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Nutrient-specific proteomic analysis of the mucin degrading bacterium Akkermansia muciniphila
Authors:Ji-Young Lee  Hyeon-Su Jin  Kyoung Su Kim  Je-Hyun Baek  Bong-Soo Kim  Dong-Woo Lee
Institution:1. Department of Biotechnology, Yonsei University, Seoul, South Korea;2. R&D Center for Clinical Mass Spectrometry, Seegene Medical Foundation, Seoul, South Korea;3. Department of Life Science, Multidisciplinary Genome Institute, Hallym University, Chuncheon, South Korea
Abstract:Akkermansia muciniphila is a prominent mucin-degrading bacterium that acts as a keystone species in regulating the human gut microbiota. Despite recently increasing research into this bacterium and its relevance to human health, a high-resolution database of its functional proteins remains scarce. Here, we provide a proteomic overview of A. muciniphila grown in different nutrient conditions ranging from defined to complex. Of 2318 protein-coding genes in the genome, we identified 841 (40%) that were expressed at the protein level. Overall, proteins involved in energy production and carbohydrate metabolism indicate that A. muciniphila relies mainly on the Embden-Meyerhof-Parnas pathway, and produces short-chain fatty acids through anaerobic fermentation in a nutrient-specific manner. Moreover, this bacterium possesses a broad repertoire of glycosyl hydrolases, together with putative peptidases and sulfatases, to cleave O-glycosylated mucin. Of them, putative mucin-degrading enzymes (Amuc_1220, Amuc_1120, Amuc_0052, Amuc_0480, and Amuc_0060) are highly abundant in the mucin-supplemented media. Furthermore, A. muciniphila uses mucin-derived monosaccharides as sources of energy and cell wall biogenesis. Our dataset provides nutrient-dependent global proteomes of A. muciniphila ATCC BAA-835 to offer insights into its metabolic functions that shape the composition of the human gut microbiota via mucin degradation.
Keywords:Akkermansia muciniphila  glycosyl hydrolase  microbiome  mucin-degrading bacteria  proteome
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