ArticleJournal of virology2011
Two distinct conformations of a rinderpest virus epitope presented by bovine major histocompatibility complex class I N*01801: a host strategy to present featured peptides.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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
29 citing papers in PubMed, 44 citations in OpenAlex.
- Structural Prediction and Antigenic Characterization of Recombinant Nucleocapsid Protein (p14) of Small Ruminant Lentivirus.Viruses · 2026Article
- Understanding the structure of swine leukocyte antigen class I molecules.Cellular & molecular biology letters · 2026Review
- Article
- A Wider and Deeper Peptide-Binding Groove for the Class I Molecules from B15 Compared with B19 Chickens Correlates with Relative Resistance to Marek's Disease.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Mooring Stone-Like ArgJournal of virology · 2022Article
- A COVID-19 T-Cell Response Detection Method Based on a Newly Identified Human CD8China CDC weekly · 2022Article
- New vistas unfold: Chicken MHC molecules reveal unexpected ways to present peptides to the immune system.Frontiers in immunology · 2022Review
- The Structure of a Peptide-Loaded Shark MHC Class I Molecule Reveals Features of the Binding between βJournal of immunology (Baltimore, Md. : 1950) · 2021Article
- Crystal structure of the giant panda MHC class I complex: First insights into the viral peptide presentation profile in the bear family.Protein science : a publication of the Protein Society · 2020Article
- The Mechanism of β2m Molecule-Induced Changes in the Peptide Presentation Profile in a Bony Fish.iScience · 2020Article
- Structures of the MHC-I molecule BF2*1501 disclose the preferred presentation of an H5N1 virus-derived epitope.The Journal of biological chemistry · 2020Article
- A Glimpse of the Peptide Profile Presentation byJournal of immunology (Baltimore, Md. : 1950) · 2020Article
- Divergent Peptide Presentations of HLA-AFrontiers in immunology · 2019Article
- The Structure of the MHC Class I Molecule of Bony Fishes Provides Insights into the Conserved Nature of the Antigen-Presenting System.Journal of immunology (Baltimore, Md. : 1950) · 2017Article
- Structural Definition of Duck Major Histocompatibility Complex Class I Molecules That Might Explain Efficient Cytotoxic T Lymphocyte Immunity to Influenza A Virus.Journal of virology · 2017Article
- Article
- Structural and Biochemical Analyses of Swine Major Histocompatibility Complex Class I Complexes and Prediction of the Epitope Map of Important Influenza A Virus Strains.Journal of virology · 2016Article
- The structural basis of chicken, swine and bovine CD8αα dimers provides insight into the co-evolution with MHC I in endotherm species.Scientific reports · 2016Article
- A modern approach for epitope prediction: identification of foot-and-mouth disease virus peptides binding bovine leukocyte antigen (BoLA) class I molecules.Immunogenetics · 2015Article
- Crystallization and preliminary X-ray diffraction analysis of the two distinct types of zebrafish β2-microglobulin.Acta crystallographica. Section F, Structural biology communications · 2015Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presentation of viral peptide epitopes to host cytotoxic T lymphocytes (CTLs) is crucial for adaptive cellular immunity to clear the virus infection, especially for some chronic viral infections. Indeed, hosts have developed effective strategies to achieve this goal. The ideal scenario would be that the peptide epitopes stimulate a broad spectrum of CTL responses with diversified T-cell receptor (TCR) usage (the TCR repertoire). It is believed that a diversified TCR repertoire requires a "featured" peptide to be presented by the host major histocompatibility complex (MHC). A featured peptide can be processed and presented in a number of ways. Here, using the X-ray diffraction method, the crystal structures of an antigenic peptide derived from rinderpest virus presented by bovine MHC class I N*01801 (BoLA-A11) have been solved, and two distinct conformations of the presented peptide are clearly displayed. A detailed analysis of the structure and comparative sequences revealed that the polymorphic amino acid isoleucine 73 (Ile73) is extremely flexible, allowing the MHC groove to adopt different conformations to accommodate the rinderpest virus peptide. This makes the peptide more featured by exposing different amino acids for T-cell recognition. The crystal structures also demonstrated that the N*01801 molecule has an unusually large A pocket, resulting in the special conformation of the P1 residue at the N terminus of the peptide. We propose that this strategy of host peptide presentation might be beneficial for creating a diversified TCR repertoire, which is important for a more-effective CTL response.
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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.