| Texto completo | |
| Autor(es): |
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]
Número total de Autores: 6
|
| Afiliação do(s) autor(es): | [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
Número total de Afiliações: 3
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Journal of Molecular Biology; v. 431, n. 4, p. 732-747, FEB 15 2019. |
| Citações Web of Science: | 0 |
| Resumo | |
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) | |
| Processo FAPESP: | 16/00740-2 - Bases mecanísticas da adaptação evolutiva à temperatura e especificidade de hidrolases glicosídicas pertencentes a novas subfamílias GH5 |
| Beneficiário: | Rosa Lorizolla Cordeiro |
| Modalidade de apoio: | Bolsas no Brasil - Doutorado Direto |
| Processo FAPESP: | 15/26982-0 - Explorando novas estratégias para a despolimerização de polissacarídeos da parede celular vegetal: da estrutura, função e desenho racional de hidrolases glicosídicas às implicações biológicas e potenciais aplicações biotecnológicas |
| Beneficiário: | Mário Tyago Murakami |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |