ArticleVirology journal2010
Reversible conformational change in herpes simplex virus glycoprotein B with fusion-from-without activity is triggered by mildly acidic pH.
Article in Virology journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Host Cell Receptor and Herpes Simplex Virus 1 Glycoprotein B Are Determinants of Low Temperature Entry.Viruses · 2026Article
- Deep mutational scanning of rabies glycoprotein defines mutational constraint and antibody-escape mutations.Cell host & microbe · 2025Article
- Herpes simplex virus 1 envelope glycoprotein C shields glycoprotein D to protect virions from entry-blocking antibodies.Journal of virology · 2025Article
- Herpes simplex virus 1 glycoprotein C promotes virus penetration from endosomes during entry, independent of interaction with heparan sulfate.Frontiers in microbiology · 2025Article
- Herpes Simplex Virus 1 Envelope Glycoprotein C Shields Glycoprotein D to Protect Virions from Entry-Blocking Antibodies.bioRxiv : the preprint server for biology · 2024Article
- Herpes Simplex Virus 1 Glycoprotein B from a Hyperfusogenic Virus Mediates Enhanced Cell-Cell Fusion.Viruses · 2024Article
- Conformational Changes in Herpes Simplex Virus Glycoprotein C.Journal of virology · 2022Article
- Entry of Alphaherpesviruses.Current issues in molecular biology · 2021Review
- Herpes Simplex Virus Entry by a Nonconventional Endocytic Pathway.Journal of virology · 2020Article
- Glycoprotein C of Herpes Simplex Virus 1 Shields Glycoprotein B from Antibody Neutralization.Journal of virology · 2020Article
- Article
- Conformational Change in Herpes Simplex Virus Entry Glycoproteins Detected by Dot Blot.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Low-pH Endocytic Entry of the Porcine Alphaherpesvirus Pseudorabies Virus.Journal of virology · 2019Article
- Acidic pH Mediates Changes in Antigenic and Oligomeric Conformation of Herpes Simplex Virus gB and Is a Determinant of Cell-Specific Entry.Journal of virology · 2018Article
- Mildly Acidic pH Triggers an Irreversible Conformational Change in the Fusion Domain of Herpes Simplex Virus 1 Glycoprotein B and Inactivation of Viral Entry.Journal of virology · 2017Article
- Herpes Simplex Virus 1 Envelope Cholesterol Facilitates Membrane Fusion.Frontiers in microbiology · 2017Article
- Herpes simplex virus Membrane Fusion.Advances in anatomy, embryology, and cell biology · 2017Review
- Herpesvirus Entry into Host Cells Mediated by Endosomal Low pH.Traffic (Copenhagen, Denmark) · 2016Review
- Polyethylene glycol-mediated fusion of herpes simplex type 1 virions with the plasma membrane of cells that support endocytic entry.Virology journal · 2015Article
- Molecular requirement for sterols in herpes simplex virus entry and infectivity.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
backgroundThe pre-fusion form of the herpes simplex virus (HSV) fusion protein gB undergoes pH-triggered conformational change in vitro and during viral entry (Dollery et al., J. Virol. 84:3759-3766, 2010). The antigenic structure of gB from the fusion-from-without (FFWO) strain of HSV-1, ANG path, resembles wild type gB that has undergone pH-triggered changes. Together, changes in the antigenic and oligomeric conformation of gB correlate with fusion activity. We tested whether the pre-fusion form of FFWO gB undergoes altered conformational change in response to low pH.
resultsA pH of 5.5 - 6.0 altered the conformation of Domains I and V of FFWO gB, which together comprise the functional region containing the hydrophobic fusion loops. The ANG path gB oligomer was altered at a similar pH. All changes were reversible. In wild type HSV lacking the UL45 protein, which has been implicated in gB-mediated fusion, gB still underwent pH-triggered changes. ANG path entry was inactivated by pretreatment of virions with low pH.
conclusionThe pre-fusion conformation of gB with enhanced fusion activity undergoes alteration in antigenic structure and oligomeric conformation in response to acidic pH. We propose that endosomal pH triggers conformational change in mutant gB with FFWO activity in a manner similar to wild type. Differences apart from this trigger may account for the increased fusion activity of FFWO gB.
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