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Volumn 114, Issue 27, 2017, Pages 7037-7042

How members of the human gut microbiota overcome the sulfation problem posed by glycosaminoglycans

Author keywords

Bacteroides thetaiotaomicron; Glycosaminoglycan degradation; Heparan sulfate; Heparin; Human gut microbiota

Indexed keywords

ENZYME; GLUCOSAMINE; GLUCURONIC ACID; GLYCOSAMINOGLYCAN; IDURONIC ACID; LYASE; PROTEINASE K; SULFATASE; CARBOHYDRATE; HEPARAN SULFATE; HEPARIN; OLIGOSACCHARIDE; POLYSACCHARIDE; POLYSACCHARIDE LYASE; SULFUR;

EID: 85021750830     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1704367114     Document Type: Article
Times cited : (103)

References (42)
  • 2
    • 67349250428 scopus 로고    scopus 로고
    • The gut microbiota shapes intestinal immune responses during health and disease
    • Round JL, Mazmanian SK (2009) The gut microbiota shapes intestinal immune responses during health and disease. Nat Rev Immunol 9:313-323.
    • (2009) Nat Rev Immunol , vol.9 , pp. 313-323
    • Round, J.L.1    Mazmanian, S.K.2
  • 5
    • 84933501802 scopus 로고    scopus 로고
    • Glycan complexity dictates microbial resource allocation in the large intestine
    • Rogowski A, et al. (2015) Glycan complexity dictates microbial resource allocation in the large intestine. Nat Commun 6:7481.
    • (2015) Nat Commun , vol.6 , pp. 7481
    • Rogowski, A.1
  • 6
    • 85017104564 scopus 로고    scopus 로고
    • Complex pectin metabolism by gut bacteria reveals novel catalytic functions
    • Ndeh D, et al. (2017) Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature 544:65-70.
    • (2017) Nature , vol.544 , pp. 65-70
    • Ndeh, D.1
  • 7
    • 69949094849 scopus 로고    scopus 로고
    • Complex glycan catabolism by the human gutmicrobiota: The Bacteroidetes Sus-like paradigm
    • Martens EC, Koropatkin NM, Smith TJ, Gordon JI (2009) Complex glycan catabolism by the human gutmicrobiota: The Bacteroidetes Sus-like paradigm. J Biol Chem 284:24673-24677.
    • (2009) J Biol Chem , vol.284 , pp. 24673-24677
    • Martens, E.C.1    Koropatkin, N.M.2    Smith, T.J.3    Gordon, J.I.4
  • 8
    • 84907228243 scopus 로고    scopus 로고
    • Efficient utilization of complex N-linked glycans is a selective advantage for Bacteroides fragilis in extraintestinal infections
    • Cao Y, Rocha ER, Smith CJ (2014) Efficient utilization of complex N-linked glycans is a selective advantage for Bacteroides fragilis in extraintestinal infections. Proc Natl Acad Sci USA 111:12901-12906.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 12901-12906
    • Cao, Y.1    Rocha, E.R.2    Smith, C.J.3
  • 9
    • 84946936348 scopus 로고    scopus 로고
    • Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation
    • Tailford LE, et al. (2015) Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation. Nat Commun 6:7624.
    • (2015) Nat Commun , vol.6 , pp. 7624
    • Tailford, L.E.1
  • 10
    • 56649100319 scopus 로고    scopus 로고
    • The structure of glycosaminoglycans and their interactions with proteins
    • Gandhi NS, Mancera RL (2008) The structure of glycosaminoglycans and their interactions with proteins. Chem Biol Drug Des 72:455-482.
    • (2008) Chem Biol Drug des , vol.72 , pp. 455-482
    • Gandhi, N.S.1    Mancera, R.L.2
  • 11
    • 0035007407 scopus 로고    scopus 로고
    • Immunohistochemical localization of heparan sulfate proteoglycan in human gastrointestinal tract
