메뉴 건너뛰기




Volumn 20, Issue 1, 2012, Pages 30-39

Microbial adhesins to gastrointestinal mucus

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; BINDING PROTEIN; BLOOD GROUP ANTIGEN; CELL SURFACE MUCIN; FIMH FIMBRIAL ADHESIN; FLAGELLIN; LECTIN; MUCIN; MUCIN 1; MUCIN 2; MUCUS BINDING PROTEIN; PILIN; UNCLASSIFIED DRUG;

EID: 84855500089     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2011.10.001     Document Type: Review
Times cited : (208)

References (82)
  • 1
    • 54449083567 scopus 로고    scopus 로고
    • The inner of the two Muc2 mucin-dependent mucus layers in colon is devoid of bacteria
    • Johansson M.E., et al. The inner of the two Muc2 mucin-dependent mucus layers in colon is devoid of bacteria. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:15064-15069.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 15064-15069
    • Johansson, M.E.1
  • 2
    • 80052587040 scopus 로고    scopus 로고
    • Sweet-talk: role of host glycosylation in bacterial pathogenesis of the gastrointestinal tract
    • Moran A.P., et al. Sweet-talk: role of host glycosylation in bacterial pathogenesis of the gastrointestinal tract. Gut 2011, 60:1412-1425.
    • (2011) Gut , vol.60 , pp. 1412-1425
    • Moran, A.P.1
  • 3
    • 67650394385 scopus 로고    scopus 로고
    • Proteomic analyses of the two mucus layers of the colon barrier reveal that their main component, the Muc2 mucin, is strongly bound to the Fcgbp protein
    • Johansson M.E., et al. Proteomic analyses of the two mucus layers of the colon barrier reveal that their main component, the Muc2 mucin, is strongly bound to the Fcgbp protein. J. Proteome Res. 2009, 8:3549-3557.
    • (2009) J. Proteome Res. , vol.8 , pp. 3549-3557
    • Johansson, M.E.1
  • 4
    • 80052748811 scopus 로고    scopus 로고
    • Colonic gene expression patterns of mucin muc2 knockout mice reveal various phases in colitis development
    • Lu P., et al. Colonic gene expression patterns of mucin muc2 knockout mice reveal various phases in colitis development. Inflamm. Bowel Dis. 2011, 17:2047-2057.
    • (2011) Inflamm. Bowel Dis. , vol.17 , pp. 2047-2057
    • Lu, P.1
  • 5
    • 79952748335 scopus 로고    scopus 로고
    • The two mucus layers of colon are organized by the MUC2 mucin, whereas the outer layer is a legislator of host-microbial interactions
    • Johansson M.E., et al. The two mucus layers of colon are organized by the MUC2 mucin, whereas the outer layer is a legislator of host-microbial interactions. Proc. Natl. Acad. Sci. U.S.A. 2011, 108(Suppl. 1):4659-4665.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , Issue.SUPPL. 1 , pp. 4659-4665
    • Johansson, M.E.1
  • 6
    • 72149108714 scopus 로고    scopus 로고
    • The membrane-bound mucins: from cell signalling to transcriptional regulation and expression in epithelial cancers
    • Jonckheere N., Van Seuningen I. The membrane-bound mucins: from cell signalling to transcriptional regulation and expression in epithelial cancers. Biochimie 2010, 92:1-11.
    • (2010) Biochimie , vol.92 , pp. 1-11
    • Jonckheere, N.1    Van Seuningen, I.2
  • 7
    • 73949140777 scopus 로고    scopus 로고
    • MUC1 limits Helicobacter pylori infection both by steric hindrance and by acting as a releasable decoy
    • Lindén S.K., et al. MUC1 limits Helicobacter pylori infection both by steric hindrance and by acting as a releasable decoy. PLoS Pathog. 2009, 5:e1000617.
    • (2009) PLoS Pathog. , vol.5
    • Lindén, S.K.1
  • 8
    • 0344875610 scopus 로고    scopus 로고
    • Evidence of regio-specific glycosylation in human intestinal mucins: presence of an acidic gradient along the intestinal tract
    • Robbe C., et al. Evidence of regio-specific glycosylation in human intestinal mucins: presence of an acidic gradient along the intestinal tract. J. Biol. Chem. 2003, 278:46337-46348.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46337-46348
    • Robbe, C.1
  • 9
    • 79951999564 scopus 로고    scopus 로고
    • High-sensitivity O-glycomic analysis of mice deficient in core 2 β1,6-N-acetylglucosaminyltransferases
    • Ismail M.N., et al. High-sensitivity O-glycomic analysis of mice deficient in core 2 β1,6-N-acetylglucosaminyltransferases. Glycobiology 2011, 21:82-98.
