Journal Article/Review

FZJ-2015-04430

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The sweet spot: defining virus-sialic acid interactions

Stencel-Baerenwald, J. E. ; Reiss, K.FZJ* ; Reiter, D. M. ; Stehle, T. ; Dermody, T. S. (Corresponding Author)

2014
Nature Publ. Group Basingstoke

This record in other databases:      

Please use a persistent id in citations: doi:10.1038/nrmicro3346

Abstract: Viral infections are initiated by attachment of the virus to host cell surface receptors, including sialic acid-containing glycans. It is now possible to rapidly identify specific glycan receptors using glycan array screening, to define atomic-level structures of virus-glycan complexes and to alter the glycan-binding site to determine the function of glycan engagement in viral disease. This Review highlights general principles of virus-glycan interactions and provides specific examples of sialic acid binding by viruses with stalk-like attachment proteins, including influenza virus, reovirus, adenovirus and rotavirus. Understanding virus-glycan interactions is essential to combating viral infections and designing improved viral vectors for therapeutic applications.

Keyword(s): Polysaccharides ; Receptors, Cell Surface ; Receptors, Virus ; N-Acetylneuraminic Acid

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 452 - Structural Biology (POF2-452) (POF2-452)

Appears in the scientific report 2015

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Database coverage:
; BIOSIS Previews ; BIOSIS Reviews Reports And Meetings ; Current Contents - Life Sciences ; IF >= 20 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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