    • Oshiro M, et al. (2001) Immunohistochemical localization of heparan sulfate proteoglycan in human gastrointestinal tract. Histochem Cell Biol 115:373-380.
    • (2001) Histochem Cell Biol , vol.115 , pp. 373-380
    • Oshiro, M.1
  • 12
    • 78649868163 scopus 로고    scopus 로고
    • A hierarchical classification of polysaccharide lyases for glycogenomics
    • Lombard V, et al. (2010) A hierarchical classification of polysaccharide lyases for glycogenomics. Biochem J 432:437-444.
    • (2010) Biochem J , vol.432 , pp. 437-444
    • Lombard, V.1
  • 13
    • 84896739821 scopus 로고    scopus 로고
    • Crystal structure of a bacterial unsaturated glucuronyl hydrolase with specificity for heparin
    • Nakamichi Y, Mikami B, Murata K, Hashimoto W (2014) Crystal structure of a bacterial unsaturated glucuronyl hydrolase with specificity for heparin. J Biol Chem 289:4787-4797.
    • (2014) J Biol Chem , vol.289 , pp. 4787-4797
    • Nakamichi, Y.1    Mikami, B.2    Murata, K.3    Hashimoto, W.4
  • 14
    • 85014468667 scopus 로고    scopus 로고
    • Conformational flexibility of PL12 family heparinases: Structure and substrate specificity of heparinase III from Bacteroides thetaiotaomicron (BT4657)
    • Ulaganathan T, et al. (2017) Conformational flexibility of PL12 family heparinases: Structure and substrate specificity of heparinase III from Bacteroides thetaiotaomicron (BT4657). Glycobiology 27:176-187.
    • (2017) Glycobiology , vol.27 , pp. 176-187
    • Ulaganathan, T.1
  • 15
    • 84906871300 scopus 로고    scopus 로고
    • Characterization of glycosaminoglycan (GAG) sulfatases from the human gut symbiont Bacteroides thetaiotaomicron reveals the first GAG-specific bacterial endosulfatase
    • Ulmer JE, et al. (2014) Characterization of glycosaminoglycan (GAG) sulfatases from the human gut symbiont Bacteroides thetaiotaomicron reveals the first GAG-specific bacterial endosulfatase. J Biol Chem 289:24289-24303.
    • (2014) J Biol Chem , vol.289 , pp. 24289-24303
    • Ulmer, J.E.1
  • 16
    • 55249108031 scopus 로고    scopus 로고
    • Mucosal glycan foraging enhances fitness and transmission of a saccharolytic human gut bacterial symbiont
    • Martens EC, Chiang HC, Gordon JI (2008) Mucosal glycan foraging enhances fitness and transmission of a saccharolytic human gut bacterial symbiont. Cell Host Microbe 4:447-457.
    • (2008) Cell Host Microbe , vol.4 , pp. 447-457
    • Martens, E.C.1    Chiang, H.C.2    Gordon, J.I.3
  • 17
    • 84860810089 scopus 로고    scopus 로고
    • A scissor blade-like closing mechanism implicated in transmembrane signaling in a Bacteroides hybrid twocomponent system
    • Lowe EC, Baslé A, Czjzek M, Firbank SJ, Bolam DN (2012) A scissor blade-like closing mechanism implicated in transmembrane signaling in a Bacteroides hybrid twocomponent system. Proc Natl Acad Sci USA 109:7298-7303.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 7298-7303
    • Lowe, E.C.1    Baslé, A.2    Czjzek, M.3    Firbank, S.J.4    Bolam, D.N.5
  • 18
    • 0035205390 scopus 로고    scopus 로고
    • Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron
    • Cho KH, Salyers AA (2001) Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron. J Bacteriol 183:7224-7230.
    • (2001) J Bacteriol , vol.183 , pp. 7224-7230
    • Cho, K.H.1    Salyers, A.A.2
  • 19
    • 84965105298 scopus 로고    scopus 로고
    • Molecular dissection of xyloglucan recognition in a prominent human gut symbiont
    • Tauzin AS, et al. (2016) Molecular dissection of xyloglucan recognition in a prominent human gut symbiont. MBio 7:e02134-e15.
