ArticleProceedings of the National Academy of Sciences of the United States of America2007
Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B.
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 57 papers.
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Who cites it
57 citing papers in PubMed, 78 citations in OpenAlex.
- Engineering HSV-1 for oncolytic therapy: From molecular entry mechanisms to retargeting strategies.Genes & diseases · 2026Review
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- Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection.Nature communications · 2023Article
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- Protective anti-gB neutralizing antibodies targeting two vulnerable sites for EBV-cell membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Herpes Simplex Virus Glycoprotein B Mutations Define Structural Sites in Domain I, the Membrane Proximal Region, and the Cytodomain That Regulate Entry.Journal of virology · 2021Article
- The structural basis of herpesvirus entry.Nature reviews. Microbiology · 2021Review
- Entry of Alphaherpesviruses.Current issues in molecular biology · 2021Review
- The N-terminus of varicella-zoster virus glycoprotein B has a functional role in fusion.PLoS pathogens · 2021Article
- The prefusion structure of herpes simplex virus glycoprotein B.Science advances · 2020Article
- Herpes Simplex Virus Cell Entry Mechanisms: An Update.Frontiers in cellular and infection microbiology · 2020Review
- Article
- Structural basis for membrane anchoring and fusion regulation of the herpes simplex virus fusogen gB.Nature structural & molecular biology · 2018Article
- Dual Ligand Insertion in gB and gD of Oncolytic Herpes Simplex Viruses for Retargeting to a Producer Vero Cell Line and to Cancer Cells.Journal of virology · 2018Article
- Structure-Function Dissection of Pseudorabies Virus Glycoprotein B Fusion Loops.Journal of virology · 2018Article
- Mapping sites of herpes simplex virus type 1 glycoprotein D that permit insertions and impact gD and gB receptors usage.Scientific reports · 2017Article
- Herpes simplex virus Membrane Fusion.Advances in anatomy, embryology, and cell biology · 2017Review
- Two distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Herpesvirus gB: A Finely Tuned Fusion Machine.Viruses · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Herpes simplex virus glycoprotein B (gB) is one of four glycoproteins essential for viral entry and cell fusion. Recently, an x-ray structure of the nearly full-length trimeric gB ectodomain was determined. Five structural domains and two linker regions were identified in what is probably a postfusion conformation. To identify functional domains of gB, we performed random linker-insertion mutagenesis. Analyses of 81 mutants revealed that only 27 could fold to permit processing and transport of gB to the cell surface. These 27 mutants fell into three categories. Insertions into two regions excluded from the solved structure (the N terminus and the C-terminal cytoplasmic tail) had no negative effect on cell fusion and viral entry activity, identifying regions that can tolerate altered structure without loss of function. Insertions into a disordered region in domain II and the adjacent linker region also permitted partial cell fusion and viral entry activity. Insertions at 16 other positions resulted in loss of cell fusion and viral entry activity, despite detectable levels of cell surface expression. Four of these insertion sites were not included in the solved structure. Two were between residues exposed to a cavity that is too small to accommodate the 5-amino acid insertions, consistent with the solved structure being different from the native prefusion structure. Ten were between residues exposed to the surface of the trimer, identifying regions that may be critical for interactions with other viral proteins or cellular components or for transitions from the prefusion to postfusion state.
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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.