The immunogenicity of a viral cytotoxic T cell epitope is controlled by its MHC-bound conformation. - Wikidata - wikimedia - TriplyDB

The immunogenicity of a viral cytotoxic T cell epitope is controlled by its MHC-bound conformation.

The immunogenicity of a viral cytotoxic T cell epitope is controlled by its MHC-bound conformation.

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Novel sequence feature variant type analysis of the HLA genetic association in systemic sclerosis A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule Structural Basis for T Cell Alloreactivity among Three HLA-B14 and HLA-B27 Antigens Natural micropolymorphism in human leukocyte antigens provides a basis for genetic control of antigen recognition Constraints within major histocompatibility complex class I restricted peptides: Presentation and consequences for T-cell recognition Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability Allelic polymorphism in the T cell receptor and its impact on immune responses Structural features underlying T-cell receptor sensitivity to concealed MHC class I micropolymorphisms Highly Divergent T-cell Receptor Binding Modes Underlie Specific Recognition of a Bulged Viral Peptide bound to a Human Leukocyte Antigen Class I Molecule Molecular Imprint of Exposure to Naturally Occurring Genetic Variants of Human Cytomegalovirus on the T cell Repertoire A Molecular Basis for the Interplay between T Cells, Viral Mutants, and Human Leukocyte Antigen Micropolymorphism Co-evolution of human leukocyte antigen (HLA) class I ligands with killer-cell immunoglobulin-like receptors (KIR) in a genetically diverse population of sub-Saharan Africans Structural and Biochemical Analyses of Swine Major Histocompatibility Complex Class I Complexes and Prediction of the Epitope Map of Important Influenza A Virus Strains.Epstein-Barr virus and multiple sclerosis: potential opportunities for immunotherapy Degenerate T-cell recognition of peptides on MHC molecules creates large holes in the T-cell repertoire.A broad profile of co-dominant epitopes shapes the peripheral Mycobacterium tuberculosis specific CD8+ T-cell immune response in South African patients with active tuberculosis.T cell epitope clustering in the highly immunogenic BZLF1 antigen of Epstein-Barr virus.Properties of MHC class I presented peptides that enhance immunogenicity Mutually exclusive T-cell receptor induction and differential susceptibility to human immunodeficiency virus type 1 mutational escape associated with a two-amino-acid difference between HLA class I subtypes A single amino acid difference within the alpha-2 domain of two naturally occurring equine MHC class I molecules alters the recognition of Gag and Rev epitopes by equine infectious anemia virus-specific CTL.Host ethnicity and virus genotype shape the hepatitis B virus-specific T-cell repertoire.Decreased T cell reactivity to Epstein-Barr virus infected lymphoblastoid cell lines in multiple sclerosis.The essential role of Epstein-Barr virus in the pathogenesis of multiple sclerosis The versatility of the αβ T-cell antigen receptor.The structural bases of direct T-cell allorecognition: implications for T-cell-mediated transplant rejection.Understanding human T-cell-mediated immunoregulation through herpesviruses.A structural voyage toward an understanding of the MHC-I-restricted immune response: lessons learned and much to be learned.Understanding the complexity and malleability of T-cell recognition.Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.A Micropolymorphism Altering the Residue Triad 97/114/156 Determines the Relative Levels of Tapasin Independence and Distinct Peptide Profiles for HLA-A(*)24 Allotypes.Soluble HLA technology as a strategy to evaluate the impact of HLA mismatches.Position 156 influences the peptide repertoire and tapasin dependency of human leukocyte antigen B*44 allotypes.Lytic EBV infection investigated by detection of Soluble Epstein-Barr virus ZEBRA in the serum of patients with PTLD.Structural basis for degenerate recognition of natural HIV peptide variants by cytotoxic lymphocytes.Defective T-cell control of Epstein-Barr virus infection in multiple sclerosis.An asymmetric model of heterozygote advantage at major histocompatibility complex genes: degenerate pathogen recognition and intersection advantage Peptide-dependent conformational fluctuation determines the stability of the human leukocyte antigen class I complex.Alloreactivity between disparate cognate and allogeneic pMHC-I complexes is the result of highly focused, peptide-dependent structural mimicry.A basic phenylalanine-rich oligo-peptide causes antibody cross-reactivity.NetTepi: an integrated method for the prediction of T cell epitopes.

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P2860

The immunogenicity of a viral cytotoxic T cell epitope is controlled by its MHC-bound conformation.

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The immunogenicity of a viral ...... by its MHC-bound conformation.

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The immunogenicity of a viral ...... by its MHC-bound conformation.

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The immunogenicity of a viral ...... by its MHC-bound conformation.

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The immunogenicity of a viral ...... by its MHC-bound conformation.

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Journal of Experimental Medicine

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Diah Elhassen

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Fleur E Tynan

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Jacqueline M Burrows

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Judy Tellam

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Kate J Green

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Lars Kjer-Nielsen

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structural Comparison of Allogeneic and Syngeneic T Cell Receptor–Peptide-Major Histocompatibility Complex Complexes

A structural basis for the selection of dominant alphabeta T cell receptors in antiviral immunity

A structural basis for immunodominant human T cell receptor recognition

A Naturally Selected Dimorphism within the HLA-B44 Supertype Alters Class I Structure, Peptide Repertoire, and T Cell Recognition

Dual, HLA-B27 Subtype-dependent Conformation of a Self-peptide

Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution

An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501

Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C terminus

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1249-1260

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10.1084/JEM.20050864

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9

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202

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James McCluskey

Anthony W. Purcell

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7492046

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