From structure to function – Ligand recognition by myeloid C-type lectin receptors
The relevance of protein-glycan interactions in immunity has long been underestimated. Yet, the immune system possesses numerous classes of glycan-binding proteins, so-called lectins. Of specific interest is the group of myeloid C-type lectin receptors (CLRs) as they are mainly expressed by myeloid...
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Elsevier
2022-01-01
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Series: | Computational and Structural Biotechnology Journal |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2001037022004664 |
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author | Swantje Fischer Felix Stegmann Vinayaga Srinivasan Gnanapragassam Bernd Lepenies |
author_facet | Swantje Fischer Felix Stegmann Vinayaga Srinivasan Gnanapragassam Bernd Lepenies |
author_sort | Swantje Fischer |
collection | DOAJ |
description | The relevance of protein-glycan interactions in immunity has long been underestimated. Yet, the immune system possesses numerous classes of glycan-binding proteins, so-called lectins. Of specific interest is the group of myeloid C-type lectin receptors (CLRs) as they are mainly expressed by myeloid cells and play an important role in the initiation of an immune response. Myeloid CLRs represent a major group amongst pattern recognition receptors (PRRs), placing them at the center of the rapidly growing field of glycoimmunology. CLRs have evolved to encompass a wide range of structures and functions and to recognize a large number of glycans and many other ligands from different classes of biopolymers. This review aims at providing the reader with an overview of myeloid CLRs and selected ligands, while highlighting recent insights into CLR-ligand interactions. Subsequently, methodological approaches in CLR-ligand research will be presented. Finally, this review will discuss how CLR-ligand interactions culminate in immunological functions, how glycan mimicry favors immune escape by pathogens, and in which way immune responses can be affected by CLR-ligand interactions in the long term. |
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format | Article |
id | doaj.art-161193ca96a94f61bf8bb7d4c155f8c7 |
institution | Directory Open Access Journal |
issn | 2001-0370 |
language | English |
last_indexed | 2024-04-11T05:18:05Z |
publishDate | 2022-01-01 |
publisher | Elsevier |
record_format | Article |
series | Computational and Structural Biotechnology Journal |
spelling | doaj.art-161193ca96a94f61bf8bb7d4c155f8c72022-12-24T04:54:49ZengElsevierComputational and Structural Biotechnology Journal2001-03702022-01-012057905812From structure to function – Ligand recognition by myeloid C-type lectin receptorsSwantje Fischer0Felix Stegmann1Vinayaga Srinivasan Gnanapragassam2Bernd Lepenies3Institute for Immunology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany; Research Center for Emerging Infections and Zoonoses, University of Veterinary Medicine Hannover, 30559 Hannover, GermanyInstitute for Immunology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany; Research Center for Emerging Infections and Zoonoses, University of Veterinary Medicine Hannover, 30559 Hannover, GermanyInstitute for Immunology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany; Research Center for Emerging Infections and Zoonoses, University of Veterinary Medicine Hannover, 30559 Hannover, GermanyInstitute for Immunology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany; Research Center for Emerging Infections and Zoonoses, University of Veterinary Medicine Hannover, 30559 Hannover, Germany; Corresponding author.The relevance of protein-glycan interactions in immunity has long been underestimated. Yet, the immune system possesses numerous classes of glycan-binding proteins, so-called lectins. Of specific interest is the group of myeloid C-type lectin receptors (CLRs) as they are mainly expressed by myeloid cells and play an important role in the initiation of an immune response. Myeloid CLRs represent a major group amongst pattern recognition receptors (PRRs), placing them at the center of the rapidly growing field of glycoimmunology. CLRs have evolved to encompass a wide range of structures and functions and to recognize a large number of glycans and many other ligands from different classes of biopolymers. This review aims at providing the reader with an overview of myeloid CLRs and selected ligands, while highlighting recent insights into CLR-ligand interactions. Subsequently, methodological approaches in CLR-ligand research will be presented. Finally, this review will discuss how CLR-ligand interactions culminate in immunological functions, how glycan mimicry favors immune escape by pathogens, and in which way immune responses can be affected by CLR-ligand interactions in the long term.http://www.sciencedirect.com/science/article/pii/S2001037022004664C-type lectin receptorsLigand identificationSignaling flexibilitySelf-non-self-discriminationImmune modulationHost-pathogen interaction |
spellingShingle | Swantje Fischer Felix Stegmann Vinayaga Srinivasan Gnanapragassam Bernd Lepenies From structure to function – Ligand recognition by myeloid C-type lectin receptors Computational and Structural Biotechnology Journal C-type lectin receptors Ligand identification Signaling flexibility Self-non-self-discrimination Immune modulation Host-pathogen interaction |
title | From structure to function – Ligand recognition by myeloid C-type lectin receptors |
title_full | From structure to function – Ligand recognition by myeloid C-type lectin receptors |
title_fullStr | From structure to function – Ligand recognition by myeloid C-type lectin receptors |
title_full_unstemmed | From structure to function – Ligand recognition by myeloid C-type lectin receptors |
title_short | From structure to function – Ligand recognition by myeloid C-type lectin receptors |
title_sort | from structure to function ligand recognition by myeloid c type lectin receptors |
topic | C-type lectin receptors Ligand identification Signaling flexibility Self-non-self-discrimination Immune modulation Host-pathogen interaction |
url | http://www.sciencedirect.com/science/article/pii/S2001037022004664 |
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