ArticleThe Journal of general virology2011
A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization.
Article in The Journal of general virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- The Major Envelope Glycoprotein of Murid Herpesvirus 4 Promotes Sexual Transmission.Journal of virology · 2017Article
- Deletion of Murid Herpesvirus 4 ORF63 Affects the Trafficking of Incoming Capsids toward the Nucleus.Journal of virology · 2015Article
- Rhadinovirus host entry by co-operative infection.PLoS pathogens · 2015Article
- Glycoprotein B cleavage is important for murid herpesvirus 4 to infect myeloid cells.Journal of virology · 2013Article
- Bovine herpesvirus 4 glycoprotein B is indispensable for lytic replication and irreplaceable by VSVg.BMC veterinary research · 2013Article
- Virion endocytosis is a major target for murid herpesvirus-4 neutralization.The Journal of general virology · 2012Article
- Article
- A heparan-dependent herpesvirus targets the olfactory neuroepithelium for host entry.PLoS pathogens · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Glycoprotein B (gB) is a conserved, essential component of gammaherpes virions and so potentially vulnerable to neutralization. However, few good gB-specific neutralizing antibodies have been identified. Here, we show that murid herpesvirus 4 is strongly neutralized by mAbs that recognize an epitope close to one of the gB fusion loops. Antibody binding did not stop gB interacting with its cellular ligands or initiating its fusion-associated conformation change, but did stop gB resolving stably to its post-fusion form, and so blocked membrane fusion to leave virions stranded in late endosomes. The conservation of gB makes this mechanism a possible general route to gammaherpesvirus neutralization.
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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.