ArticlePloS one2012
Herpesvirus glycoproteins undergo multiple antigenic changes before membrane fusion.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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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
8 citing papers in PubMed, 12 citations in OpenAlex.
- Sequential Immunizations with heterosubtypic virus-like particles elicit cross protection against divergent influenza A viruses in mice.Scientific reports · 2018Article
- The Major Envelope Glycoprotein of Murid Herpesvirus 4 Promotes Sexual Transmission.Journal of virology · 2017Article
- 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
- Myeloid infection links epithelial and B cell tropisms of Murid Herpesvirus-4.PLoS pathogens · 2012Article
- Virion endocytosis is a major target for murid herpesvirus-4 neutralization.The Journal of general virology · 2012Article
- Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.Journal of virology · 2012Article
- A heparan-dependent herpesvirus targets the olfactory neuroepithelium for host entry.PLoS pathogens · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Herpesvirus entry is a complicated process involving multiple virion glycoproteins and culminating in membrane fusion. Glycoprotein conformation changes are likely to play key roles. Studies of recombinant glycoproteins have revealed some structural features of the virion fusion machinery. However, how the virion glycoproteins change during infection remains unclear. Here using conformation-specific monoclonal antibodies we show in situ that each component of the Murid Herpesvirus-4 (MuHV-4) entry machinery--gB, gH/gL and gp150--changes in antigenicity before tegument protein release begins. Further changes then occurred upon actual membrane fusion. Thus virions revealed their final fusogenic form only in late endosomes. The substantial antigenic differences between this form and that of extracellular virions suggested that antibodies have only a limited opportunity to block virion membrane fusion.
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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.