TY  - JOUR
AU  - Mallagaray, Alvaro
AU  - Lockhauserbäumer, Julia
AU  - Hansman, Grant
AU  - Uetrecht, Charlotte
AU  - Peters, Thomas
TI  - Attachment of Norovirus to Histo Blood Group Antigens: A Cooperative Multistep Process
JO  - Angewandte Chemie / International edition
VL  - 54
IS  - 41
SN  - 1433-7851
CY  - Weinheim
PB  - Wiley-VCH
M1  - PUBDB-2015-03498
SP  - 12014 – 12019
PY  - 2015
AB  - Human noroviruses recognize histo blood group antigens (HBGAs) as cellular attachment factors. Recently, it has been discovered that norovirus infection can be significantly enhanced by HBGA binding. Yet the attachment process and how it promotes host-cell entry is only poorly understood. The binding of a norovirus protruding (P) domain of a predominant GII.4 Saga strain to HBGAs at atomic resolution was studied. So far, independent and equivalent multiple binding sites were held responsible for attachment. Using NMR experiments we show that norovirus-HBGA binding is a cooperative multi-step process, and native mass spectrometry reveals four instead of two HBGA binding sites per P-dimer. An accompanying crystallographic study has disclosed four instead of two l-fucose binding sites per P-dimer of a related GII.10 strain1 further supporting our findings. We have uncovered a novel paradigm for norovirus-HBGA recognition that will inspire further studies into norovirus–host interactions.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000363396000020
C6  - pmid:26329854
DO  - DOI:10.1002/anie.201505672
UR  - https://bib-pubdb1.desy.de/record/224307
ER  -