Ontology highlight
ABSTRACT:
SUBMITTER: Mallagaray A
PROVIDER: S-EPMC6428809 | biostudies-literature | 2019 Mar
REPOSITORIES: biostudies-literature
Mallagaray Alvaro A Creutznacher Robert R Dülfer Jasmin J Mayer Philipp H O PHO Grimm Lena Lisbeth LL Orduña Jose Maria JM Trabjerg Esben E Stehle Thilo T Rand Kasper D KD Blaum Bärbel S BS Uetrecht Charlotte C Peters Thomas T
Nature communications 20190321 1
Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employ protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P-domain of a prevalent virus strain (GII.4). We report a highly selective transformation of asparagine 373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This ...[more]