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Infant Gut Microbial Metagenome Mining of α-l-Fucosidases with Activity on Fucosylated Human Milk Oligosaccharides and Glycoconjugates

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Infant Gut Microbial Metagenome Mining of α-l-Fucosidases with Activity on Fucosylated Human Milk Oligosaccharides and Glycoconjugates

dc.contributor.author	Moya-Gonzálvez, Eva M.
dc.contributor.author	Peña-Gil, Nazaret
dc.contributor.author	Rubio-Del-Campo, Antonio
dc.contributor.author	Coll-Marqués, José M.
dc.contributor.author	Gozalbo Rovira, Roberto Vicente
dc.contributor.author	Monedero García, Vicente
dc.contributor.author	Rodríguez Díaz, Jesús
dc.contributor.author	Yebra Yebra, María Jesús
dc.date.accessioned	2022-10-04T16:33:49Z
dc.date.available	2022-10-04T16:33:49Z
dc.date.issued	2022
dc.identifier.citation	Moya-Gonzálvez, Eva M. Peña-Gil, Nazaret Rubio-Del-Campo, Antonio Coll-Marqués, José M. Gozalbo Rovira, Roberto Vicente Monedero García, Vicente Rodríguez Díaz, Jesús Yebra Yebra, María Jesús 2022 Infant Gut Microbial Metagenome Mining of α-l-Fucosidases with Activity on Fucosylated Human Milk Oligosaccharides and Glycoconjugates Microbiology Spectrum 10 4 e01775-22
dc.identifier.uri	https://hdl.handle.net/10550/84113
dc.description.abstract	The gastrointestinal microbiota members produce α-l-fucosidases that play key roles in mucosal, human milk, and dietary oligosaccharide assimilation. Here, 36 open reading frames (ORFs) coding for putative α-l-fucosidases belonging to glycosyl hydrolase family 29 (GH29) were identified through metagenome analysis of breast-fed infant fecal microbiome. Twenty-two of those ORFs showed a complete coding sequence with deduced amino acid sequences displaying the highest degree of identity with α-l-fucosidases from Bacteroides thetaiotaomicron, Bacteroides caccae, Phocaeicola vulgatus, Phocaeicola dorei, Ruminococcus gnavus, and Streptococcus parasanguinis. Based on sequence homology, 10 α-l-fucosidase genes were selected for substrate specificity characterization. The α-l-fucosidases Fuc18, Fuc19A, Fuc35B, Fuc39, and Fuc1584 showed hydrolytic activity on α1,3/4-linked fucose present in Lewis blood antigens and the human milk oligosaccharide (HMO) 3-fucosyllactose. In addition, Fuc1584 also hydrolyzed fucosyl-α-1,6-N-acetylglucosamine (6FN), a component of the core fucosylation of N-glycans. Fuc35A and Fuc193 showed activity on α1,2/3/4/6 linkages from H type-2, Lewis blood antigens, HMOs and 6FN. Fuc30 displayed activity only on α1,6-linked l-fucose, and Fuc5372 showed a preference for α1,2 linkages. Fuc2358 exhibited a broad substrate specificity releasing l-fucose from all the tested free histo-blood group antigens, HMOs, and 6FN. This latest enzyme also displayed activity in glycoconjugates carrying lacto-N-fucopentaose II (Lea) and lacto-N-fucopentaose III (Lex) and in the glycoprotein mucin. Fuc18, Fuc19A, and Fuc39 also removed l-fucose from neoglycoproteins and human α-1 acid glycoprotein. These results give insight into the great diversity of α-l-fucosidases from the infant gut microbiota, thus supporting the hypothesis that fucosylated glycans are crucial for shaping the newborn microbiota composition.
dc.language.iso	eng
dc.relation.ispartof	Microbiology Spectrum, 2022, vol. 10, num. 4, p. e01775-22
dc.subject	Microbiologia
dc.subject	Genòmica
dc.title	Infant Gut Microbial Metagenome Mining of α-l-Fucosidases with Activity on Fucosylated Human Milk Oligosaccharides and Glycoconjugates
dc.type	journal article	es_ES
dc.date.updated	2022-10-04T16:33:50Z
dc.identifier.doi	10.1128/spectrum.01775-22
dc.identifier.idgrec	154821
dc.rights.accessRights	open access	es_ES