    • (2011) Glycobiology , vol.21 , pp. 82-98
    • Ismail, M.N.1
  • 10
    • 66249136714 scopus 로고    scopus 로고
    • A complex, but uniform O-glycosylation of the human MUC2 mucin from colonic biopsies analyzed by nanoLC/MSn
    • Larsson J.M., et al. A complex, but uniform O-glycosylation of the human MUC2 mucin from colonic biopsies analyzed by nanoLC/MSn. Glycobiology 2009, 19:756-766.
    • (2009) Glycobiology , vol.19 , pp. 756-766
    • Larsson, J.M.1
  • 11
    • 79952756170 scopus 로고    scopus 로고
    • Mucin dynamics and enteric pathogens
    • McGuckin M.A., et al. Mucin dynamics and enteric pathogens. Nat. Rev. Microbiol. 2011, 9:265-278.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 265-278
    • McGuckin, M.A.1
  • 12
    • 79251581856 scopus 로고    scopus 로고
    • Importance and regulation of the colonic mucus barrier in a mouse model of colitis
    • Petersson J., et al. Importance and regulation of the colonic mucus barrier in a mouse model of colitis. Am. J. Physiol. Gastrointest. Liver Physiol. 2011, 300:G327-G333.
    • (2011) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.300
    • Petersson, J.1
  • 13
    • 77953610970 scopus 로고    scopus 로고
    • Muc2 protects against lethal infectious colitis by disassociating pathogenic and commensal bacteria from the colonic mucosa
    • Bergstrom K.S., et al. Muc2 protects against lethal infectious colitis by disassociating pathogenic and commensal bacteria from the colonic mucosa. PLoS Pathog. 2010, 6:e1000902.
    • (2010) PLoS Pathog. , vol.6
    • Bergstrom, K.S.1
  • 14
    • 77951672971 scopus 로고    scopus 로고
    • Mucin gene deficiency in mice impairs host resistance to an enteric parasitic infection
    • Hasnain S.Z., et al. Mucin gene deficiency in mice impairs host resistance to an enteric parasitic infection. Gastroenterology 2010, 138:1763-1771.
    • (2010) Gastroenterology , vol.138 , pp. 1763-1771
    • Hasnain, S.Z.1
  • 15
    • 30744450499 scopus 로고    scopus 로고
    • Comparative analysis of proteins with a mucus-binding domain found exclusively in lactic acid bacteria
    • Boekhorst J., et al. Comparative analysis of proteins with a mucus-binding domain found exclusively in lactic acid bacteria. Microbiology 2006, 152:273-280.
    • (2006) Microbiology , vol.152 , pp. 273-280
    • Boekhorst, J.1
  • 16
    • 0036181685 scopus 로고    scopus 로고
    • A high-molecular-mass cell-surface protein from Lactobacillus reuteri 1063 adheres to mucus components
    • Roos S., Jonsson H. A high-molecular-mass cell-surface protein from Lactobacillus reuteri 1063 adheres to mucus components. Microbiology 2002, 148:433-442.
    • (2002) Microbiology , vol.148 , pp. 433-442
    • Roos, S.1    Jonsson, H.2
  • 17
    • 70450230470 scopus 로고    scopus 로고
    • Crystal structure of a mucus-binding protein repeat reveals an unexpected functional immunoglobulin binding activity
    • MacKenzie D.A., et al. Crystal structure of a mucus-binding protein repeat reveals an unexpected functional immunoglobulin binding activity. J. Biol. Chem. 2009, 284:32444-32453.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32444-32453
    • MacKenzie, D.A.1
  • 18
    • 79952266302 scopus 로고    scopus 로고
    • The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri
    • Frese S.A., et al. The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri. PLoS Genet. 2011, 7:e1001314.
    • (2011) PLoS Genet. , vol.7
    • Frese, S.A.1
  • 19
    • 78049489313 scopus 로고    scopus 로고
    • Strain-specific diversity of mucus-binding proteins in the adhesion and aggregation properties of Lactobacillus reuteri
    • Mackenzie D.A., et al. Strain-specific diversity of mucus-binding proteins in the adhesion and aggregation properties of Lactobacillus reuteri. Microbiology 2010, 156:3368-3378.
