TY - JOUR
T1 - Norovirus, glycans and attachment
AU - Taube, Stefan
AU - Mallagaray, Alvaro
AU - Peters, Thomas
N1 - Funding Information:
This work has been supported by the German Research Council (DFG) as part of a research unit ( ViroCarb , FOR2327, Grant No. DFG Pe494/12-1 (T.P.) and DFG TA1093-2 (S.T.)). A.M. has also been a recipient of a Marie Curie fellowship (2013-2015) within the 7 th Framework Programme of the EU (Grant Agreement No. 329485, NoroCarb ). S.T. is also funded by the DFG grant TA1093-1.
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 2018/8
Y1 - 2018/8
N2 - Noroviruses engage glycans as essential attachment factors to promote infection of host cells. The past decade has witnessed significant progress in the field of norovirus research. Cell culture systems and animal models have become available, and structural biology and biophysics have significantly expanded our understanding of norovirus–glycan interactions. From crystallography, many high-resolution crystal structures are now available disclosing key elements of glycan recognition at atomic resolution. On this basis, NMR spectroscopy, native mass spectrometry, and biophysical techniques targeting membrane attached glycans have raised more intricate questions about the nature of norovirus–glycan attachment implying that a static picture of glycan recognition is insufficient. Linking novel biophysical observations to biological aspects of norovirus host cell entry is a challenge. Therefore, in a first step, this review summarizes and discusses recent biophysical approaches potentially paving the way to a dynamical picture of norovirus-glycan attachment. Novel insights from norovirus–glycan binding studies are put into perspective with current general developments in the field of protein–glycan interactions, hopefully provoking new ideas for norovirus research.
AB - Noroviruses engage glycans as essential attachment factors to promote infection of host cells. The past decade has witnessed significant progress in the field of norovirus research. Cell culture systems and animal models have become available, and structural biology and biophysics have significantly expanded our understanding of norovirus–glycan interactions. From crystallography, many high-resolution crystal structures are now available disclosing key elements of glycan recognition at atomic resolution. On this basis, NMR spectroscopy, native mass spectrometry, and biophysical techniques targeting membrane attached glycans have raised more intricate questions about the nature of norovirus–glycan attachment implying that a static picture of glycan recognition is insufficient. Linking novel biophysical observations to biological aspects of norovirus host cell entry is a challenge. Therefore, in a first step, this review summarizes and discusses recent biophysical approaches potentially paving the way to a dynamical picture of norovirus-glycan attachment. Novel insights from norovirus–glycan binding studies are put into perspective with current general developments in the field of protein–glycan interactions, hopefully provoking new ideas for norovirus research.
UR - http://www.scopus.com/inward/record.url?scp=85046846157&partnerID=8YFLogxK
U2 - 10.1016/j.coviro.2018.04.007
DO - 10.1016/j.coviro.2018.04.007
M3 - Scientific review articles
C2 - 29754860
AN - SCOPUS:85046846157
SN - 1879-6257
VL - 31
SP - 33
EP - 42
JO - Current Opinion in Virology
JF - Current Opinion in Virology
ER -