Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Butyrophilin 3A1 binds phosphorylated antigens and stimulates human γδ T cells

Vavassori, Stefano, Kumar, Anil, Wan, Gan Siok, Ramanjaneyulu, Gundimeda S., Cavallari, Marco, El Daker, Sary, Beddoe, Travis, Theodossis, Alex, Williams, Neal K., Gostick, Emma, Price, David, Soudamini, Dinish U., Voon, Kong Kien, Olivo, Malini, Rossjohn, Jamie, Mori, Lucia and De Libero, Gennaro 2013. Butyrophilin 3A1 binds phosphorylated antigens and stimulates human γδ T cells. Nature Immunology 14 (9) , pp. 908-916. 10.1038/ni.2665

Full text not available from this repository.

Abstract

Human T cells that express a T cell antigen receptor (TCR) containing γ-chain variable region 9 and δ-chain variable region 2 (Vγ9Vδ2) recognize phosphorylated prenyl metabolites as antigens in the presence of antigen-presenting cells but independently of major histocompatibility complex (MHC), the MHC class I–related molecule MR1 and antigen-presenting CD1 molecules. Here we used genetic approaches to identify the molecule that binds and presents phosphorylated antigens. We found that the butyrophilin BTN3A1 bound phosphorylated antigens with low affinity, at a stoichiometry of 1:1, and stimulated mouse T cells with transgenic expression of a human Vγ9Vδ2 TCR. The structures of the BTN3A1 distal domain in complex with host- or microbe-derived phosphorylated antigens had an immunoglobulin-like fold in which the antigens bound in a shallow pocket. Soluble Vγ9Vδ2 TCR interacted specifically with BTN3A1-antigen complexes. Accordingly, BTN3A1 represents an antigen-presenting molecule required for the activation of Vγ9Vδ2 T cells.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Systems Immunity Research Institute (SIURI)
Subjects: R Medicine > R Medicine (General)
Publisher: Nature Publishing Group
ISSN: 1529-2908
Last Modified: 16 Nov 2017 20:28
URI: http://orca.cf.ac.uk/id/eprint/52383

Citation Data

Cited 180 times in Scopus. View in Scopus. Powered By Scopus® Data

Cited 86 times in Web of Science. View in Web of Science.

Actions (repository staff only)

Edit Item Edit Item