    • (2010) Microbiology , vol.156 , pp. 3368-3378
    • Mackenzie, D.A.1
  • 20
    • 75749140534 scopus 로고    scopus 로고
    • The extracellular biology of the lactobacilli
    • Kleerebezem M., et al. The extracellular biology of the lactobacilli. FEMS Microbiol. Rev. 2010, 34:199-230.
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 199-230
    • Kleerebezem, M.1
  • 21
    • 34548491198 scopus 로고    scopus 로고
    • Internalins: a complex family of leucine-rich repeat-containing proteins in Listeria monocytogenes
    • Bierne H., et al. Internalins: a complex family of leucine-rich repeat-containing proteins in Listeria monocytogenes. Microbes Infect. 2007, 9:1156-1166.
    • (2007) Microbes Infect. , vol.9 , pp. 1156-1166
    • Bierne, H.1
  • 22
    • 77953990216 scopus 로고    scopus 로고
    • Functional and probiotic attributes of an indigenous isolate of Lactobacillus plantarum
    • Kaushik J.K., et al. Functional and probiotic attributes of an indigenous isolate of Lactobacillus plantarum. PLoS ONE 2009, 4:e8099.
    • (2009) PLoS ONE , vol.4
    • Kaushik, J.K.1
  • 23
    • 77956621135 scopus 로고    scopus 로고
    • Adhesion capability of first two domains at N terminus of NP_785232 protein and their interaction with a UV-absorbing component from human mucus
    • Du L., et al. Adhesion capability of first two domains at N terminus of NP_785232 protein and their interaction with a UV-absorbing component from human mucus. Lett. Appl. Microbiol. 2010, 51:400-405.
    • (2010) Lett. Appl. Microbiol. , vol.51 , pp. 400-405
    • Du, L.1
  • 24
    • 33845754821 scopus 로고    scopus 로고
    • Factors involved in binding of Lactobacillus plantarum Lp6 to rat small intestinal mucus
    • Sun J., et al. Factors involved in binding of Lactobacillus plantarum Lp6 to rat small intestinal mucus. Lett. Appl. Microbiol. 2007, 44:79-85.
    • (2007) Lett. Appl. Microbiol. , vol.44 , pp. 79-85
    • Sun, J.1
  • 25
    • 23944432874 scopus 로고    scopus 로고
    • Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum
    • Pretzer G., et al. Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum. J. Bacteriol. 2005, 187:6128-6136.
    • (2005) J. Bacteriol. , vol.187 , pp. 6128-6136
    • Pretzer, G.1
  • 26
    • 53549117107 scopus 로고    scopus 로고
    • Mannose-specific interaction of Lactobacillus plantarum with porcine jejunal epithelium
    • Gross G., et al. Mannose-specific interaction of Lactobacillus plantarum with porcine jejunal epithelium. FEMS Immunol. Med. Microbiol. 2008, 54:215-223.
    • (2008) FEMS Immunol. Med. Microbiol. , vol.54 , pp. 215-223
    • Gross, G.1
  • 27
    • 79960079000 scopus 로고    scopus 로고
    • Functional characterization of a mucus-specific LPXTG surface adhesin from probiotic Lactobacillus rhamnosus GG
    • von Ossowski I., et al. Functional characterization of a mucus-specific LPXTG surface adhesin from probiotic Lactobacillus rhamnosus GG. Appl. Environ. Microbiol. 2011, 77:4465-4472.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 4465-4472
    • von Ossowski, I.1
  • 28
    • 79958042948 scopus 로고    scopus 로고
    • Lactobacillus adhesion to mucus
    • Maxwell L., et al. Lactobacillus adhesion to mucus. Nutrients 2011, 3:613-636.
    • (2011) Nutrients , vol.3 , pp. 613-636
    • Maxwell, L.1
  • 29
    • 0030588148 scopus 로고    scopus 로고
    • A collagen binding protein from Lactobacillus reuteri is part of an ABC transporter system?
    • Roos S., et al. A collagen binding protein from Lactobacillus reuteri is part of an ABC transporter system?. FEMS Microbiol. Lett. 1996, 144:33-38.
    • (1996) FEMS Microbiol. Lett. , vol.144 , pp. 33-38
    • Roos, S.1
  • 30
    • 0036253495 scopus 로고    scopus 로고
    • Purification and characterization of a surface protein from Lactobacillus fermentum 104R that binds to porcine small intestinal mucus and gastric mucin
    • Rojas M., et al. Purification and characterization of a surface protein from Lactobacillus fermentum 104R that binds to porcine small intestinal mucus and gastric mucin. Appl. Environ. Microbiol. 2002, 68:2330-2336.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2330-2336
    • Rojas, M.1
  • 31
    • 72849142871 scopus 로고    scopus 로고
    • Lactobacillus fermentum BCS87 expresses mucus- and mucin-binding proteins on the cell surface
    • Macías-Rodríguez M.E., et al. Lactobacillus fermentum BCS87 expresses mucus- and mucin-binding proteins on the cell surface. J. Appl. Microbiol. 2009, 107:1866-1874.