    • (2016) MBio , vol.7 , pp. e15-e02134
    • Tauzin, A.S.1
  • 20
    • 84867238386 scopus 로고    scopus 로고
    • Multidomain carbohydrate-binding proteins involved in Bacteroides thetaiotaomicron starch metabolism
    • Cameron EA, et al. (2012) Multidomain carbohydrate-binding proteins involved in Bacteroides thetaiotaomicron starch metabolism. J Biol Chem 287:34614-34625.
    • (2012) J Biol Chem , vol.287 , pp. 34614-34625
    • Cameron, E.A.1
  • 21
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston AB, Bolam DN, Gilbert HJ, Davies GJ (2004) Carbohydrate-binding modules: Fine-tuning polysaccharide recognition. Biochem J 382:769-781.
    • (2004) Biochem J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 22
    • 71749109423 scopus 로고    scopus 로고
    • Structural snapshots of heparin depolymerization by heparin lyase i
    • Han YH, et al. (2009) Structural snapshots of heparin depolymerization by heparin lyase I. J Biol Chem 284:34019-34027.
    • (2009) J Biol Chem , vol.284 , pp. 34019-34027
    • Han, Y.H.1
  • 23
    • 77955302026 scopus 로고    scopus 로고
    • Crystal structure of exotype alginate lyase Atu3025 from Agrobacterium tumefaciens
    • Ochiai A, Yamasaki M, Mikami B, Hashimoto W, Murata K (2010) Crystal structure of exotype alginate lyase Atu3025 from Agrobacterium tumefaciens. J Biol Chem 285: 24519-24528.
    • (2010) J Biol Chem , vol.285 , pp. 24519-24528
    • Ochiai, A.1    Yamasaki, M.2    Mikami, B.3    Hashimoto, W.4    Murata, K.5
  • 24
    • 84906937037 scopus 로고    scopus 로고
    • Tuning transcription of nutrient utilization genes to catabolic rate promotes growth in a gut bacterium
    • Raghavan V, Lowe EC, Townsend GE, 2nd, Bolam DN, Groisman EA (2014) Tuning transcription of nutrient utilization genes to catabolic rate promotes growth in a gut bacterium. Mol Microbiol 93:1010-1025.
    • (2014) Mol Microbiol , vol.93 , pp. 1010-1025
    • Raghavan, V.1    Lowe, E.C.2    Townsend, G.E.3    Bolam, D.N.4    Groisman, E.A.5
  • 25
    • 0032475864 scopus 로고    scopus 로고
    • Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine
    • Dierks T, et al. (1998) Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J Biol Chem 273:25560-25564.
    • (1998) J Biol Chem , vol.273 , pp. 25560-25564
    • Dierks, T.1
  • 26
    • 0028000790 scopus 로고
    • Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria
    • Titgemeyer F, Reizer J, Reizer A, Saier MH, Jr (1994) Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology 140:2349-2354.
    • (1994) Microbiology , vol.140 , pp. 2349-2354
    • Titgemeyer, F.1    Reizer, J.2    Reizer, A.3    Saier, M.H.4
  • 27
    • 84942237687 scopus 로고    scopus 로고
    • The outer mucus layer hosts a distinct intestinal microbial niche
    • Li H, et al. (2015) The outer mucus layer hosts a distinct intestinal microbial niche. Nat Commun 6:8292.
    • (2015) Nat Commun , vol.6 , pp. 8292
    • Li, H.1
  • 28
    • 84892828465 scopus 로고    scopus 로고
    • Diet rapidly and reproducibly alters the human gut microbiome
    • David LA, et al. (2014) Diet rapidly and reproducibly alters the human gut microbiome. Nature 505:559-563.
    • (2014) Nature , vol.505 , pp. 559-563
    • David, L.A.1
  • 29
    • 69949123813 scopus 로고    scopus 로고
    • Identifying genetic determinants needed to establish a human gut symbiont in its habitat
    • Goodman AL, et al. (2009) Identifying genetic determinants needed to establish a human gut symbiont in its habitat. Cell Host Microbe 6:279-289.
