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Mannose–fucose recognition by DC-SIGN
Dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN). DC-SIGN is a C-type lectin receptor that recognizes N-linked high-mannose oligosaccharides and branched fucosylated structures. It is now clear that the biological role of DC-SIGN is two-fold. It is primarily expressed by dendritic cells...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7150001/ http://dx.doi.org/10.1016/B978-0-12-374546-0.00034-1 |
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author | Geurtsen, Jeroen Driessen, Nicole N. Appelmelk, Ben J. |
author_facet | Geurtsen, Jeroen Driessen, Nicole N. Appelmelk, Ben J. |
author_sort | Geurtsen, Jeroen |
collection | PubMed |
description | Dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN). DC-SIGN is a C-type lectin receptor that recognizes N-linked high-mannose oligosaccharides and branched fucosylated structures. It is now clear that the biological role of DC-SIGN is two-fold. It is primarily expressed by dendritic cells and mediates important functions necessary for the induction of successful immune responses that are essential for the clearance of microbial infections, such as the capture, destruction, and presentation of microbial pathogens to induce successful immune responses. Yet, on the other hand, pathogens may also exploit DC-SIGN to modulate DC functioning thereby skewing the immune response and promoting their own survival. This chapter presents an overview of the structure of DC-SIGN and its expression pattern among immune cells. The current state of knowledge of DC-SIGN-carbohydrate interactions is discussed and how these interactions influence dendritic cell functioning is examined. The molecular aspects that underlie the selectivity of DC-SIGN for mannose-and fucose-containing carbohydrates are detailed. Furthermore, the chapter discusses the role of DC-SIGN in dendritic cell biology and how certain bacterial pathogens exploit DC-SIGN to escape immune surveillance. |
format | Online Article Text |
id | pubmed-7150001 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
record_format | MEDLINE/PubMed |
spelling | pubmed-71500012020-04-13 Mannose–fucose recognition by DC-SIGN Geurtsen, Jeroen Driessen, Nicole N. Appelmelk, Ben J. Microbial Glycobiology Article Dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN). DC-SIGN is a C-type lectin receptor that recognizes N-linked high-mannose oligosaccharides and branched fucosylated structures. It is now clear that the biological role of DC-SIGN is two-fold. It is primarily expressed by dendritic cells and mediates important functions necessary for the induction of successful immune responses that are essential for the clearance of microbial infections, such as the capture, destruction, and presentation of microbial pathogens to induce successful immune responses. Yet, on the other hand, pathogens may also exploit DC-SIGN to modulate DC functioning thereby skewing the immune response and promoting their own survival. This chapter presents an overview of the structure of DC-SIGN and its expression pattern among immune cells. The current state of knowledge of DC-SIGN-carbohydrate interactions is discussed and how these interactions influence dendritic cell functioning is examined. The molecular aspects that underlie the selectivity of DC-SIGN for mannose-and fucose-containing carbohydrates are detailed. Furthermore, the chapter discusses the role of DC-SIGN in dendritic cell biology and how certain bacterial pathogens exploit DC-SIGN to escape immune surveillance. 2010 2009-10-22 /pmc/articles/PMC7150001/ http://dx.doi.org/10.1016/B978-0-12-374546-0.00034-1 Text en Copyright © 2010 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Geurtsen, Jeroen Driessen, Nicole N. Appelmelk, Ben J. Mannose–fucose recognition by DC-SIGN |
title | Mannose–fucose recognition by DC-SIGN |
title_full | Mannose–fucose recognition by DC-SIGN |
title_fullStr | Mannose–fucose recognition by DC-SIGN |
title_full_unstemmed | Mannose–fucose recognition by DC-SIGN |
title_short | Mannose–fucose recognition by DC-SIGN |
title_sort | mannose–fucose recognition by dc-sign |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7150001/ http://dx.doi.org/10.1016/B978-0-12-374546-0.00034-1 |
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