    • (2009) J. Appl. Microbiol. , vol.107 , pp. 1866-1874
    • Macías-Rodríguez, M.E.1
  • 32
    • 77955831992 scopus 로고    scopus 로고
    • Identification of a new adhesin-like protein from Lactobacillus mucosae ME-340 with specific affinity to the human blood group A and B antigens
    • Watanabe M., et al. Identification of a new adhesin-like protein from Lactobacillus mucosae ME-340 with specific affinity to the human blood group A and B antigens. J. Appl. Microbiol. 2010, 109:927-935.
    • (2010) J. Appl. Microbiol. , vol.109 , pp. 927-935
    • Watanabe, M.1
  • 33
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    • Granato D., et al. Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins. Infect. Immun. 2004, 72:2160-2169.
    • (2004) Infect. Immun. , vol.72 , pp. 2160-2169
    • Granato, D.1
  • 34
    • 29644437923 scopus 로고    scopus 로고
    • GroEL of Lactobacillus johnsonii La1 (NCC 533) is cell surface associated: potential role in interactions with the host and the gastric pathogen Helicobacter pylori
    • Bergonzelli G.E., et al. GroEL of Lactobacillus johnsonii La1 (NCC 533) is cell surface associated: potential role in interactions with the host and the gastric pathogen Helicobacter pylori. Infect. Immun. 2006, 74:425-434.
    • (2006) Infect. Immun. , vol.74 , pp. 425-434
    • Bergonzelli, G.E.1
  • 35
    • 44249099682 scopus 로고    scopus 로고
    • Cell surface Lactobacillus plantarum LA 318 glyceraldehyde-3-phosphate dehydrogenase (GAPDH) adheres to human colonic mucin
    • Kinoshita H., et al. Cell surface Lactobacillus plantarum LA 318 glyceraldehyde-3-phosphate dehydrogenase (GAPDH) adheres to human colonic mucin. J. Appl. Microbiol. 2008, 104:1667-1674.
    • (2008) J. Appl. Microbiol. , vol.104 , pp. 1667-1674
    • Kinoshita, H.1
  • 36
    • 35048815089 scopus 로고    scopus 로고
    • Host protein binding and adhesive properties of H6 and H7 flagella of attaching and effacing Escherichia coli
    • Erdem A.L., et al. Host protein binding and adhesive properties of H6 and H7 flagella of attaching and effacing Escherichia coli. J. Bacteriol. 2007, 189:7426-7435.
    • (2007) J. Bacteriol. , vol.189 , pp. 7426-7435
    • Erdem, A.L.1
  • 37
    • 0035189181 scopus 로고    scopus 로고
    • Role of FliC and FliD flagellar proteins of Clostridium difficile in adherence and gut colonization
    • Tasteyre A., et al. Role of FliC and FliD flagellar proteins of Clostridium difficile in adherence and gut colonization. Infect. Immun. 2001, 69:7937-7940.
    • (2001) Infect. Immun. , vol.69 , pp. 7937-7940
    • Tasteyre, A.1
  • 38
    • 66849103966 scopus 로고    scopus 로고
    • Identification of surface proteins involved in the adhesion of a probiotic Bacillus cereus strain to mucin and fibronectin
    • Sánchez B., et al. Identification of surface proteins involved in the adhesion of a probiotic Bacillus cereus strain to mucin and fibronectin. Microbiology 2009, 155:1708-1716.
    • (2009) Microbiology , vol.155 , pp. 1708-1716
    • Sánchez, B.1
  • 39
    • 79953758208 scopus 로고    scopus 로고
    • A flagellin-producing Lactococcus strain: interactions with mucin and enteropathogens
    • Sánchez B., et al. A flagellin-producing Lactococcus strain: interactions with mucin and enteropathogens. FEMS Microbiol. Lett. 2011, 318:101-107.
    • (2011) FEMS Microbiol. Lett. , vol.318 , pp. 101-107
    • Sánchez, B.1
  • 40
    • 41749110006 scopus 로고    scopus 로고
    • RosE represses Std fimbrial expression in Salmonella enterica serotype Typhimurium
    • Chessa D., et al. RosE represses Std fimbrial expression in Salmonella enterica serotype Typhimurium. Mol. Microbiol. 2008, 68:573-587.
