Structural basis for plastic glycolipid recognition of the C-type lectin Mincle.

Binding Sites Cord Factors / chemistry Glycolipids / chemistry Lectins, C-Type / chemistry Mutagenesis Humans
C-type lectin receptor adjuvant cell surface receptors glycolipid innate immunity mycobacteria nuclear magnetic resonance pattern recognition receptor

Journal

Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697

Informations de publication

Date de publication:
07 09 2023
Historique:
received: 18 05 2021
revised: 26 04 2023
accepted: 26 05 2023
medline: 11 9 2023
pubmed: 23 6 2023
entrez: 22 6 2023
Statut: ppublish

Résumé

Mincle (macrophage-inducible C-type lectin, CLEC4E) is a C-type lectin immune-stimulatory receptor for cord factor, trehalose dimycolate (TDM), which serves as a potent component of adjuvants. The recognition of glycolipids by Mincle, especially their lipid parts, is poorly understood. Here, we performed nuclear magnetic resonance analysis, revealing that titration of trehalose harboring a linear short acyl chain showed a chemical shift perturbation of hydrophobic residues next to the Ca-binding site. Notably, there were split signals for Tyr201 upon complex formation, indicating two binding modes for the acyl chain. In addition, most Mincle residues close to the Ca-binding site showed no observable signals, suggesting their mobility on an ∼ ms scale even after complex formation. Mutagenesis study supported two putative lipid-binding modes for branched acyl-chain TDM binding. These results provide novel insights into the plastic-binding modes of Mincle toward a wide range of glycol- and glycerol-lipids, important for rational adjuvant development.

Identifiants

DOI: 10.1016/j.str.2023.05.018 PMID: 37348496
pubmed: 37348496
pii: S0969-2126(23)00194-6
doi: 10.1016/j.str.2023.05.018
pii:
doi:

Substances chimiques

Cord Factors 0
Glycolipids 0
Lectins, C-Type 0
CLEC4D protein, human 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1077-1085.e5

Informations de copyright

Copyright © 2023 Elsevier Ltd. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

Auteurs

Atsushi Furukawa (A)

Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; Faculty of Pharmaceutical Sciences, Institute of Medical, Pharmaceutical and Health Sciences, Kanazawa University, Kanazawa 920-1192, Japan.

Yusuke Shuchi (Y)

Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.

Jiaqi Wang (J)

Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.

Pablo Adrian Guillen-Poza (PA)

Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.

Shigenari Ishizuka (S)

Department of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Suita 565-0871, Japan; Laboratory of Molecular Immunology, Immunology Frontier Research Center, Osaka University, Suita 565-0871, Japan.

Misuzu Kagoshima (M)

Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.

Risa Ikeno (R)

Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.

Hiroyuki Kumeta (H)

Faculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, Japan.

Sho Yamasaki (S)

Department of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Suita 565-0871, Japan; Laboratory of Molecular Immunology, Immunology Frontier Research Center, Osaka University, Suita 565-0871, Japan.

Takanori Matsumaru (T)

Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; Department of Chemistry, Faculty of Science and Technology, Keio University, Yokohama 223-8522, Japan.

Takashi Saitoh (T)

Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; Department of Medicinal Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University of Science, Sapporo 006-8585, Japan.

Katsumi Maenaka (K)

Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; Global Station for Biosurfaces and Drug Discovery, Hokkaido University, Sapporo 060-0812, Japan; Hokkaido University Institute for Vaccine Research & Development, Sapporo 060-0812, Japan. Electronic address: maenaka@pharm.hokudai.ac.jp.

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Classifications MeSH

questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Sites de fixation › Structural basis for plastic glycolipid...
questionsmedicales.fr › Facteurs biologiques › Toxines biologiques › Toxines bactériennes › Facteurs cord › Structural basis for plastic glycolipid...
questionsmedicales.fr › Lipides › Glycolipides › Structural basis for plastic glycolipid...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Lectines › Lectines de type C › Structural basis for plastic glycolipid...
questionsmedicales.fr › Phénomènes génétiques › Mutagenèse › Structural basis for plastic glycolipid...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Structural basis for plastic glycolipid...