Article (Scientific journals)
Initial Step of Virus Entry: Virion Binding to Cell-Surface Glycans.
Koehler, Melanie; Delguste, Martin; Sieben, Christian et al.
2020In Annual Review of Virology
Peer reviewed
 

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Abstract :
[en] Virus infection is an intricate process that requires the concerted action of both viral and host cell components. Entry of viruses into cells is initiated by interactions between viral proteins and cell-surface receptors. Various cell-surface glycans function as initial, usually low-affinity attachment factors, providing a first anchor of the virus to the cell surface, and further facilitate high-affinity binding to virus-specific cell-surface receptors, while other glycans function as specific entry receptors themselves. It is now possible to rapidly identify specific glycan receptors using different techniques, define atomic-level structures of virus-glycan complexes, and study these interactions at the single-virion level. This review provides a detailed overview of the role of glycans in viral infection and highlights experimental approaches to study virus-glycan binding along with specific examples. In particular, we highlight the development of the atomic force microscope to investigate interactions with glycans at the single-virion level directly on living mammalian cells, which offers new perspectives to better understand virus-glycan interactions in physiologically relevant conditions. Expected final online publication date for the Annual Review of Virology, Volume 7 is September 29, 2020. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.
Disciplines :
Microbiology
Author, co-author :
Koehler, Melanie
Delguste, Martin
Sieben, Christian
Gillet, Laurent  ;  Université de Liège - ULiège > Département des maladies infectieuses et parasitaires (DMI) > Vaccinologie vétérinaire
Alsteens, David
Language :
English
Title :
Initial Step of Virus Entry: Virion Binding to Cell-Surface Glycans.
Publication date :
2020
Journal title :
Annual Review of Virology
ISSN :
2327-056X
eISSN :
2327-0578
Publisher :
Annual Reviews
Peer reviewed :
Peer reviewed
Available on ORBi :
since 17 May 2020

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