Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function

Abstract Chitin is an important structural component of numerous fungal pathogens and parasitic nematodes. The human macrophage chitotriosidase (HCHT) is a chitinase that hydrolyses glycosidic bonds between the N-acetyl-D-glucosamine units of this biopolymer. HCHT belongs to the Glycoside Hydrolase...

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Autores principales:	Oscar Crasson, Gaston Courtade, Raphaël R. Léonard, Finn Lillelund Aachmann, François Legrand, Raffaella Parente, Denis Baurain, Moreno Galleni, Morten Sørlie, Marylène Vandevenne
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0ab5cc52c909439b89b969d8a493a705
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spelling	oai:doaj.org-article:0ab5cc52c909439b89b969d8a493a7052021-12-02T11:51:11ZHuman Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function10.1038/s41598-017-02382-z2045-2322https://doaj.org/article/0ab5cc52c909439b89b969d8a493a7052017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02382-zhttps://doaj.org/toc/2045-2322Abstract Chitin is an important structural component of numerous fungal pathogens and parasitic nematodes. The human macrophage chitotriosidase (HCHT) is a chitinase that hydrolyses glycosidic bonds between the N-acetyl-D-glucosamine units of this biopolymer. HCHT belongs to the Glycoside Hydrolase (GH) superfamily and contains a well-characterized catalytic domain appended to a chitin-binding domain (ChBDCHIT1). Although its precise biological function remains unclear, HCHT has been described to be involved in innate immunity. In this study, the molecular basis for interaction with insoluble chitin as well as with soluble chito-oligosaccharides has been determined. The results suggest a new mechanism as a common binding mode for many Carbohydrate Binding Modules (CBMs). Furthermore, using a phylogenetic approach, we have analysed the modularity of HCHT and investigated the evolutionary paths of its catalytic and chitin binding domains. The phylogenetic analyses indicate that the ChBDCHIT1 domain dictates the biological function of HCHT and not its appended catalytic domain. This observation may also be a general feature of GHs. Altogether, our data have led us to postulate and discuss that HCHT acts as an immune catalyser.Oscar CrassonGaston CourtadeRaphaël R. LéonardFinn Lillelund AachmannFrançois LegrandRaffaella ParenteDenis BaurainMoreno GalleniMorten SørlieMarylène VandevenneNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Oscar Crasson Gaston Courtade Raphaël R. Léonard Finn Lillelund Aachmann François Legrand Raffaella Parente Denis Baurain Moreno Galleni Morten Sørlie Marylène Vandevenne Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function
description	Abstract Chitin is an important structural component of numerous fungal pathogens and parasitic nematodes. The human macrophage chitotriosidase (HCHT) is a chitinase that hydrolyses glycosidic bonds between the N-acetyl-D-glucosamine units of this biopolymer. HCHT belongs to the Glycoside Hydrolase (GH) superfamily and contains a well-characterized catalytic domain appended to a chitin-binding domain (ChBDCHIT1). Although its precise biological function remains unclear, HCHT has been described to be involved in innate immunity. In this study, the molecular basis for interaction with insoluble chitin as well as with soluble chito-oligosaccharides has been determined. The results suggest a new mechanism as a common binding mode for many Carbohydrate Binding Modules (CBMs). Furthermore, using a phylogenetic approach, we have analysed the modularity of HCHT and investigated the evolutionary paths of its catalytic and chitin binding domains. The phylogenetic analyses indicate that the ChBDCHIT1 domain dictates the biological function of HCHT and not its appended catalytic domain. This observation may also be a general feature of GHs. Altogether, our data have led us to postulate and discuss that HCHT acts as an immune catalyser.
format	article
author	Oscar Crasson Gaston Courtade Raphaël R. Léonard Finn Lillelund Aachmann François Legrand Raffaella Parente Denis Baurain Moreno Galleni Morten Sørlie Marylène Vandevenne
author_facet	Oscar Crasson Gaston Courtade Raphaël R. Léonard Finn Lillelund Aachmann François Legrand Raffaella Parente Denis Baurain Moreno Galleni Morten Sørlie Marylène Vandevenne
author_sort	Oscar Crasson
title	Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function
title_short	Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function
title_full	Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function
title_fullStr	Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function
title_full_unstemmed	Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function
title_sort	human chitotriosidase: catalytic domain or carbohydrate binding module, who’s leading hcht’s biological function
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/0ab5cc52c909439b89b969d8a493a705
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Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function

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