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Bitter-sweet symphony: glycan–lectin interactions in virus biology

Wander Van Breedam UGent, Stefan Pöhlmann, Herman Favoreel UGent, Raoul de Groot and Hans Nauwynck UGent (2014) FEMS MICROBIOLOGY REVIEWS. 38(4). p.598-632
abstract
Glycans are carbohydrate modifications typically found on proteins or lipids, and can act as ligands for glycan-binding proteins called lectins. Glycans and lectins play crucial roles in the function of cells and organs, and in the immune system of animals and humans. Viral pathogens use glycans and lectins that are encoded by their own or the host genome for their replication and spread. Recent advances in glycobiological research indicate that glycans and lectins mediate key interactions at the virus-host interface, controlling viral spread and/or activation of the immune system. This review reflects on glycan–lectin interactions in the context of viral infection and antiviral immunity. A short introduction illustrates the nature of glycans and lectins, and conveys the basic principles of their interactions. Subsequently, examples are discussed highlighting specific glycan–lectin interactions and how they affect the progress of viral infections, either benefiting the host or the virus. Moreover, glycan and lectin variability and their potential biological consequences are discussed. Finally, the review outlines how recent advances in the glycan–lectin field might be transformed into promising new approaches to antiviral therapy.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (review)
publication status
published
subject
keyword
RESPIRATORY SYNCYTIAL VIRUS, DC-SIGN, TRANSMISSIBLE GASTROENTERITIS CORONAVIRUS, C-TYPE LECTIN, collectin, receptor-destroying enzyme, antiviral, galectin, hemagglutinin, SIALIDASE FUSION PROTEIN, INFLUENZA-A VIRUS, HUMAN-IMMUNODEFICIENCY-VIRUS, INNATE IMMUNE-SYSTEM, SURFACTANT PROTEIN-D, N-LINKED GLYCOSYLATION, MANNOSE-BINDING LECTIN
journal title
FEMS MICROBIOLOGY REVIEWS
Fems Microbiol. Rev.
volume
38
issue
4
pages
598 - 632
Web of Science type
Review
Web of Science id
000339553200002
JCR category
MICROBIOLOGY
JCR impact factor
13.244 (2014)
JCR rank
4/119 (2014)
JCR quartile
1 (2014)
ISSN
0168-6445
DOI
10.1111/1574-6976.12052
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
4211230
handle
http://hdl.handle.net/1854/LU-4211230
date created
2013-12-17 16:02:32
date last changed
2016-12-19 15:38:24
@article{4211230,
  abstract     = {Glycans are carbohydrate modifications typically found on proteins or lipids, and can act as ligands for glycan-binding proteins called lectins. Glycans and lectins play crucial roles in the function of cells and organs, and in the immune system of animals and humans. Viral pathogens use glycans and lectins that are encoded by their own or the host genome for their replication and spread. Recent advances in glycobiological research indicate that glycans and lectins mediate key interactions at the virus-host interface, controlling viral spread and/or activation of the immune system. This review reflects on glycan--lectin interactions in the context of viral infection and antiviral immunity. A short introduction illustrates the nature of glycans and lectins, and conveys the basic principles of their interactions. Subsequently, examples are discussed highlighting specific glycan--lectin interactions and how they affect the progress of viral infections, either benefiting the host or the virus. Moreover, glycan and lectin variability and their potential biological consequences are discussed. Finally, the review outlines how recent advances in the glycan--lectin field might be transformed into promising new approaches to antiviral therapy.},
  author       = {Van Breedam, Wander and P{\"o}hlmann, Stefan and Favoreel, Herman and de Groot, Raoul and Nauwynck, Hans},
  issn         = {0168-6445},
  journal      = {FEMS MICROBIOLOGY REVIEWS},
  keyword      = {RESPIRATORY SYNCYTIAL VIRUS,DC-SIGN,TRANSMISSIBLE GASTROENTERITIS CORONAVIRUS,C-TYPE LECTIN,collectin,receptor-destroying enzyme,antiviral,galectin,hemagglutinin,SIALIDASE FUSION PROTEIN,INFLUENZA-A VIRUS,HUMAN-IMMUNODEFICIENCY-VIRUS,INNATE IMMUNE-SYSTEM,SURFACTANT PROTEIN-D,N-LINKED GLYCOSYLATION,MANNOSE-BINDING LECTIN},
  language     = {eng},
  number       = {4},
  pages        = {598--632},
  title        = {Bitter-sweet symphony: glycan--lectin interactions in virus biology},
  url          = {http://dx.doi.org/10.1111/1574-6976.12052},
  volume       = {38},
  year         = {2014},
}

Chicago
Van Breedam, Wander, Stefan Pöhlmann, Herman Favoreel, Raoul de Groot, and Hans Nauwynck. 2014. “Bitter-sweet Symphony: Glycan–lectin Interactions in Virus Biology.” Fems Microbiology Reviews 38 (4): 598–632.
APA
Van Breedam, W., Pöhlmann, S., Favoreel, H., de Groot, R., & Nauwynck, H. (2014). Bitter-sweet symphony: glycan–lectin interactions in virus biology. FEMS MICROBIOLOGY REVIEWS, 38(4), 598–632.
Vancouver
1.
Van Breedam W, Pöhlmann S, Favoreel H, de Groot R, Nauwynck H. Bitter-sweet symphony: glycan–lectin interactions in virus biology. FEMS MICROBIOLOGY REVIEWS. 2014;38(4):598–632.
MLA
Van Breedam, Wander, Stefan Pöhlmann, Herman Favoreel, et al. “Bitter-sweet Symphony: Glycan–lectin Interactions in Virus Biology.” FEMS MICROBIOLOGY REVIEWS 38.4 (2014): 598–632. Print.