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Volumn 83, Issue 5, 2012, Pages 894-907

A structural motif is the recognition site for a new family of bacterial protein O-glycosyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN INVOLVED IN DIFFUSE ADHERENCE; AIDA ASSOCIATED HEPTOSYLTRANSFERASE; BACTERIAL PROTEIN; GLYCOSYLTRANSFERASE; PERTACTIN; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84857356491     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.07973.x     Document Type: Article
Times cited : (25)

References (40)
  • 1
    • 0024517699 scopus 로고
    • Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli
    • Benz, I., and Schmidt, M.A. (1989) Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli. Infect Immun 57: 1506-1511.
    • (1989) Infect Immun , vol.57 , pp. 1506-1511
    • Benz, I.1    Schmidt, M.A.2
  • 2
    • 0034939563 scopus 로고    scopus 로고
    • Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-I adhesin
    • Benz, I., and Schmidt, M.A. (2001) Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-I adhesin. Mol Microbiol 40: 1403-1413.
    • (2001) Mol Microbiol , vol.40 , pp. 1403-1413
    • Benz, I.1    Schmidt, M.A.2
  • 3
    • 33746068641 scopus 로고    scopus 로고
    • Comparison of virulence gene profiles of Escherichia coli strains isolated from healthy and diarrheic swine
    • Chapman, T.A., Wu, X.Y., Barchia, I., Bettelheim, K.A., Driesen, S., Trott, D., etal. (2006) Comparison of virulence gene profiles of Escherichia coli strains isolated from healthy and diarrheic swine. Appl Environ Microbiol 72: 4782-4795.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 4782-4795
    • Chapman, T.A.1    Wu, X.Y.2    Barchia, I.3    Bettelheim, K.A.4    Driesen, S.5    Trott, D.6
  • 4
    • 37449035041 scopus 로고    scopus 로고
    • Functional organization of the autotransporter adhesin involved in diffuse adherence
    • Charbonneau, M.E., and Mourez, M. (2007) Functional organization of the autotransporter adhesin involved in diffuse adherence. J Bacteriol 189: 9020-9029.
    • (2007) J Bacteriol , vol.189 , pp. 9020-9029
    • Charbonneau, M.E.1    Mourez, M.2
  • 5
    • 33845452751 scopus 로고    scopus 로고
    • Proteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I)
    • Charbonneau, M.E., Berthiaume, F., and Mourez, M. (2006) Proteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I). J Bacteriol 188: 8504-8512.
    • (2006) J Bacteriol , vol.188 , pp. 8504-8512
    • Charbonneau, M.E.1    Berthiaume, F.2    Mourez, M.3
  • 6
    • 37449026606 scopus 로고    scopus 로고
    • O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence
    • Charbonneau, M.E., Girard, V., Nikolakakis, A., Campos, M., Berthiaume, F., Dumas, F., etal. (2007) O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence. J Bacteriol 189: 8880-8889.
    • (2007) J Bacteriol , vol.189 , pp. 8880-8889
    • Charbonneau, M.E.1    Girard, V.2    Nikolakakis, A.3    Campos, M.4    Berthiaume, F.5    Dumas, F.6
  • 7
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 8
    • 0029965091 scopus 로고    scopus 로고
    • Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis
    • Dobos, K.M., Khoo, K.H., Swiderek, K.M., Brennan, P.J., and Belisle, J.T. (1996) Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis. J Bacteriol 178: 2498-2506.
    • (1996) J Bacteriol , vol.178 , pp. 2498-2506
    • Dobos, K.M.1    Khoo, K.H.2    Swiderek, K.M.3    Brennan, P.J.4    Belisle, J.T.5
  • 9
    • 84857355592 scopus 로고    scopus 로고
    • Characterization of EhaJ, a new autotransporter protein from enterohemorrhagic and enteropathogenic Escherichia coli
    • Easton, D.M., Totsika, M., Allsopp, L., Phan, M.D., Idris, A., Wurpel, D.J., etal. (2011) Characterization of EhaJ, a new autotransporter protein from enterohemorrhagic and enteropathogenic Escherichia coli. Front Microbiol 2: 120.
    • (2011) Front Microbiol , vol.2 , pp. 120
    • Easton, D.M.1    Totsika, M.2    Allsopp, L.3    Phan, M.D.4    Idris, A.5    Wurpel, D.J.6
  • 10
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley, P., Charles, I.G., Fairweather, N.F., and Isaacs, N.W. (1996) Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature 381: 90-92.
