Fucoidan and Derived Oligo-Fucoses: Structural Features with Relevance in Competitive Inhibition of Gastrointestinal Norovirus Binding

Norovirus infections belong to the most common causes of human gastroenteritis worldwide and epidemic outbreaks are responsible for hundreds of thousands of deaths annually. In humans, noroviruses are known to bind to gastrointestinal epithelia via recognition of blood-group active mucin-type O-glyc...

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Autores principales:	Franz-Georg Hanisch, Cem Aydogan, Horst Schroten
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	fucoidan norovirus carbohydrate-lectin binding food additive mass spectrometry Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/01ee4990b9ed48ff8dcf014fe3dc6617
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spelling	oai:doaj.org-article:01ee4990b9ed48ff8dcf014fe3dc66172021-11-25T18:12:38ZFucoidan and Derived Oligo-Fucoses: Structural Features with Relevance in Competitive Inhibition of Gastrointestinal Norovirus Binding10.3390/md191105911660-3397https://doaj.org/article/01ee4990b9ed48ff8dcf014fe3dc66172021-10-01T00:00:00Zhttps://www.mdpi.com/1660-3397/19/11/591https://doaj.org/toc/1660-3397Norovirus infections belong to the most common causes of human gastroenteritis worldwide and epidemic outbreaks are responsible for hundreds of thousands of deaths annually. In humans, noroviruses are known to bind to gastrointestinal epithelia via recognition of blood-group active mucin-type O-glycans. Considering the involvement of <span style="font-variant: small-caps;">l</span>-α-fucose residues in these glycans, their high valency on epithelial surfaces far surpasses the low affinity, though specific interactions of monovalent milk oligosaccharides. Based on these findings, we attempted to identify polyfucoses (fucans) with the capacity to block binding of the currently most prevalent norovirus strain GII.4 (Sydney, 2012, JX459908) to human and animal gastrointestinal mucins. We provide evidence that inhibitory effects on capsid binding are exerted in a competitive manner by α-fucosyl residues on <i>Fucus vesiculosus</i> fucoidan, but also on the galacto-fucan from <i>Undaria pinnatifida</i> and their oligo-fucose processing products. Insight into novel structural aspects of fucoidan and derived oligosaccharides from low-mass <i>Undaria pinnatifida</i> were revealed by GCMS and MALDI mass spectrometry. In targeting noroviral spread attenuation, this study provides first steps towards a prophylactic food additive that is produced from algal species.Franz-Georg HanischCem AydoganHorst SchrotenMDPI AGarticlefucoidannoroviruscarbohydrate-lectin bindingfood additivemass spectrometryBiology (General)QH301-705.5ENMarine Drugs, Vol 19, Iss 591, p 591 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	fucoidan norovirus carbohydrate-lectin binding food additive mass spectrometry Biology (General) QH301-705.5
spellingShingle	fucoidan norovirus carbohydrate-lectin binding food additive mass spectrometry Biology (General) QH301-705.5 Franz-Georg Hanisch Cem Aydogan Horst Schroten Fucoidan and Derived Oligo-Fucoses: Structural Features with Relevance in Competitive Inhibition of Gastrointestinal Norovirus Binding
description	Norovirus infections belong to the most common causes of human gastroenteritis worldwide and epidemic outbreaks are responsible for hundreds of thousands of deaths annually. In humans, noroviruses are known to bind to gastrointestinal epithelia via recognition of blood-group active mucin-type O-glycans. Considering the involvement of <span style="font-variant: small-caps;">l</span>-α-fucose residues in these glycans, their high valency on epithelial surfaces far surpasses the low affinity, though specific interactions of monovalent milk oligosaccharides. Based on these findings, we attempted to identify polyfucoses (fucans) with the capacity to block binding of the currently most prevalent norovirus strain GII.4 (Sydney, 2012, JX459908) to human and animal gastrointestinal mucins. We provide evidence that inhibitory effects on capsid binding are exerted in a competitive manner by α-fucosyl residues on <i>Fucus vesiculosus</i> fucoidan, but also on the galacto-fucan from <i>Undaria pinnatifida</i> and their oligo-fucose processing products. Insight into novel structural aspects of fucoidan and derived oligosaccharides from low-mass <i>Undaria pinnatifida</i> were revealed by GCMS and MALDI mass spectrometry. In targeting noroviral spread attenuation, this study provides first steps towards a prophylactic food additive that is produced from algal species.
format	article
author	Franz-Georg Hanisch Cem Aydogan Horst Schroten
author_facet	Franz-Georg Hanisch Cem Aydogan Horst Schroten
author_sort	Franz-Georg Hanisch
title	Fucoidan and Derived Oligo-Fucoses: Structural Features with Relevance in Competitive Inhibition of Gastrointestinal Norovirus Binding
title_short	Fucoidan and Derived Oligo-Fucoses: Structural Features with Relevance in Competitive Inhibition of Gastrointestinal Norovirus Binding
title_full	Fucoidan and Derived Oligo-Fucoses: Structural Features with Relevance in Competitive Inhibition of Gastrointestinal Norovirus Binding
title_fullStr	Fucoidan and Derived Oligo-Fucoses: Structural Features with Relevance in Competitive Inhibition of Gastrointestinal Norovirus Binding
title_full_unstemmed	Fucoidan and Derived Oligo-Fucoses: Structural Features with Relevance in Competitive Inhibition of Gastrointestinal Norovirus Binding
title_sort	fucoidan and derived oligo-fucoses: structural features with relevance in competitive inhibition of gastrointestinal norovirus binding
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/01ee4990b9ed48ff8dcf014fe3dc6617
work_keys_str_mv	AT franzgeorghanisch fucoidanandderivedoligofucosesstructuralfeatureswithrelevanceincompetitiveinhibitionofgastrointestinalnorovirusbinding AT cemaydogan fucoidanandderivedoligofucosesstructuralfeatureswithrelevanceincompetitiveinhibitionofgastrointestinalnorovirusbinding AT horstschroten fucoidanandderivedoligofucosesstructuralfeatureswithrelevanceincompetitiveinhibitionofgastrointestinalnorovirusbinding
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Fucoidan and Derived Oligo-Fucoses: Structural Features with Relevance in Competitive Inhibition of Gastrointestinal Norovirus Binding

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