Mechanism of pathogen recognition by human dectin-2

Feinberg, Hadar; Jégouzo, Sabine A.  F.; Rex, Maximus J.; Drickamer, Kurt; Weis, William I.; Taylor, Maureen E.

doi:10.1074/jbc.m117.799080

Title: Mechanism of pathogen recognition by human dectin-2

Journal Article · Mon Jun 26 00:00:00 EDT 2017 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.m117.799080· OSTI ID:1625085

Feinberg, Hadar ^[1]; Jégouzo, Sabine A. F. ^[2]; Rex, Maximus J. ^[2]; Drickamer, Kurt ^[2]; Weis, William I. ^[1]; Taylor, Maureen E. ^[2]

Stanford Univ., CA (United States). School of Medicine. Dept. of Structural Biology and and Molecular and Cellular Physiology
Imperial College, London (United Kingdom). Dept. of Life Sciences

Dectin-2, a C-type lectin on macrophages and other cells of the innate immune system, functions in response to pathogens, particularly fungi. The carbohydrate-recognition domain (CRD) in dectin-2 is linked to a transmembrane sequence that interacts with the common Fc receptor subunit to initiate immune signaling. The molecular mechanism by which dectin-2 selectively binds to pathogens has been investigated by characterizing the CRD expressed in a bacterial system. Competition binding studies indicated that the CRD binds to monosaccharides with modest affinity and that affinity was greatly enhanced for mannose-linked1-2 or1-4 to a second mannose residue. Glycan array analysis confirmed selective binding of the CRD to glycans that contain Man1-2Man epitopes. Crystals of the CRD in complex with a mammalian-type high-mannose Man9GlcNAc2 oligosaccharide exhibited interaction with Man1–2Man on two different termini of the glycan, with the reducing-end mannose residue ligated to Ca2 in a primary binding site and the nonreducing terminal mannose residue occupying an adjacent secondary site. Comparison of the binding sites in DC-SIGN and langerin, two other pathogen-binding receptors of the innate immune system, revealed why these two binding sites accommodate only terminal Man1-2Man structures, whereas dectin-2 can bind Man1–2Man in internal positions in mannans and other polysaccharides. The specificity and geometry of the dectin-2-binding site provide the molecular mechanism for binding of dectin-2 to fungal mannans and also to bacterial lipopolysaccharides, capsular polysaccharides, and lipoarabinomannans that contain the Man1-2Man disaccharide unit.

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Research Organization:: SLAC National Accelerator Lab., Menlo Park, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1625085

Journal Information:: Journal of Biological Chemistry, Vol. 292, Issue 32; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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