    • (2008) Mol. Microbiol. , vol.68 , pp. 573-587
    • Chessa, D.1
  • 41
    • 60349107594 scopus 로고    scopus 로고
    • Salmonella enterica serotype Typhimurium Std fimbriae bind terminal α(1,2)fucose residues in the cecal mucosa
    • Chessa D., et al. Salmonella enterica serotype Typhimurium Std fimbriae bind terminal α(1,2)fucose residues in the cecal mucosa. Mol. Microbiol. 2009, 71:864-875.
    • (2009) Mol. Microbiol. , vol.71 , pp. 864-875
    • Chessa, D.1
  • 42
    • 0033989804 scopus 로고    scopus 로고
    • Characterization and purification of porcine small intestinal mucus receptor for Escherichia coli K88ac fimbrial adhesin
    • Jin L.Z., et al. Characterization and purification of porcine small intestinal mucus receptor for Escherichia coli K88ac fimbrial adhesin. FEMS Immunol. Med. Microbiol. 2000, 27:17-22.
    • (2000) FEMS Immunol. Med. Microbiol. , vol.27 , pp. 17-22
    • Jin, L.Z.1
  • 43
    • 17544403800 scopus 로고    scopus 로고
    • Fimbriae extracts from enterotoxigenic Escherichia coli strains of bovine and porcine origin with K99 and/or F41 antigens
    • Vázquez F., et al. Fimbriae extracts from enterotoxigenic Escherichia coli strains of bovine and porcine origin with K99 and/or F41 antigens. Vet. Microbiol. 1996, 48:231-241.
    • (1996) Vet. Microbiol. , vol.48 , pp. 231-241
    • Vázquez, F.1
  • 44
    • 0029152850 scopus 로고
    • Characterization of glycoprotein glycan receptors for Escherichia coli F17 fimbrial lectin
    • Mouricout M., et al. Characterization of glycoprotein glycan receptors for Escherichia coli F17 fimbrial lectin. Microb. Pathog. 1995, 18:297-306.
    • (1995) Microb. Pathog. , vol.18 , pp. 297-306
    • Mouricout, M.1
  • 45
    • 0041664004 scopus 로고    scopus 로고
    • The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine
    • Buts L., et al. The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine. Mol. Microbiol. 2003, 49:705-715.
    • (2003) Mol. Microbiol. , vol.49 , pp. 705-715
    • Buts, L.1
  • 46
    • 0036094156 scopus 로고    scopus 로고
    • Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection
    • Hung C.S., et al. Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection. Mol. Microbiol. 2002, 44:903-915.
    • (2002) Mol. Microbiol. , vol.44 , pp. 903-915
    • Hung, C.S.1
  • 47
    • 77952513211 scopus 로고    scopus 로고
    • Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting
    • Le Trong I., et al. Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting. Cell 2010, 141:645-655.
    • (2010) Cell , vol.141 , pp. 645-655
    • Le Trong, I.1
  • 48
    • 70350134948 scopus 로고    scopus 로고
    • Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human-mucus binding protein
    • Kankainen M., et al. Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human-mucus binding protein. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:17193-17198.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 17193-17198
    • Kankainen, M.1
  • 49
    • 77950289123 scopus 로고    scopus 로고
    • Mucosal adhesion properties of the probiotic Lactobacillus rhamnosus GG SpaCBA and SpaFED pilin subunits
    • von Ossowski I., et al. Mucosal adhesion properties of the probiotic Lactobacillus rhamnosus GG SpaCBA and SpaFED pilin subunits. Appl. Environ. Microbiol. 2010, 76:2049-2057.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 2049-2057
    • von Ossowski, I.1
  • 50
    • 77954695213 scopus 로고    scopus 로고
    • Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors
    • Magalhães A., Reis C.A. Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors. Braz. J. Med. Biol. Res. 2010, 43:611-618.
    • (2010) Braz. J. Med. Biol. Res. , vol.43 , pp. 611-618
    • Magalhães, A.1    Reis, C.A.2
  • 51
    • 40449090246 scopus 로고    scopus 로고
    • Four modes of adhesion are used during Helicobacter pylori binding to human mucins in the oral and gastric niches
    • Lindén S.K., et al. Four modes of adhesion are used during Helicobacter pylori binding to human mucins in the oral and gastric niches. Helicobacter 2008, 13:81-93.
