, and U S 3 proteins localized on nuclear membranes and perinuclear virions; the U S 3 protein was also on cytoplasmic membranes and extranuclear virions. The U L 31 and U L 34 proteins were not detected in extracellular virions. U S 3 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 U S 3 protein plays an important, but nonessential, role in the egress pathway.
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