ArticleThe Journal of experimental medicine1997
The active site of ICP47, a herpes simplex virus-encoded inhibitor of the major histocompatibility complex (MHC)-encoded peptide transporter associated with antigen processing (TAP), maps to the NH2-terminal 35 residues.
Article in The Journal of experimental medicine, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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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
40 citing papers in PubMed, 170 citations in OpenAlex.
- Beyond oncogenesis: the unexplored benefits of viruses in cancer immunity.Nature reviews. Cancer · 2026Review
- Antitumor power of oncolytic HSV engineered with IL-12 and IL-15.Molecular therapy. Oncology · 2025Article
- Identification of TAP2 protein variants resistant to inhibition by the HSV1 ICP47 protein.bioRxiv : the preprint server for biology · 2024Article
- Semisynthetic Viral Inhibitor for Light Control of the MHC I Peptide Loading Complex.Angewandte Chemie (International ed. in English) · 2022Article
- Simplexviruses Successfully Adapt to Their Host by Fine-Tuning Immune Responses.Molecular biology and evolution · 2022Article
- "Non-Essential" Proteins of HSV-1 with Essential Roles In Vivo: A Comprehensive Review.Viruses · 2020Review
- Optical control of the antigen translocation by synthetic photo-conditional viral inhibitors.Chemical science · 2019Article
- Moving the Cellular Peptidome by Transporters.Frontiers in cell and developmental biology · 2018Review
- A highly conserved sequence of the viral TAP inhibitor ICP47 is required for freezing of the peptide transport cycle.Scientific reports · 2017Article
- Structure of the transporter associated with antigen processing trapped by herpes simplex virus.eLife · 2016Article
- A dual inhibition mechanism of herpesviral ICP47 arresting a conformationally thermostable TAP complex.Scientific reports · 2016Article
- A mechanism of viral immune evasion revealed by cryo-EM analysis of the TAP transporter.Nature · 2016Article
- Viral inhibition of the transporter associated with antigen processing (TAP): a striking example of functional convergent evolution.PLoS pathogens · 2015Review
- Review
- Critical analysis of an oncolytic herpesvirus encoding granulocyte-macrophage colony stimulating factor for the treatment of malignant melanoma.Oncolytic virotherapy · 2014Review
- HSV-2 specifically down regulates HLA-C expression to render HSV-2-infected DCs susceptible to NK cell killing.PLoS pathogens · 2013Article
- Comparing effects of BK virus agnoprotein and herpes simplex-1 ICP47 on MHC-I and MHC-II expression.Clinical & developmental immunology · 2013Article
- The human transporter associated with antigen processing: molecular models to describe peptide binding competent states.The Journal of biological chemistry · 2012Article
- Equine herpesvirus type 4 UL56 and UL49.5 proteins downregulate cell surface major histocompatibility complex class I expression independently of each other.Journal of virology · 2012Article
- ABC proteins in antigen translocation and viral inhibition.Nature chemical biology · 2010Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
The herpes simplex virus (HSV) immediate early protein ICP47 inhibits the transporter associated with antigen processing (TAP)-dependent peptide translocation. As a consequence, empty major histocompatibility complex (MHC) class I molecules are retained in the endoplasmic reticulum and recognition of HSV-infected cells by cytotoxic T lymphocytes is abolished. We chemically synthesized full-length ICP47 (sICP47) and show that sICP47 inhibits TAP-dependent peptide translocation in human cells. Its biological activity is indistinguishable from that of recombinant ICP47 (rICP47). By using synthetic peptides, we mapped the core sequence of ICP47 minimally required for TAP inhibition to residues 2-35. This segment is located within the region of the molecule conserved between ICP47 from HSV-1 and HSV-2. Through alanine scanning substitution we identified three segments within this region that are critical for the ability to inhibit TAP function. The interaction of ICP47 with TAP is unlikely to mimic precisely that of the transported peptides, as deduced from differential labeling of the TAP1 and TAP2 subunits using sICP47 fragments with chemical cross-linkers.
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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.