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PMID: 25388295 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

Molecular details of a starch utilization pathway in the human gut symbiont Eubacterium rectale.

Molecular microbiology ·Vol. 95 ·No. 2 ·2015-01-00 ·Pages 209-30

Cockburn DW, Orlovsky NI, Foley MH, Kwiatkowski KJ, Bahr CM, Maynard M, Demeler B, Koropatkin NM

Abstract

Eubacterium rectale is a prominent human gut symbiont yet little is known about the molecular strategies this bacterium has developed to acquire nutrients within the competitive gut ecosystem. Starch is one of the most abundant glycans in the human diet, and E. rectale increases in vivo when the host consumes a diet rich in resistant starch, although it is not a primary degrader of this glycan. Here we present the results of a quantitative proteomics study in which we identify two glycoside hydrolase 13 family enzymes, and three ABC transporter solute-binding proteins that are abundant during growth on starch and, we hypothesize, work together at the cell surface to degrade starch and capture the released maltooligosaccharides. EUR_21100 is a multidomain cell wall anchored amylase that preferentially targets starch polysaccharides, liberating maltotetraose, whereas the membrane-associated maltogenic amylase EUR_01860 breaks down maltooligosaccharides longer than maltotriose. The three solute-binding proteins display a range of glycan-binding specificities that ensure the capture of glucose through maltoheptaose and some α1,6-branched glycans. Taken together, we describe a pathway for starch utilization by E. rectale DSM 17629 that may be conserved among other starch-degrading Clostridium cluster XIVa organisms in the human gut.

MeSH Terms
ATP-Binding Cassette Transporters/genetics,metabolism Carbohydrate Metabolism Cell Membrane/metabolism Cell Wall/metabolism Chromatography, Thin Layer Eubacterium/genetics,growth & development,metabolism Glycoside Hydrolases/genetics,metabolism Maltose/analogs & derivatives,metabolism Mass Spectrometry Microarray Analysis Oligosaccharides/metabolism Proteomics Starch/metabolism Trisaccharides/metabolism
Chemicals
ATP-Binding Cassette Transporters Oligosaccharides Trisaccharides maltooligosaccharides maltotriose Maltose Starch maltotetraose Glycoside Hydrolases glucan 1,4-alpha-maltohydrolase
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Cockburn Darrell W
Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA.
Orlovsky Nicole I
Foley Matthew H
Kwiatkowski Kurt J
Bahr Constance M
Maynard Mallory
Demeler Borries
Koropatkin Nicole M
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Article Info
Journal
Molecular microbiology
Abbr.
Mol Microbiol
ISSN
1365-2958
Published
2015-01-00
Epub
2014-00-19
Pages
209-30
Language
English
Region
England
NLM ID
8712028
PMCID
PMC4437465
Subset
IM
Grants
NCI NIH HHS · P30 CA054174 · United States
NIDDK NIH HHS · P30 DK034933 · United States
NIGMS NIH HHS · T32 GM008353 · United States
NIDDK NIH HHS · DK 034933 · United States
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