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Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
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Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
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Journal Article
Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
2018
Overview
Through major histocompatibility complex class Ia leader sequence-derived (VL9) peptide binding and CD94/NKG2 receptor engagement, human leucocyte antigen E (HLA-E) reports cellular health to NK cells. Previous studies demonstrated a strong bias for VL9 binding by HLA-E, a preference subsequently supported by structural analyses. However,
Mycobacteria tuberculosis
(Mtb) infection and Rhesus cytomegalovirus-vectored SIV vaccinations revealed contexts where HLA-E and the rhesus homologue, Mamu-E, presented diverse pathogen-derived peptides to CD8
+
T cells, respectively. Here we present crystal structures of HLA-E in complex with HIV and Mtb-derived peptides. We show that despite the presence of preferred primary anchor residues, HLA-E-bound peptides can adopt alternative conformations within the peptide binding groove. Furthermore, combined structural and mutagenesis analyses illustrate a greater tolerance for hydrophobic and polar residues in the primary pockets than previously appreciated. Finally, biochemical studies reveal HLA-E peptide binding and exchange characteristics with potential relevance to its alternative antigen presenting function in vivo.
Human leucocyte antigen E (HLA-E) directly engages NK cells but also presents antigen to CD8
+
T cells. Here the authors show crystal structures of HLA-E in complex with peptides derived from HIV and
Mycobacterium tuberculosis
, and describe binding conformations, the positional impact of residues involved and discuss implications for functional presentation to CD8
+
T cells.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/16
/ 82/80
/ 82/83
/ Animals
/ Antigens
/ Binding
/ CD8-Positive T-Lymphocytes - cytology
/ CD8-Positive T-Lymphocytes - immunology
/ Enzyme-Linked Immunosorbent Assay
/ Epitopes
/ Histocompatibility antigen HLA
/ Histocompatibility Antigens Class I - immunology
/ HIV
/ Homology
/ Human immunodeficiency virus
/ Humanities and Social Sciences
/ Humans
/ Killer Cells, Natural - immunology
/ Major histocompatibility complex
/ Peptides
/ Residues
/ Science
