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Norovirus drug candidates that inhibit viral capsid attachment to human histo-blood group antigens
KTH, Skolan för teknikvetenskap (SCI), Teoretisk fysik. KTH, Centra, Science for Life Laboratory, SciLifeLab.
Vise andre og tillknytning
2016 (engelsk)Inngår i: Antiviral Research, ISSN 0166-3542, E-ISSN 1872-9096, Vol. 133, s. 14-22Artikkel, forskningsoversikt (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
Elsevier, 2016. Vol. 133, s. 14-22
Emneord [en]
Antiviral therapy, Binding inhibitors, Human histo-blood group antigen, Norovirus, Norovirus capsid proteins
HSV kategori
Identifikatorer
URN: urn:nbn:se:kth:diva-194909DOI: 10.1016/j.antiviral.2016.07.006ISI: 000384856200003Scopus ID: 2-s2.0-84978646169OAI: oai:DiVA.org:kth-194909DiVA, id: diva2:1044421
Merknad

QC 20161103

Tilgjengelig fra: 2016-11-03 Laget: 2016-11-01 Sist oppdatert: 2019-09-19bibliografisk kontrollert

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