ArticlePLoS pathogens2016
Human Cytomegalovirus gH/gL Forms a Stable Complex with the Fusion Protein gB in Virions.
Article in PLoS pathogens, 2016. 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.
- Pre-assembled complexes and allosteric effects: parallels between eukaryotic phosphorylation cascades and membrane fusion during herpesviral entry.Journal of virology · 2026Review
- Progress and prospects for herpesvirus vaccination using gB antigens.Frontiers in immunology · 2026Review
- Article
- Herpes simplex virus 1 envelope glycoprotein C shields glycoprotein D to protect virions from entry-blocking antibodies.Journal of virology · 2025Article
- Feasibility of using saliva for Cytomegalovirus detection and genotyping in pediatric hematopoietic stem cell transplant recipients.Acta odontologica latinoamericana : AOL · 2025Article
- Allosteric mechanism of membrane fusion activation in a herpesvirus.bioRxiv : the preprint server for biology · 2024Article
- The Autonomous Fusion Activity of Human Cytomegalovirus Glycoprotein B Is Regulated by Its Carboxy-Terminal Domain.Viruses · 2024Article
- Herpes Simplex Virus 1 Envelope Glycoprotein C Shields Glycoprotein D to Protect Virions from Entry-Blocking Antibodies.bioRxiv : the preprint server for biology · 2024Article
- Targeted mutagenesis of the herpesvirus fusogen central helix captures transition states.Nature communications · 2023Article
- Article
- A single, improbable B cell receptor mutation confers potent neutralization against cytomegalovirus.PLoS pathogens · 2023Article
- Characterization of Plasma Immunoglobulin G Responses in Elite Neutralizers of Human Cytomegalovirus.The Journal of infectious diseases · 2022Article
- Herpes Simplex Virus 1 Entry Glycoproteins Form Complexes before and during Membrane Fusion.mBio · 2022Article
- Development of broadly neutralizing antibodies targeting the cytomegalovirus subdominant antigen gH.Communications biology · 2022Article
- Identification of functionally important domains of human cytomegalovirus gO that act after trimer binding to receptors.PLoS pathogens · 2022Article
- Structural basis for HCMV Pentamer recognition by neuropilin 2 and neutralizing antibodies.Science advances · 2022Article
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Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Human cytomegalovirus (HCMV) is a ubiquitous virus that is a major pathogen in newborns and immunocompromised or immunosuppressed patients. HCMV infects a wide variety of cell types using distinct entry pathways that involve different forms of the gH/gL glycoprotein: gH/gL/gO and gH/gL/UL128-131 as well as the viral fusion glycoprotein, gB. However, the minimal or core fusion machinery (sufficient for cell-cell fusion) is just gH/gL and gB. Here, we demonstrate that HCMV gB and gH/gL form a stable complex early after their synthesis and in the absence of other viral proteins. gH/gL can interact with gB mutants that are unable to mediate cell-cell fusion. gB-gH/gL complexes included as much as 16-50% of the total gH/gL in HCMV virus particles. In contrast, only small amounts of gH/gL/gO and gH/gL/UL128-131 complexes were found associated with gB. All herpesviruses express gB and gH/gL molecules and most models describing herpesvirus entry suggest that gH/gL interacts with gB to mediate membrane fusion, although there is no direct evidence for this. For herpes simplex virus (HSV-1) it has been suggested that after receptor binding gH/gL binds to gB either just before, or coincident with membrane fusion. Therefore, our results have major implications for these models, demonstrating that HCMV gB and gH/gL forms stable gB-gH/gL complexes that are incorporated virions without receptor binding or membrane fusion. Moreover, our data is the best support to date for the proposal that gH/gL interacts with gB.
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