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

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 o...

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Autores principales: Rambaruth, Neela D. S., Jégouzo, Sabine A. F., Marlor, Hayley, Taylor, Maureen E., Drickamer, Kurt
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4533885/
https://www.ncbi.nlm.nih.gov/pubmed/25884549
http://dx.doi.org/10.3390/molecules20046670
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author Rambaruth, Neela D. S.
Jégouzo, Sabine A. F.
Marlor, Hayley
Taylor, Maureen E.
Drickamer, Kurt
author_facet Rambaruth, Neela D. S.
Jégouzo, Sabine A. F.
Marlor, Hayley
Taylor, Maureen E.
Drickamer, Kurt
author_sort Rambaruth, Neela D. S.
collection PubMed
description 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.
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spelling pubmed-45338852015-08-12 Mouse Mincle: Characterization as a Model for Human Mincle and Evolutionary Implications Rambaruth, Neela D. S. Jégouzo, Sabine A. F. Marlor, Hayley Taylor, Maureen E. Drickamer, Kurt Molecules Article 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. MDPI 2015-04-15 /pmc/articles/PMC4533885/ /pubmed/25884549 http://dx.doi.org/10.3390/molecules20046670 Text en © 2015 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Rambaruth, Neela D. S.
Jégouzo, Sabine A. F.
Marlor, Hayley
Taylor, Maureen E.
Drickamer, Kurt
Mouse Mincle: Characterization as a Model for Human Mincle and Evolutionary Implications
title Mouse Mincle: Characterization as a Model for Human Mincle and Evolutionary Implications
title_full Mouse Mincle: Characterization as a Model for Human Mincle and Evolutionary Implications
title_fullStr Mouse Mincle: Characterization as a Model for Human Mincle and Evolutionary Implications
title_full_unstemmed Mouse Mincle: Characterization as a Model for Human Mincle and Evolutionary Implications
title_short Mouse Mincle: Characterization as a Model for Human Mincle and Evolutionary Implications
title_sort mouse mincle: characterization as a model for human mincle and evolutionary implications
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4533885/
https://www.ncbi.nlm.nih.gov/pubmed/25884549
http://dx.doi.org/10.3390/molecules20046670
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