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Norovirus drug candidates that inhibit viral capsid attachment to human histo-blood group antigens
KTH, School of Engineering Sciences (SCI), Theoretical Physics.
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2016 (English)In: Antiviral Research, ISSN 0166-3542, E-ISSN 1872-9096, Vol. 133, 14-22 p.Article in journal (Refereed) Published
Abstract [en]

Human noroviruses are the leading causative agents of epidemic and sporadic viral gastroenteritis and childhood diarrhoea worldwide. Human histo-blood group antigens (HBGA) serve as receptors for norovirus capsid protein attachment and play a critical role in infection. This makes HBGA-norovirus binding a promising target for drug development. Recently solved crystal structures of norovirus bound to HBGA have provided a structural basis for identification of potential anti-norovirus drugs and subsequently performed in silico and in vitro drug screens have identified compounds that block norovirus binding and may thereby serve as structural templates for design of therapeutic norovirus inhibitors. This review explores norovirus therapeutic options based on the strategy of blocking norovirus-HBGA binding.

Place, publisher, year, edition, pages
Elsevier, 2016. Vol. 133, 14-22 p.
Keyword [en]
Antiviral therapy, Binding inhibitors, Human histo-blood group antigen, Norovirus, Norovirus capsid proteins
National Category
Physical Sciences
Identifiers
URN: urn:nbn:se:kth:diva-194909DOI: 10.1016/j.antiviral.2016.07.006ScopusID: 2-s2.0-84978646169OAI: oai:DiVA.org:kth-194909DiVA: diva2:1044421
Note

QC 20161103

Available from: 2016-11-03 Created: 2016-11-01 Last updated: 2016-11-03Bibliographically approved

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