    • (2008) Helicobacter , vol.13 , pp. 81-93
    • Lindén, S.K.1
  • 52
    • 35648945254 scopus 로고    scopus 로고
    • Campylobacter flagella: not just for motility
    • Guerry P. Campylobacter flagella: not just for motility. Trends Microbiol. 2007, 15:456-461.
    • (2007) Trends Microbiol. , vol.15 , pp. 456-461
    • Guerry, P.1
  • 53
    • 0013238319 scopus 로고    scopus 로고
    • Campylobacter jejuni binds intestinal H(O) antigen (Fucα1, 2Galβ1, 4GlcNAc), and fucosyloligosaccharides of human milk inhibit its binding and infection
    • Ruiz-Palacios G.M., et al. Campylobacter jejuni binds intestinal H(O) antigen (Fucα1, 2Galβ1, 4GlcNAc), and fucosyloligosaccharides of human milk inhibit its binding and infection. J. Biol. Chem. 2003, 278:14112-14120.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14112-14120
    • Ruiz-Palacios, G.M.1
  • 54
    • 18344392519 scopus 로고    scopus 로고
    • Human-milk glycans that inhibit pathogen binding protect breast-feeding infants against infectious diarrhea
    • Morrow A.L., et al. Human-milk glycans that inhibit pathogen binding protect breast-feeding infants against infectious diarrhea. J. Nutr. 2005, 135:1304-1307.
    • (2005) J. Nutr. , vol.135 , pp. 1304-1307
    • Morrow, A.L.1
  • 55
    • 34547678389 scopus 로고    scopus 로고
    • MUC1 cell surface mucin is a critical element of the mucosal barrier to infection
    • McAuley J.L., et al. MUC1 cell surface mucin is a critical element of the mucosal barrier to infection. J. Clin. Invest. 2007, 117:2313-2324.
    • (2007) J. Clin. Invest. , vol.117 , pp. 2313-2324
    • McAuley, J.L.1
  • 56
    • 62849083844 scopus 로고    scopus 로고
    • Differential carbohydrate recognition by Campylobacter jejuni strain 11168: influences of temperature and growth conditions
    • Day C.J., et al. Differential carbohydrate recognition by Campylobacter jejuni strain 11168: influences of temperature and growth conditions. PLoS ONE 2009, 4:e4927.
    • (2009) PLoS ONE , vol.4
    • Day, C.J.1
  • 57
    • 48949101533 scopus 로고    scopus 로고
    • Campylobacter jejuni response to human mucin MUC2: modulation of colonization and pathogenicity determinants
    • Tu Q.V., et al. Campylobacter jejuni response to human mucin MUC2: modulation of colonization and pathogenicity determinants. J. Med. Microbiol. 2008, 57:795-802.
    • (2008) J. Med. Microbiol. , vol.57 , pp. 795-802
    • Tu, Q.V.1
  • 58
    • 25844435822 scopus 로고    scopus 로고
    • Porcine gastric mucin binds to recombinant norovirus particles and competitively inhibits their binding to histo-blood group antigens and Caco-2 cells
    • Tian P., et al. Porcine gastric mucin binds to recombinant norovirus particles and competitively inhibits their binding to histo-blood group antigens and Caco-2 cells. Lett. Appl. Microbiol. 2005, 41:315-320.
    • (2005) Lett. Appl. Microbiol. , vol.41 , pp. 315-320
    • Tian, P.1
  • 59
    • 78650425742 scopus 로고    scopus 로고
    • Specificity and kinetics of norovirus binding to magnetic bead-conjugated histo-blood group antigens
    • Tian P., et al. Specificity and kinetics of norovirus binding to magnetic bead-conjugated histo-blood group antigens. J. Appl. Microbiol. 2010, 109:1753-1762.
    • (2010) J. Appl. Microbiol. , vol.109 , pp. 1753-1762
    • Tian, P.1
  • 60
    • 34249822248 scopus 로고    scopus 로고
    • Structural basis for the recognition of blood group trisaccharides by norovirus
    • Cao S., et al. Structural basis for the recognition of blood group trisaccharides by norovirus. J. Virol. 2007, 81:5949-5957.
    • (2007) J. Virol. , vol.81 , pp. 5949-5957
    • Cao, S.1
  • 61
    • 52049112292 scopus 로고    scopus 로고
    • Norovirus pathogenesis: mechanisms of persistence and immune evasion in human populations
    • Donaldson E.F., et al. Norovirus pathogenesis: mechanisms of persistence and immune evasion in human populations. Immunol. Rev. 2008, 225:190-211.
