ArticleThe Journal of general virology2008
Glycoprotein B switches conformation during murid herpesvirus 4 entry.
Article in The Journal of general virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Article
- Multivalent binding of herpesvirus to living cells is tightly regulated during infection.Science advances · 2018Article
- Herpesvirus Entry into Host Cells Mediated by Endosomal Low pH.Traffic (Copenhagen, Denmark) · 2016Review
- Deletion of Murid Herpesvirus 4 ORF63 Affects the Trafficking of Incoming Capsids toward the Nucleus.Journal of virology · 2015Article
- Polyethylene glycol-mediated fusion of herpes simplex type 1 virions with the plasma membrane of cells that support endocytic entry.Virology journal · 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
- Article
- Myeloid infection links epithelial and B cell tropisms of Murid Herpesvirus-4.PLoS pathogens · 2012Article
- Murine gammaherpesvirus 68 glycoprotein 150 does not contribute to latency amplification in vivo.Virology journal · 2012Article
- Virion endocytosis is a major target for murid herpesvirus-4 neutralization.The Journal of general virology · 2012Article
- Bovine herpesvirus type 4 glycoprotein L is nonessential for infectivity but triggers virion endocytosis during entry.Journal of virology · 2012Article
- Article
- Low-pH-dependent changes in the conformation and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity.Journal of virology · 2011Article
- A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization.The Journal of general virology · 2011Article
- Vaccination with murid herpesvirus-4 glycoprotein B reduces viral lytic replication but does not induce detectable virion neutralization.The Journal of general virology · 2010Article
- Low pH-induced conformational change in herpes simplex virus glycoprotein B.Journal of virology · 2010Article
- Antibody limits in vivo murid herpesvirus-4 replication by IgG Fc receptor-dependent functions.The Journal of general virology · 2009Article
- Glycoprotein L sets the neutralization profile of murid herpesvirus 4.The Journal of general virology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Herpesviruses are ancient pathogens that infect all vertebrates. The most conserved component of their entry machinery is glycoprotein B (gB), yet how gB functions is unclear. A striking feature of the murid herpesvirus 4 (MuHV-4) gB is its resistance to neutralization. Here, we show by direct visualization of infected cells that the MuHV-4 gB changes its conformation between extracellular virions and those in late endosomes, where capsids are released. Specifically, epitopes on its N-terminal cell-binding domain become inaccessible, whilst non-N-terminal epitopes are revealed, consistent with structural changes reported for the vesicular stomatitis virus glycoprotein G. Inhibitors of endosomal acidification blocked the gB conformation switch. They also blocked capsid release and the establishment of infection, implying that the gB switch is a key step in entry. Neutralizing antibodies could only partially inhibit the switch. Their need to engage a less vulnerable, upstream form of gB, because its fusion form is revealed only in endosomes, helps to explain why gB-directed MuHV-4 neutralization is so difficult.
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What OpenQuestion holds
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.