Next Article in Journal
Coordination and Crystallization Molecules: Their Interactions Affecting the Dimensionality of Metalloporphyrinic SCFs
Next Article in Special Issue
Glycodendrimers and Modified ELISAs: Tools to Elucidate Multivalent Interactions of Galectins 1 and 3
Previous Article in Journal
Optimization of γ-Aminobutyric Acid Production by Lactobacillus plantarum Taj-Apis362 from Honeybees
Previous Article in Special Issue
Heparin/Heparan Sulfate Proteoglycans Glycomic Interactome in Angiogenesis: Biological Implications and Therapeutical Use
Article Menu

Export Article

Open AccessArticle
Molecules 2015, 20(4), 6670-6682;

Mouse Mincle: Characterization as a Model for Human Mincle and Evolutionary Implications

Department of Life Sciences, Imperial College, London SW7 2AZ, UK
Author to whom correspondence should be addressed.
Academic Editor: Els Van Damme
Received: 13 March 2015 / Revised: 7 April 2015 / Accepted: 13 April 2015 / Published: 15 April 2015
(This article belongs to the Special Issue Protein-Carbohydrate Interactions, and Beyond)
Full-Text   |   PDF [2652 KB, uploaded 15 April 2015]   |  


Mincle, the macrophage-inducible C-type lectin also known as CLEC-4E, binds to the mycobacterial glycolipid trehalose dimycolate and initiates a signaling cascade by serving as a receptor for Mycobacterium tuberculosis and other pathogenic mycobacterial species. Studies of the biological functions of human mincle often rely on mouse models, based on the assumption that the biological properties of the mouse receptor mimic those of the human protein. Experimental support for this assumption has been obtained by expression of the carbohydrate-recognition domain of mouse mincle and characterization of its interaction with small molecule analogs of trehalose dimycolate. The results confirm that the ligand-binding properties of mouse mincle closely parallel those of the human receptor. These findings are consistent with the conservation of key amino acid residues that have been shown to form the ligand-binding site in human and cow mincle. Sequence alignment reveals that these residues are conserved in a wide range of mammalian species, suggesting that mincle has a conserved function in binding ligands that may include endogenous mammalian glycans or pathogen glycans in addition to trehalose dimycolate. View Full-Text
Keywords: glycan-binding receptor; lectin; mycobacteria glycan-binding receptor; lectin; mycobacteria

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Rambaruth, N.D.S.; Jégouzo, S.A.F.; Marlor, H.; Taylor, M.E.; Drickamer, K. Mouse Mincle: Characterization as a Model for Human Mincle and Evolutionary Implications. Molecules 2015, 20, 6670-6682.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top