Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens

ABSTRACT Human norovirus interacts with the polymorphic human histo-blood group antigens (HBGAs), and this interaction is thought to be important for infection. The genogroup II genotype 4 (GII.4) noroviruses are the dominant cluster, evolve every other year, and are thought to modify their binding...

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Autores principales:	Bishal K. Singh, Mila M. Leuthold, Grant S. Hansman
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2016
Materias:	X-ray crystallography norovirus virus structure Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/f378bb0c89dc4286b732365953f86e16
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spelling	oai:doaj.org-article:f378bb0c89dc4286b732365953f86e162021-11-15T15:21:23ZStructural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens10.1128/mSphere.00049-162379-5042https://doaj.org/article/f378bb0c89dc4286b732365953f86e162016-04-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSphere.00049-16https://doaj.org/toc/2379-5042ABSTRACT Human norovirus interacts with the polymorphic human histo-blood group antigens (HBGAs), and this interaction is thought to be important for infection. The genogroup II genotype 4 (GII.4) noroviruses are the dominant cluster, evolve every other year, and are thought to modify their binding interactions with different HBGA types. Most human noroviruses bind HBGAs, while some strains were found to have minimal or no HBGA interactions. Here, we explain some possible structural constraints for several noroviruses that were found to bind poorly to HBGAs by using X-ray crystallography. We showed that one aspartic acid was flexible or positioned away from the fucose moiety of the HBGAs and this likely hindered binding, although other fucose-interacting residues were perfectly oriented. Interestingly, a neighboring loop also appeared to influence the loop hosting the aspartic acid. These new findings might explain why some human noroviruses bound HBGAs poorly, although further studies are required.Bishal K. SinghMila M. LeutholdGrant S. HansmanAmerican Society for MicrobiologyarticleX-ray crystallographynorovirusvirus structureMicrobiologyQR1-502ENmSphere, Vol 1, Iss 2 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	X-ray crystallography norovirus virus structure Microbiology QR1-502
spellingShingle	X-ray crystallography norovirus virus structure Microbiology QR1-502 Bishal K. Singh Mila M. Leuthold Grant S. Hansman Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens
description	ABSTRACT Human norovirus interacts with the polymorphic human histo-blood group antigens (HBGAs), and this interaction is thought to be important for infection. The genogroup II genotype 4 (GII.4) noroviruses are the dominant cluster, evolve every other year, and are thought to modify their binding interactions with different HBGA types. Most human noroviruses bind HBGAs, while some strains were found to have minimal or no HBGA interactions. Here, we explain some possible structural constraints for several noroviruses that were found to bind poorly to HBGAs by using X-ray crystallography. We showed that one aspartic acid was flexible or positioned away from the fucose moiety of the HBGAs and this likely hindered binding, although other fucose-interacting residues were perfectly oriented. Interestingly, a neighboring loop also appeared to influence the loop hosting the aspartic acid. These new findings might explain why some human noroviruses bound HBGAs poorly, although further studies are required.
format	article
author	Bishal K. Singh Mila M. Leuthold Grant S. Hansman
author_facet	Bishal K. Singh Mila M. Leuthold Grant S. Hansman
author_sort	Bishal K. Singh
title	Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens
title_short	Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens
title_full	Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens
title_fullStr	Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens
title_full_unstemmed	Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens
title_sort	structural constraints on human norovirus binding to histo-blood group antigens
publisher	American Society for Microbiology
publishDate	2016
url	https://doaj.org/article/f378bb0c89dc4286b732365953f86e16
work_keys_str_mv	AT bishalksingh structuralconstraintsonhumannorovirusbindingtohistobloodgroupantigens AT milamleuthold structuralconstraintsonhumannorovirusbindingtohistobloodgroupantigens AT grantshansman structuralconstraintsonhumannorovirusbindingtohistobloodgroupantigens
_version_	1718428167384858624

Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens

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