ArticleProceedings of the National Academy of Sciences of the United States of America2007
Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.
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Who cites it
109 citing papers in PubMed, 182 citations in OpenAlex.
- ER protein CLCC1 promotes nuclear envelope fusion in herpesviral and host processes.Nature communications · 2025Article
- Structure of the Kaposi's sarcoma-associated herpesvirus gB in post-fusion conformation.Journal of virology · 2025Article
- A thorough insight into the life cycle of the Epstein-Barr virus. From the molecular to the organismal level.Current research in microbial sciences · 2025Review
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- Current Insights into the Maturation of Epstein-Barr Virus Particles.Microorganisms · 2024Review
- Targeted mutagenesis of the herpesvirus fusogen central helix captures transition states.Nature communications · 2023Article
- Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection.Nature communications · 2023Article
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- Anti-herpes simplex virus activities and mechanisms of marine derived compounds.Frontiers in cellular and infection microbiology · 2023Review
- Role of the Orphan Transporter SLC35E1 in the Nuclear Egress of Herpes Simplex Virus 1.Journal of virology · 2022Article
- The human cytomegalovirus decathlon: Ten critical replication events provide opportunities for restriction.Frontiers in cell and developmental biology · 2022Review
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- Viral use and subversion of membrane organization and trafficking.Journal of cell science · 2021Review
- Nuclear Egress.Current issues in molecular biology · 2021Review
- The XPO6 Exportin Mediates Herpes Simplex Virus 1 gM Nuclear Release Late in Infection.Journal of virology · 2020Article
49 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Herpesviruses must traverse the nuclear envelope to gain access to the cytoplasm and, ultimately, to exit cells. It is believed that herpesvirus nucleocapsids enter the perinuclear space by budding through the inner nuclear membrane (NM). To reach the cytoplasm these enveloped particles must fuse with the outer NM and the unenveloped capsids then acquire a second envelope in the trans-Golgi network. Little is known about the process by which herpesviruses virions fuse with the outer NM. Here we show that a herpes simplex virus (HSV) mutant lacking both the two putative fusion glycoproteins gB and gH failed to cross the nuclear envelope. Enveloped virions accumulated in the perinuclear space or in membrane vesicles that bulged into the nucleoplasm (herniations). By contrast, mutants lacking just gB or gH showed only minor or no defects in nuclear egress. We concluded that either HSV gB or gH can promote fusion between the virion envelope and the outer NM. It is noteworthy that fusion associated with HSV entry requires the cooperative action of both gB and gH, suggesting that the two types of fusion (egress versus entry) are dissimilar processes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.