ArticlePloS one2011
Bovine herpesvirus type 1 (BHV-1) UL49.5 luminal domain residues 30 to 32 are critical for MHC-I down-regulation in virus-infected cells.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- MHC-I pathway disruption by viruses: insights into immune evasion and vaccine design for animals.Frontiers in immunology · 2025Review
- The Cell-Mediated Immune Response againstVaccines · 2023Review
- Article
- BoHV-1-Vectored BVDV-2 Subunit Vaccine Induces BVDV Cross-Reactive Cellular Immune Responses and Protects against BVDV-2 Challenge.Vaccines · 2021Article
- Anti-viral immunity in the tumor microenvironment: implications for the rational design of herpes simplex virus type 1 oncolytic virotherapy.Current clinical microbiology reports · 2019Article
- Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics.Biochimica et biophysica acta. Biomembranes · 2019Article
- Bovine Herpesvirus 1 UJournal of virology · 2018Article
- Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M.Viruses · 2016Article
- CD8(+) T-cell Immune Evasion Enables Oncolytic Virus Immunotherapy.EBioMedicine · 2016Article
- Equine Herpesvirus 1 Multiply Inserted Transmembrane Protein pUL43 Cooperates with pUL56 in Downregulation of Cell Surface Major Histocompatibility Complex Class I.Journal of virology · 2015Article
- An MHC class I immune evasion gene of Marek׳s disease virus.Virology · 2015Article
- Felid herpesvirus type 1 infection in cats: a natural host model for alphaherpesvirus pathogenesis.ISRN veterinary science · 2012Article
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3 authors.
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Abstract
Bovine herpesvirus type 1 (BHV-1) U(L)49.5 inhibits transporter associated with antigen processing (TAP) and down-regulates cell-surface expression of major histocompatibility complex (MHC) class I molecules to promote immune evasion. We have constructed a BHV-1 U(L)49.5 cytoplasmic tail (CT) null and several U(L)49.5 luminal domain mutants in the backbone of wild-type BHV-1 or BHV-1 U(L)49.5 CT- null viruses and determined their relative TAP mediated peptide transport inhibition and MHC-1 down-regulation properties compared with BHV-1 wt. Based on our results, the U(L)49.5 luminal domain residues 30-32 and U(L)49.5 CT residues, together, promote efficient TAP inhibition and MHC-I down-regulation functions. In vitro, BHV-1 U(L)49.5 Δ30-32 CT-null virus growth property was similar to that of BHV-1 wt and like the wt U(L)49.5, the mutant U(L)49.5 was incorporated in the virion envelope and it formed a complex with gM in the infected cells.
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