    • (2008) Immunol. Rev. , vol.225 , pp. 190-211
    • Donaldson, E.F.1
  • 62
    • 33845889108 scopus 로고    scopus 로고
    • Lactic acid bacteria (LAB) bind to human B- or H-antigens expressed on intestinal mucosa
    • Uchida H., et al. Lactic acid bacteria (LAB) bind to human B- or H-antigens expressed on intestinal mucosa. Biosci. Biotechnol. Biochem. 2006, 70:3073-3076.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 3073-3076
    • Uchida, H.1
  • 63
    • 33747312017 scopus 로고    scopus 로고
    • Lactobacilli binding human A-antigen expressed in intestinal mucosa
    • Uchida H., et al. Lactobacilli binding human A-antigen expressed in intestinal mucosa. Res. Microbiol. 2006, 157:659-665.
    • (2006) Res. Microbiol. , vol.157 , pp. 659-665
    • Uchida, H.1
  • 64
    • 56949100404 scopus 로고    scopus 로고
    • Cell surface glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Lactobacillus plantarum LA 318 recognizes human A and B blood group antigens
    • Kinoshita H., et al. Cell surface glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Lactobacillus plantarum LA 318 recognizes human A and B blood group antigens. Res. Microbiol. 2008, 159:685-691.
    • (2008) Res. Microbiol. , vol.159 , pp. 685-691
    • Kinoshita, H.1
  • 65
    • 0023608699 scopus 로고
    • Rat and human colonic mucins bind to and inhibit adherence lectin of Entamoeba histolytica
    • Chadee K., et al. Rat and human colonic mucins bind to and inhibit adherence lectin of Entamoeba histolytica. J. Clin. Invest. 1987, 80:1245-1254.
    • (1987) J. Clin. Invest. , vol.80 , pp. 1245-1254
    • Chadee, K.1
  • 66
    • 0036000594 scopus 로고    scopus 로고
    • Structure and function of the Entamoeba histolytica Gal/GalNAc lectin
    • Mann B.J. Structure and function of the Entamoeba histolytica Gal/GalNAc lectin. Int. Rev. Cytol. 2002, 216:59-80.
    • (2002) Int. Rev. Cytol. , vol.216 , pp. 59-80
    • Mann, B.J.1
  • 67
    • 0036405392 scopus 로고    scopus 로고
    • The bittersweet interface of parasite and host: lectin-carbohydrate interactions during human invasion by the parasite Entamoeba histolytica
    • Petri W.A., et al. The bittersweet interface of parasite and host: lectin-carbohydrate interactions during human invasion by the parasite Entamoeba histolytica. Annu. Rev. Microbiol. 2002, 56:39-64.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 39-64
    • Petri, W.A.1
  • 68
    • 28444453298 scopus 로고    scopus 로고
    • Roles for the galactose-/N-acetylgalactosamine-binding lectin of Entamoeba in parasite virulence and differentiation
    • Frederick J.R., et al. Roles for the galactose-/N-acetylgalactosamine-binding lectin of Entamoeba in parasite virulence and differentiation. Glycobiology 2005, 15:53R-59R.
    • (2005) Glycobiology , vol.15
    • Frederick, J.R.1
  • 69
    • 53249151506 scopus 로고    scopus 로고
    • Microbial recognition of human cell surface glycoconjugates
    • Imberty A., Varrot A. Microbial recognition of human cell surface glycoconjugates. Curr. Opin. Struct. Biol. 2008, 18:567-576.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 567-576
    • Imberty, A.1    Varrot, A.2
  • 70
    • 55849092826 scopus 로고    scopus 로고
    • Intestinal adherence of Vibrio cholerae involves a coordinated interaction between colonization factor GbpA and mucin
    • Bhowmick R., et al. Intestinal adherence of Vibrio cholerae involves a coordinated interaction between colonization factor GbpA and mucin. Infect. Immun. 2008, 76:4968-4977.
    • (2008) Infect. Immun. , vol.76 , pp. 4968-4977
    • Bhowmick, R.1
  • 71
    • 33745590851 scopus 로고    scopus 로고
    • N-Glycosylation of the MUC1 mucin in epithelial cells and secretions
    • Parry S., et al. N-Glycosylation of the MUC1 mucin in epithelial cells and secretions. Glycobiology 2006, 16:623-634.
