ArticleJournal of virology2002
A tyrosine-based motif in the cytoplasmic tail of pseudorabies virus glycoprotein B is important for both antibody-induced internalization of viral glycoproteins and efficient cell-to-cell spread.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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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Who cites it
34 citing papers in PubMed, 50 citations in OpenAlex.
- How vaccine research took me on an international journey.Human vaccines & immunotherapeutics · 2026Article
- Pseudorabies Virus Glycoproteins E and B Application in Vaccine and Diagnosis Kit Development.Vaccines · 2024Review
- Internalization of rabies virus glycoprotein differs between pathogenic and attenuated virus strains.The Journal of general virology · 2023Article
- Article
- Viral Interactions with Adaptor-Protein Complexes: A Ubiquitous Trait among Viral Species.International journal of molecular sciences · 2021Review
- The Neuropathic Itch Caused by Pseudorabies Virus.Pathogens (Basel, Switzerland) · 2020Review
- Alphaherpesvirus infection of mice primes PNS neurons to an inflammatory state regulated by TLR2 and type I IFN signaling.PLoS pathogens · 2019Article
- Expression of the Pseudorabies Virus gB Glycoprotein Triggers NK Cell Cytotoxicity and Increases Binding of the Activating NK Cell Receptor PILRβ.Journal of virology · 2019Article
- The Pseudorabies Virus Glycoprotein gE/gI Complex Suppresses Type I Interferon Production by Plasmacytoid Dendritic Cells.Journal of virology · 2017Article
- In vivo imaging of alphaherpesvirus infection reveals synchronized activity dependent on axonal sorting of viral proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- An immunoreceptor tyrosine-based inhibition motif in varicella-zoster virus glycoprotein B regulates cell fusion and skin pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Alphaherpesvirus infection disrupts mitochondrial transport in neurons.Cell host & microbe · 2012Article
- Herpes simplex virus 1 glycoprotein B and US3 collaborate to inhibit CD1d antigen presentation and NKT cell function.Journal of virology · 2011Article
- Role of the herpes simplex virus 1 Us3 kinase phosphorylation site and endocytosis motifs in the intracellular transport and neurovirulence of envelope glycoprotein B.Journal of virology · 2011Article
- Optimal replication of human cytomegalovirus correlates with endocytosis of glycoprotein gpUL132.Journal of virology · 2010Article
- Anti-glycoprotein H antibody impairs the pathogenicity of varicella-zoster virus in skin xenografts in the SCID mouse model.Journal of virology · 2010Article
- Directional transneuronal spread of α-herpesvirus infection.Future virology · 2009Article
- Pseudorabies virus infection alters neuronal activity and connectivity in vitro.PLoS pathogens · 2009Article
- Virion-incorporated glycoprotein B mediates transneuronal spread of pseudorabies virus.Journal of virology · 2009Article
- Herpes simplex virus 1 protein kinase Us3 phosphorylates viral envelope glycoprotein B and regulates its expression on the cell surface.Journal of virology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudorabies virus (PRV), a swine alphaherpesvirus, is capable of causing viremia in vaccinated animals. Two mechanisms that may help PRV avoid recognition by the host immune system during this viremia are direct cell-to-cell spread in tissue and antibody-induced internalization of viral cell surface glycoproteins in PRV-infected blood monocytes, the carrier cells of the virus in the blood. PRV glycoprotein B (gB) is crucial during both processes. Here we show that mutating a tyrosine residue located in a YXXPhi motif in the gB cytoplasmic tail results in decreased efficiency of cell-to-cell spread and a strong reduction in antibody-induced internalization of viral cell surface glycoproteins. Mutating the dileucine motif in the gB tail led to an increased cell-to-cell spread of the virus and the formation of large syncytia.
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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.