Ultrastructural Localization of the Herpes Simplex Virus Type 1 U L 31, U L 34, and U S 3 Proteins Suggests Specific Roles in Primary Envelopment and Egress of Nucleocapsids
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- 1 September 2002
- journal article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 76 (17) , 8939-8952
- https://doi.org/10.1128/jvi.76.17.8939-8952.2002
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.Keywords
This publication has 83 references indexed in Scilit:
- Intracellular Trafficking of the UL11 Tegument Protein of Herpes Simplex Virus Type 1Journal of Virology, 2001
- U L 31 and U L 34 Proteins of Herpes Simplex Virus Type 1 Form a Complex That Accumulates at the Nuclear Rim and Is Required for Envelopment of NucleocapsidsJournal of Virology, 2001
- The U S 3 Protein Kinase Blocks Apoptosis Induced by the d 120 Mutant of Herpes Simplex Virus 1 at a Premitochondrial StageJournal of Virology, 2001
- Egress of Alphaherpesviruses: Comparative Ultrastructural StudyJournal of Virology, 2001
- Retrieval of human cytomegalovirus glycoprotein B from the infected cell surface for virus envelopmentArchiv für die gesamte Virusforschung, 1996
- Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane.The Journal of cell biology, 1995
- The US3-encoded protein kinase from pseudorabies virus affects egress of virions from the nucleusJournal of General Virology, 1995
- The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal.The Journal of cell biology, 1993
- The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane.The Journal of cell biology, 1993
- Characterization of Herpes Simplex Virus Strains Differing in their Effects on Social Behaviour of Infected CellsJournal of General Virology, 1968