ArticleJournal of virology2004
Internalization of pseudorabies virus glycoprotein B is mediated by an interaction between the YQRL motif in its cytoplasmic domain and the clathrin-associated AP-2 adaptor complex.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Recombinant Alphaherpesvirus Vectors in Veterinary Vaccinology: Platforms, Applications, and Translational Challenges.International journal of molecular sciences · 2026Review
- AP2: an indispensable host factor in virus infection.Journal of virology · 2026Review
- Numb-Associated Kinases-Mediated AP2M1 Activation Facilitates Porcine Reproductive and Respiratory Syndrome Virus Entry.Transboundary and emerging diseases · 2026Article
- Crystal structures of the μ2 subunit of clathrin-adaptor protein 2 in complex with peptides derived from human papillomavirus 16 E7.Journal of microbiology (Seoul, Korea) · 2025Article
- Virus infection and vesicle trafficking.Frontiers in immunology · 2025Review
- Pseudorabies virus uses clathrin mediated endocytosis to enter PK15 swine cell line.Frontiers in microbiology · 2024Article
- TMEM41B Is an Interferon-Stimulated Gene That Promotes Pseudorabies Virus Replication.Journal of virology · 2023Article
- Viral Interactions with Adaptor-Protein Complexes: A Ubiquitous Trait among Viral Species.International journal of molecular sciences · 2021Review
- Remodeling of host membranes during herpesvirus assembly and egress.Protein & cell · 2019Review
- Dynamin Is Required for Efficient Cytomegalovirus Maturation and Envelopment.Journal of virology · 2018Article
- Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein.Journal of virology · 2017Article
- Review
- 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
- Optimal replication of human cytomegalovirus correlates with endocytosis of glycoprotein gpUL132.Journal of virology · 2010Article
- 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
- Contribution of endocytic motifs in the cytoplasmic tail of herpes simplex virus type 1 glycoprotein B to virus replication and cell-cell fusion.Journal of virology · 2007Article
- Replication of feline coronaviruses in peripheral blood monocytes.Archives of virology · 2005Article
- Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine.Microbiology and molecular biology reviews : MMBR · 2005Review
- Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress.Journal of virology · 2005Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cytoplasmic domain of pseudorabies virus (PRV) glycoprotein B (gB) contains three putative internalization motifs. Previously, we demonstrated that the tyrosine-based YQRL motif at positions 902 to 905, but not the YMSI motif at positions 864 to 867 or the LL doublet at positions 887 and 888, is required for correct functioning of gB during antibody-mediated internalization of PRV cell surface-bound glycoproteins. In the present study, we demonstrate that the YQRL motif is also crucial to allow spontaneous internalization of PRV gB, and thus, that spontaneous and antibody-mediated internalizations of PRV gB occur through closely related mechanisms. Furthermore, we found that PRV gB colocalizes with the cellular clathrin-associated AP-2 adaptor complex and that this colocalization depends on the YQRL motif. In addition, by coimmunoprecipitation assays, we found that during both spontaneous and antibody-dependent internalization, PRV gB physically interacts with AP-2, and that efficient interaction between gB and AP-2 required an intact YQRL motif. Collectively, these findings demonstrate for the first time that during internalization of an alphaherpesvirus envelope protein, i.e., PRV gB, a specific amino acid sequence in the cytoplasmic tail of the protein interacts with AP-2 and may constitute a common AP-2-mediated mechanism of internalization of alphaherpesvirus envelope proteins.
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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.