Ontology highlight
ABSTRACT:
PROVIDER: PRJNA937070 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:We implemented transcriptomic analyses of blood and hippocampus of old mice treated with Akkermansia muciniphila Membrane Protein for 8 weeks.
2023-08-25 | GSE162123 | GEO
Project description:Total RNA from ileum of three groups of mice are sequenced. The three groups are 1. wild type mice. 2. mice with IFNg gene knockout. 3. IFNg gene knockout mice after colonization of Akkermansia muciniphila
2015-06-05 | E-MTAB-3633 | biostudies-arrayexpress
Project description:Kees2018 - Genome-scale constraint-based
model of the mucin-degrader Akkermansia
muciniphila
This model is described in the article:
Model-driven design of a
minimal medium for Akkermansia muciniphila confirms mucus
adaptation.
van der Ark KCH, Aalvink S,
Suarez-Diez M, Schaap PJ, de Vos WM, Belzer C.
Microb Biotechnol 2018 Jan; :
Abstract:
The abundance of the human intestinal symbiont Akkermansia
muciniphila has found to be inversely correlated with several
diseases, including metabolic syndrome and obesity.
A. muciniphila is known to use mucin as sole carbon and
nitrogen source. To study the physiology and the potential for
therapeutic applications of this bacterium, we designed a
defined minimal medium. The composition of the medium was based
on the genome-scale metabolic model of A. muciniphila and
the composition of mucin. Our results indicate that
A. muciniphila does not code for GlmS, the enzyme that
mediates the conversion of fructose-6-phosphate (Fru6P) to
glucosamine-6-phosphate (GlcN6P), which is essential in
peptidoglycan formation. The only annotated enzyme that could
mediate this conversion is Amuc-NagB on locus Amuc_1822. We
found that Amuc-NagB was unable to form GlcN6P from Fru6P at
physiological conditions, while it efficiently catalyzed the
reverse reaction. To overcome this inability,
N-acetylglucosamine needs to be present in the medium for
A. muciniphila growth. With these findings, the
genome-scale metabolic model was updated and used to accurately
predict growth of A. muciniphila on synthetic media. The
finding that A. muciniphila has a necessity for GlcNAc,
which is present in mucin further prompts the adaptation to its
mucosal niche.
This model is hosted on
BioModels Database
and identified by:
MODEL1710040000.
To cite BioModels Database, please use:
Chelliah V et al. BioModels: ten-year
anniversary. Nucl. Acids Res. 2015, 43(Database
issue):D542-8.
To the extent possible under law, all copyright and related or
neighbouring rights to this encoded model have been dedicated to
the public domain worldwide. Please refer to
CC0
Public Domain Dedication for more information.
2021-02-15 | MODEL1710040000 | BioModels
Project description:Previous studies have implicated a causal role for the gut bacterium Akkermansia muciniphila in counteracting diet-induced obesity and metabolic dysfunctions. However, a systems level understanding of the molecular mechanisms underlying the anti-obesogenic effect of A. muciniphila is lacking. Using fructose-induced obese mice as a model, we carried out multiomics studies to investigate the molecular cascades mediating the effect of A. muciniphila. We found that A. muciniphila colonization in fructose-induced obese mice triggered significant shifts in gut microbiota composition as well as alterations in numerous gut and plasma metabolites and gene expression in the hypothalamus. Among these, we found that the metabolite oleoyl-ethanolamide in the gut and circulation and hypothalamic oxytocin are the key regulators of gut-brain interactions that underlie the A. muciniphila anti-obesity effect. Our multiomics investigation elucidates the molecular regulators and pathways involved in the communication between A. muciniphila in the gut and hypothalamic neurons that counter fructose-induced obesity .
2022-09-03 | GSE212491 | GEO
Project description:Akkermansia muciniphila, a common member of the human gut microbiota, is considered to be a beneficial resident of the intestinal mucus layer. Surface-exposed molecules produced by this organism likely play important roles in colonization and communication with other microbes and the host, but the protein composition of the outer membrane has not been characterized thus far. Herein we identify A. muciniphila proteins after enrichment and fractionation of the outer membrane proteome of A. muciniphila.
2016-09-27 | PXD004400 | Pride