    • (1996) Nature , vol.381 , pp. 90-92
    • Emsley, P.1    Charles, I.G.2    Fairweather, N.F.3    Isaacs, N.W.4
  • 11
    • 64249095086 scopus 로고    scopus 로고
    • A general O-glycosylation system important to the physiology of a major human intestinal symbiont
    • Fletcher, C.M., Coyne, M.J., Villa, O.F., Chatzidaki-Livanis, M., and Comstock, L.E. (2009) A general O-glycosylation system important to the physiology of a major human intestinal symbiont. Cell 137: 321-331.
    • (2009) Cell , vol.137 , pp. 321-331
    • Fletcher, C.M.1    Coyne, M.J.2    Villa, O.F.3    Chatzidaki-Livanis, M.4    Comstock, L.E.5
  • 12
    • 79952797070 scopus 로고    scopus 로고
    • Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis
    • Fletcher, C.M., Coyne, M.J., and Comstock, L.E. (2011) Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis. J Biol Chem 286: 3219-3226.
    • (2011) J Biol Chem , vol.286 , pp. 3219-3226
    • Fletcher, C.M.1    Coyne, M.J.2    Comstock, L.E.3
  • 13
    • 0030894597 scopus 로고    scopus 로고
    • Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide:galnac transferase peptide binding site
    • Gerken, T.A., Owens, C.L., and Pasumarthy, M. (1997) Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide:galnac transferase peptide binding site. J Biol Chem 272: 9709-9719.
    • (1997) J Biol Chem , vol.272 , pp. 9709-9719
    • Gerken, T.A.1    Owens, C.L.2    Pasumarthy, M.3
  • 14
    • 0027772063 scopus 로고
    • The nature of the carbohydrate-peptide linkage region in glycoproteins from the cellulosomes of Clostridium thermocellum and Bacteroides cellulosolvens
    • Gerwig, G.J., Kamerling, J., Vliegenthart, J.F., Morag, E., Lamed, R., and Bayer, E.A. (1993) The nature of the carbohydrate-peptide linkage region in glycoproteins from the cellulosomes of Clostridium thermocellum and Bacteroides cellulosolvens. J Biol Chem 268: 26956-26960.
    • (1993) J Biol Chem , vol.268 , pp. 26956-26960
    • Gerwig, G.J.1    Kamerling, J.2    Vliegenthart, J.F.3    Morag, E.4    Lamed, R.5    Bayer, E.A.6
  • 15
    • 0037673430 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis
    • Grass, S., Buscher, A.Z., Swords, W.E., Apicella, M.A., Barenkamp, S.J., Ozchlewski, N., and St Geme, J.W., 3rd (2003) The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis. Mol Microbiol 48: 737-751.
    • (2003) Mol Microbiol , vol.48 , pp. 737-751
    • Grass, S.1    Buscher, A.Z.2    Swords, W.E.3    Apicella, M.A.4    Barenkamp, S.J.5    Ozchlewski, N.6    St Geme 3rd, J.W.7
  • 16
    • 77954080496 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin
    • Grass, S., Lichti, C.F., Townsend, R.R., Gross, J., and St Geme, J.W., 3rd (2010) The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin. PLoS Pathog 6: e1000919.
    • (2010) PLoS Pathog , vol.6
    • Grass, S.1    Lichti, C.F.2    Townsend, R.R.3    Gross, J.4    St Geme 3rd, J.W.5
  • 17
    • 54449094921 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification
    • Gross, J., Grass, S., Davis, A.E., Gilmore-Erdmann, P., Townsend, R.R., and St Geme, J.W., 3rd (2008) The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification. J Biol Chem 283: 26010-26015.
    • (2008) J Biol Chem , vol.283 , pp. 26010-26015
    • Gross, J.1    Grass, S.2    Davis, A.E.3    Gilmore-Erdmann, P.4    Townsend, R.R.5    St Geme 3rd, J.W.6
  • 19
    • 79956083561 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements
    • Ielmini, M.V., and Feldman, M.F. (2011) Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements. Glycobiology 21: 734-742.
    • (2011) Glycobiology , vol.21 , pp. 734-742
    • Ielmini, M.V.1    Feldman, M.F.2
  • 20
    • 33747790227 scopus 로고    scopus 로고
    • The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of Type V secretory proteins
    • Kajava, A.V., and Steven, A.C. (2006) The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of Type V secretory proteins. J Struct Biol 155: 306-315.
