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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

N-glycan Utilization by Bifidobacterium Gut Symbionts Involves a Specialist beta-Mannosidase

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Author(s):
Cordeiro, Rosa Lorizolla [1, 2] ; Siqueira Pirolla, Renan Augusto [1] ; Persinoti, Gabriela Felix [1] ; Gozzo, Fabio Cesar [3] ; de Giuseppe, Priscila Oliveira [1] ; Murakami, Mario Tyago [1]
Total Authors: 6
Affiliation:
[1] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Bioethanol Sci & Technol Lab CTBE, BR-13083970 Campinas, SP - Brazil
[2] Univ Estadual Campinas, Inst Biol, Grad Program Funct & Mol Biol, Campinas, SP - Brazil
[3] Univ Estadual Campinas, Inst Chem, Dalton Mass Spectrometry Lab, Campinas, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Journal of Molecular Biology; v. 431, n. 4, p. 732-747, FEB 15 2019.
Web of Science Citations: 0
Abstract

Bifidobacteria represent one of the first colonizers of human gut microbiota, providing to this ecosystem better health and nutrition. To maintain a mutualistic relationship, they have enzymes to degrade and use complex carbohydrates non-digestible by their hosts. To succeed in the densely populated gut environment, they evolved molecular strategies that remain poorly understood. Herein, we report a novel mechanism found in probiotic Bifidobacteria for the depolymerization of the ubiquitous 2-acetamido-2-deoxy-4-O-(beta-D-mannopyranosyl)-D-glucopyranose (Man-beta-1,4-GlcNAc), a disaccharide that composes the universal core of eukaryotic N-glycans. In contrast to Bacteroidetes, these Bifidobacteria have a specialist and strain-specific beta-mannosidase that contains three distinctive structural elements conferring high selectivity for Man-beta-1,4-GlcNAc: a lid that undergoes conformational changes upon substrate binding, a tryptophan residue swapped between the two dimeric subunits to accommodate the GlcNAc moiety, and a Rossmann fold subdomain strategically located near to the active site pocket. These key structural elements for Man-beta-1,4-GlcNAc specificity are highly conserved in Bifidobacterium species adapted to the gut of a wide range of social animals, including bee, pig, rabbit, and human. Together, our findings uncover an unprecedented molecular strategy employed by Bifidobacteria to selectively uptake carbohydrates from N-glycans in social hosts. (C) 2019 Elsevier Ltd. All rights reserved. (AU)

FAPESP's process: 16/00740-2 - Mechanistic bases of evolutionary adaptation to temperature and specificity of glycoside hydrolases belonging to novel GH5 subfamilies
Grantee:Rosa Lorizolla Cordeiro
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 15/26982-0 - Exploring novel strategies for depolymerization of plant cell-wall polysaccharides: from structure, function and rational design of glycosyl hydrolases to biological implications and potential biotechnological applications
Grantee:Mário Tyago Murakami
Support Opportunities: Research Projects - Thematic Grants