    • (2009) Cell Host Microbe , vol.6 , pp. 279-289
    • Goodman, A.L.1
  • 30
    • 84878391810 scopus 로고    scopus 로고
    • Dynamic responses of Bacteroides thetaiotaomicron during growth on glycan mixtures
    • Rogers TE, et al. (2013) Dynamic responses of Bacteroides thetaiotaomicron during growth on glycan mixtures. Mol Microbiol 88:876-890.
    • (2013) Mol Microbiol , vol.88 , pp. 876-890
    • Rogers, T.E.1
  • 31
    • 84929298167 scopus 로고    scopus 로고
    • Colitogenic Bacteroides thetaiotaomicron antigens access host immune cells in a sulfatase-dependent manner via outer membrane vesicles
    • Hickey CA, et al. (2015) Colitogenic Bacteroides thetaiotaomicron antigens access host immune cells in a sulfatase-dependent manner via outer membrane vesicles. Cell Host Microbe 17:672-680.
    • (2015) Cell Host Microbe , vol.17 , pp. 672-680
    • Hickey, C.A.1
  • 32
    • 46049115447 scopus 로고    scopus 로고
    • Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices
    • Koropatkin NM, Martens EC, Gordon JI, Smith TJ (2008) Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices. Structure 16:1105-1115.
    • (2008) Structure , vol.16 , pp. 1105-1115
    • Koropatkin, N.M.1    Martens, E.C.2    Gordon, J.I.3    Smith, T.J.4
  • 33
    • 80053584469 scopus 로고    scopus 로고
    • Characterization of an N-acetylmuramic acid/N-acetylglucosamine kinase of Clostridium acetobutylicum
    • Reith J, Berking A, Mayer C (2011) Characterization of an N-acetylmuramic acid/N-acetylglucosamine kinase of Clostridium acetobutylicum. J Bacteriol 193:5386-5392.
    • (2011) J Bacteriol , vol.193 , pp. 5386-5392
    • Reith, J.1    Berking, A.2    Mayer, C.3
  • 34
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67:235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 35
    • 84928985213 scopus 로고    scopus 로고
    • Automatic prediction of polysaccharide utilization loci in Bacteroidetes species
    • Terrapon N, Lombard V, Gilbert HJ, Henrissat B (2015) Automatic prediction of polysaccharide utilization loci in Bacteroidetes species. Bioinformatics 31:647-655.
    • (2015) Bioinformatics , vol.31 , pp. 647-655
    • Terrapon, N.1    Lombard, V.2    Gilbert, H.J.3    Henrissat, B.4
  • 38
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 25:495-503.
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.1
  • 39
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MH (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys J 80:2946-2953.
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 40
    • 0036930752 scopus 로고    scopus 로고
    • Addition of missing loops and domains to protein models by x-ray solution scattering
    • Petoukhov MV, Eady NA, Brown KA, Svergun DI (2002) Addition of missing loops and domains to protein models by x-ray solution scattering. Biophys J 83:3113-3125.
    • (2002) Biophys J , vol.83 , pp. 3113-3125
    • Petoukhov, M.V.1    Eady, N.A.2    Brown, K.A.3    Svergun, D.I.4
  • 41
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in smallangle scattering
    • Volkov VV, Svergun DI (2003) Uniqueness of ab initio shape determination in smallangle scattering. J Appl Crystallogr 36:860-864.
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 42
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies GJ, Wilson KS, Henrissat B (1997) Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J 321:557-559.
    • (1997) Biochem J , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.