    • (2006) J Struct Biol , vol.155 , pp. 306-315
    • Kajava, A.V.1    Steven, A.C.2
  • 21
    • 33745875356 scopus 로고    scopus 로고
    • Self-associating autotransporters, SAATs: functional and structural similarities
    • Klemm, P., Vejborg, R.M., and Sherlock, O. (2006) Self-associating autotransporters, SAATs: functional and structural similarities. Int J Med Microbiol 296: 187-195.
    • (2006) Int J Med Microbiol , vol.296 , pp. 187-195
    • Klemm, P.1    Vejborg, R.M.2    Sherlock, O.3
  • 22
    • 45349105648 scopus 로고    scopus 로고
    • Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation
    • Knudsen, S.K., Stensballe, A., Franzmann, M., Westergaard, U.B., and Otzen, D.E. (2008) Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation. Biochem J 412: 563-577.
    • (2008) Biochem J , vol.412 , pp. 563-577
    • Knudsen, S.K.1    Stensballe, A.2    Franzmann, M.3    Westergaard, U.B.4    Otzen, D.E.5
  • 23
    • 33646564396 scopus 로고    scopus 로고
    • Definition of the bacterial N-glycosylation site consensus sequence
    • Kowarik, M., Young, N.M., Numao, S., Schulz, B.L., Hug, I., Callewaert, N., etal. (2006) Definition of the bacterial N-glycosylation site consensus sequence. EMBO J 25: 1957-1966.
    • (2006) EMBO J , vol.25 , pp. 1957-1966
    • Kowarik, M.1    Young, N.M.2    Numao, S.3    Schulz, B.L.4    Hug, I.5    Callewaert, N.6
  • 24
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus, M.B., Nam, Y., Jiang, J., Sliz, P., and Walker, S. (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469: 564-567.
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 25
    • 0032783142 scopus 로고    scopus 로고
    • Identification of a glycoprotein produced by enterotoxigenic Escherichia coli
    • Lindenthal, C., and Elsinghorst, E.A. (1999) Identification of a glycoprotein produced by enterotoxigenic Escherichia coli. Infect Immun 67: 4084-4091.
    • (1999) Infect Immun , vol.67 , pp. 4084-4091
    • Lindenthal, C.1    Elsinghorst, E.A.2
  • 26
    • 0036122161 scopus 로고    scopus 로고
    • Functional substitution of the TibC protein of enterotoxigenic Escherichia coli strains for the autotransporter adhesin heptosyltransferase of the AIDA system
    • Moormann, C., Benz, I., and Schmidt, M.A. (2002) Functional substitution of the TibC protein of enterotoxigenic Escherichia coli strains for the autotransporter adhesin heptosyltransferase of the AIDA system. Infect Immun 70: 2264-2270.
    • (2002) Infect Immun , vol.70 , pp. 2264-2270
    • Moormann, C.1    Benz, I.2    Schmidt, M.A.3
  • 27
    • 0035161265 scopus 로고    scopus 로고
    • The AIDA autotransporter system is associated with F18 and stx2e in Escherichia coli isolates from pigs diagnosed with edema disease and postweaning diarrhea
    • Niewerth, U., Frey, A., Voss, T., Bouguenec, C.L., Baljer, G., Franke, S., and Schmidt, M.A. (2001) The AIDA autotransporter system is associated with F18 and stx2e in Escherichia coli isolates from pigs diagnosed with edema disease and postweaning diarrhea. Clin Diagn Lab Immunol 8: 143-149.
    • (2001) Clin Diagn Lab Immunol , vol.8 , pp. 143-149
    • Niewerth, U.1    Frey, A.2    Voss, T.3    Bouguenec, C.L.4    Baljer, G.5    Franke, S.6    Schmidt, M.A.7
  • 28
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: sweeter than ever
    • Nothaft, H., and Szymanski, C.M. (2010) Protein glycosylation in bacteria: sweeter than ever. Nat Rev Microbiol 8: 765-778.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 29
    • 0029040382 scopus 로고
    • Novel, specific O-glycosylation of secreted Flavobacterium meningosepticum proteins. Asp-Ser and Asp-Thr-Thr consensus sites
    • Plummer, T.H., Jr, Tarentino, A.L., and Hauer, C.R. (1995) Novel, specific O-glycosylation of secreted Flavobacterium meningosepticum proteins. Asp-Ser and Asp-Thr-Thr consensus sites. J Biol Chem 270: 13192-13196.
