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Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding

Abstract:

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-...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-018-05459-z

Authors


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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM Experimental Medicine
Oxford college:
Linacre College
Role:
Author
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Institution:
University of Oxford
Division:
MPLS Division
Department:
NDM; Wellcome Centre for Human Genetics
Role:
Author
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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Role:
Author
ORCID:
0000-0002-0587-7560
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM; Wellcome Centre for Human Genetics
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Role:
Author
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Funding agency for:
Jones, E
Grant:
203141/Z/16/Z
More from this funder
Funding agency for:
Jones, E
Grant:
203141/Z/16/Z
More from this funder
Funding agency for:
Jones, E
Grant:
203141/Z/16/Z
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Publisher:
Springer Nature Publisher's website
Journal:
Nature Communications Journal website
Volume:
9
Publication date:
2018-08-07
Acceptance date:
2018-07-04
DOI:
EISSN:
2041-1723
ISSN:
2041-1723
Pmid:
30087334
Source identifiers:
904970
Language:
English
Keywords:
Pubs id:
pubs:904970
UUID:
uuid:aab7a8b3-82f8-4cad-9efc-78e8baf57f59
Local pid:
pubs:904970
Deposit date:
2018-08-16

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