Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation

The exopolysaccharide galactosaminogalactan (GAG) is an important virulence factor of the fungal pathogen Aspergillus fumigatus. Here, the authors study an A. fumigatus enzyme that deacetylates GAG in a metal-dependent manner and constitutes a founding member of a new carbohydrate esterase family.

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Autores principales:	Natalie C. Bamford, François Le Mauff, Jaime C. Van Loon, Hanna Ostapska, Brendan D. Snarr, Yongzhen Zhang, Elena N. Kitova, John S. Klassen, Jeroen D. C. Codée, Donald C. Sheppard, P. Lynne Howell
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/bc12a17a65694000bd265c5f6442da5e
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spelling	oai:doaj.org-article:bc12a17a65694000bd265c5f6442da5e2021-12-02T15:43:16ZStructural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation10.1038/s41467-020-16144-52041-1723https://doaj.org/article/bc12a17a65694000bd265c5f6442da5e2020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16144-5https://doaj.org/toc/2041-1723The exopolysaccharide galactosaminogalactan (GAG) is an important virulence factor of the fungal pathogen Aspergillus fumigatus. Here, the authors study an A. fumigatus enzyme that deacetylates GAG in a metal-dependent manner and constitutes a founding member of a new carbohydrate esterase family.Natalie C. BamfordFrançois Le MauffJaime C. Van LoonHanna OstapskaBrendan D. SnarrYongzhen ZhangElena N. KitovaJohn S. KlassenJeroen D. C. CodéeDonald C. SheppardP. Lynne HowellNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Natalie C. Bamford François Le Mauff Jaime C. Van Loon Hanna Ostapska Brendan D. Snarr Yongzhen Zhang Elena N. Kitova John S. Klassen Jeroen D. C. Codée Donald C. Sheppard P. Lynne Howell Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation
description	The exopolysaccharide galactosaminogalactan (GAG) is an important virulence factor of the fungal pathogen Aspergillus fumigatus. Here, the authors study an A. fumigatus enzyme that deacetylates GAG in a metal-dependent manner and constitutes a founding member of a new carbohydrate esterase family.
format	article
author	Natalie C. Bamford François Le Mauff Jaime C. Van Loon Hanna Ostapska Brendan D. Snarr Yongzhen Zhang Elena N. Kitova John S. Klassen Jeroen D. C. Codée Donald C. Sheppard P. Lynne Howell
author_facet	Natalie C. Bamford François Le Mauff Jaime C. Van Loon Hanna Ostapska Brendan D. Snarr Yongzhen Zhang Elena N. Kitova John S. Klassen Jeroen D. C. Codée Donald C. Sheppard P. Lynne Howell
author_sort	Natalie C. Bamford
title	Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation
title_short	Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation
title_full	Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation
title_fullStr	Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation
title_full_unstemmed	Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation
title_sort	structural and biochemical characterization of the exopolysaccharide deacetylase agd3 required for aspergillus fumigatus biofilm formation
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/bc12a17a65694000bd265c5f6442da5e
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Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation

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