    • (1995) J Biol Chem , vol.270 , pp. 13192-13196
    • Plummer Jr., T.H.1    Tarentino, A.L.2    Hauer, C.R.3
  • 30
    • 33846781661 scopus 로고    scopus 로고
    • Contribution of AIDA-I to the pathogenicity of a porcine diarrheagenic Escherichia coli and to intestinal colonization through biofilm formation in pigs
    • Ravi, M., Ngeleka, M., Kim, S.H., Gyles, C., Berthiaume, F., Mourez, M., etal. (2007) Contribution of AIDA-I to the pathogenicity of a porcine diarrheagenic Escherichia coli and to intestinal colonization through biofilm formation in pigs. Vet Microbiol 120: 308-319.
    • (2007) Vet Microbiol , vol.120 , pp. 308-319
    • Ravi, M.1    Ngeleka, M.2    Kim, S.H.3    Gyles, C.4    Berthiaume, F.5    Mourez, M.6
  • 32
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: glycoproteins in bacterial pathogens
    • Schmidt, M.A., Riley, L.W., and Benz, I. (2003) Sweet new world: glycoproteins in bacterial pathogens. Trends Microbiol 11: 554-561.
    • (2003) Trends Microbiol , vol.11 , pp. 554-561
    • Schmidt, M.A.1    Riley, L.W.2    Benz, I.3
  • 33
    • 9244250348 scopus 로고    scopus 로고
    • Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation
    • Sherlock, O., Schembri, M.A., Reisner, A., and Klemm, P. (2004) Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation. J Bacteriol 186: 8058-8065.
    • (2004) J Bacteriol , vol.186 , pp. 8058-8065
    • Sherlock, O.1    Schembri, M.A.2    Reisner, A.3    Klemm, P.4
  • 34
    • 33644769605 scopus 로고    scopus 로고
    • Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein
    • Sherlock, O., Dobrindt, U., Jensen, J.B., Vejborg, R.M., and Klemm, P. (2006) Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein. J Bacteriol 188: 1798-1807.
    • (2006) J Bacteriol , vol.188 , pp. 1798-1807
    • Sherlock, O.1    Dobrindt, U.2    Jensen, J.B.3    Vejborg, R.M.4    Klemm, P.5
  • 35
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski, C.M., and Wren, B.W. (2005) Protein glycosylation in bacterial mucosal pathogens. Nat Rev Microbiol 3: 225-237.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 225-237
    • Szymanski, C.M.1    Wren, B.W.2
  • 36
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski, C.M., Yao, R., Ewing, C., Trust, T.J., and Guerry, P. (1999) Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol Microbiol 32: 1022-1030.
    • (1999) Mol Microbiol , vol.32 , pp. 1022-1030
    • Szymanski, C.M.1    Yao, R.2    Ewing, C.3    Trust, T.J.4    Guerry, P.5
  • 37
    • 77749288958 scopus 로고    scopus 로고
    • Glycosylation of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans is dependent upon the lipopolysaccharide biosynthetic pathway
    • Tang, G., and Mintz, K. (2010) Glycosylation of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans is dependent upon the lipopolysaccharide biosynthetic pathway. J Bacteriol 192: 1395-1404.
    • (2010) J Bacteriol , vol.192 , pp. 1395-1404
    • Tang, G.1    Mintz, K.2
  • 39
    • 0033616129 scopus 로고    scopus 로고
    • Oligosaccharyltransferase: a complex multisubunit enzyme of the endoplasmic reticulum
    • Yan, Q., and Lennarz, W.J. (1999) Oligosaccharyltransferase: a complex multisubunit enzyme of the endoplasmic reticulum. Biochem Biophys Res Commun 266: 684-689.
    • (1999) Biochem Biophys Res Commun , vol.266 , pp. 684-689
    • Yan, Q.1    Lennarz, W.J.2
  • 40
    • 34250195741 scopus 로고    scopus 로고
    • Prevalence of virulence genes in Escherichia coli strains recently isolated from young pigs with diarrhea in the US
    • Zhang, W., Zhao, M., Ruesch, L., Omot, A., and Francis, D. (2007) Prevalence of virulence genes in Escherichia coli strains recently isolated from young pigs with diarrhea in the US. Vet Microbiol 123: 145-152.
    • (2007) Vet Microbiol , vol.123 , pp. 145-152
    • Zhang, W.1    Zhao, M.2    Ruesch, L.3    Omot, A.4    Francis, D.5


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