    • (2006) Glycobiology , vol.16 , pp. 623-634
    • Parry, S.1
  • 72
    • 0035884645 scopus 로고    scopus 로고
    • Sd(a)-antigen-like structures carried on core 3 are prominent features of glycans from the mucin of normal human descending colon
    • Capon C., et al. Sd(a)-antigen-like structures carried on core 3 are prominent features of glycans from the mucin of normal human descending colon. Biochem. J. 2001, 358:657-664.
    • (2001) Biochem. J. , vol.358 , pp. 657-664
    • Capon, C.1
  • 73
    • 10644254423 scopus 로고    scopus 로고
    • Structural diversity and specific distribution of O-glycans in normal human mucins along the intestinal tract
    • Robbe C., et al. Structural diversity and specific distribution of O-glycans in normal human mucins along the intestinal tract. Biochem. J. 2004, 384:307-316.
    • (2004) Biochem. J. , vol.384 , pp. 307-316
    • Robbe, C.1
  • 74
    • 34250378697 scopus 로고    scopus 로고
    • Increased susceptibility to colitis and colorectal tumors in mice lacking core 3-derived O-glycans
    • An G., et al. Increased susceptibility to colitis and colorectal tumors in mice lacking core 3-derived O-glycans. J. Exp. Med. 2007, 204:1417-1429.
    • (2007) J. Exp. Med. , vol.204 , pp. 1417-1429
    • An, G.1
  • 75
    • 67650069705 scopus 로고    scopus 로고
    • Glycosyltransferase function in core 2-type protein O glycosylation
    • Stone E.L., et al. Glycosyltransferase function in core 2-type protein O glycosylation. Mol. Cell. Biol. 2009, 29:3770-3782.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3770-3782
    • Stone, E.L.1
  • 76
    • 79953307656 scopus 로고    scopus 로고
    • Loss of intestinal core 1-derived O-glycans causes spontaneous colitis in mice
    • Fu J., et al. Loss of intestinal core 1-derived O-glycans causes spontaneous colitis in mice. J. Clin. Invest. 2011, 121:1657-1666.
    • (2011) J. Clin. Invest. , vol.121 , pp. 1657-1666
    • Fu, J.1
  • 77
    • 80054767981 scopus 로고    scopus 로고
    • Altered O-glycosylation profile of MUC2 mucin occurs in active ulcerative colitis and is associated with increased inflammation
    • Larsson J.M., et al. Altered O-glycosylation profile of MUC2 mucin occurs in active ulcerative colitis and is associated with increased inflammation. Inflamm. Bowel Dis. 2011, 17:2299-2307.
    • (2011) Inflamm. Bowel Dis. , vol.17 , pp. 2299-2307
    • Larsson, J.M.1
  • 78
    • 79952445770 scopus 로고    scopus 로고
    • Crystal structure of the mucin-binding domain of Spr1345 from Streptococcus pneumoniae
    • Du Y., et al. Crystal structure of the mucin-binding domain of Spr1345 from Streptococcus pneumoniae. J. Struct. Biol. 2011, 174:252-257.
    • (2011) J. Struct. Biol. , vol.174 , pp. 252-257
    • Du, Y.1
  • 79
    • 33846237748 scopus 로고    scopus 로고
    • Genome-based identification and characterization of a putative mucin-binding protein from the surface of Streptococcus pneumoniae
    • Bumbaca D., et al. Genome-based identification and characterization of a putative mucin-binding protein from the surface of Streptococcus pneumoniae. Proteins 2007, 66:547-558.
    • (2007) Proteins , vol.66 , pp. 547-558
    • Bumbaca, D.1
  • 80
    • 79955397980 scopus 로고    scopus 로고
    • Fold and function of the InlB B-repeat
    • Ebbes M., et al. Fold and function of the InlB B-repeat. J. Biol. Chem. 2011, 286:15496-15506.
    • (2011) J. Biol. Chem. , vol.286 , pp. 15496-15506
    • Ebbes, M.1
  • 81
    • 16544390386 scopus 로고    scopus 로고
    • Fimbriae, pili, flagella and bacterial virulence
    • Jonson A.B., et al. Fimbriae, pili, flagella and bacterial virulence. Contrib. Microbiol. 2005, 12:67-89.
    • (2005) Contrib. Microbiol. , vol.12 , pp. 67-89
    • Jonson, A.B.1
  • 82
    • 0035026232 scopus 로고    scopus 로고
    • The adherent gastrointestinal mucus gel layer: thickness and physical state in vivo
    • Atuma C., et al. The adherent gastrointestinal mucus gel layer: thickness and physical state in vivo. Am. J. Physiol. Gastrointest. Liver Physiol. 2001, 280:G922-G929.
    • (2001) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.280
    • Atuma, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.