메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

Global Identification of Prokaryotic Glycoproteins Based on an Escherichia coli Proteome Microarray

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN;

EID: 84868689228     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049080     Document Type: Article
Times cited : (8)

References (55)
  • 1
    • 70349333832 scopus 로고    scopus 로고
    • Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes
    • Kung LA, Tao SC, Qian J, Smith MG, Snyder M, et al. (2009) Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes. Mol Syst Biol 5: 308.
    • (2009) Mol Syst Biol , vol.5 , pp. 308
    • Kung, L.A.1    Tao, S.C.2    Qian, J.3    Smith, M.G.4    Snyder, M.5
  • 2
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, Sharon N, (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1473: 4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 3
    • 80053133500 scopus 로고    scopus 로고
    • Human sperm binding is mediated by the sialyl-Lewis(x) oligosaccharide on the zona pellucida
    • Pang PC, Chiu PC, Lee CL, Chang LY, Panico M, et al. (2011) Human sperm binding is mediated by the sialyl-Lewis(x) oligosaccharide on the zona pellucida. Science 333: 1761-1764.
    • (2011) Science , vol.333 , pp. 1761-1764
    • Pang, P.C.1    Chiu, P.C.2    Lee, C.L.3    Chang, L.Y.4    Panico, M.5
  • 4
    • 84860382308 scopus 로고    scopus 로고
    • The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer
    • Rambaruth ND, Greenwell P, Dwek MV, (2012) The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer. Glycobiology 22: 839-848.
    • (2012) Glycobiology , vol.22 , pp. 839-848
    • Rambaruth, N.D.1    Greenwell, P.2    Dwek, M.V.3
  • 5
    • 84865556124 scopus 로고    scopus 로고
    • Chitin-like molecules associate with Cryptococcus neoformans glucuronoxylomannan to form a glycan complex with previously unknown properties
    • Ramos CL, Fonseca FL, Rodrigues J, Guimaraes AJ, Cinelli LP, et al. (2012) Chitin-like molecules associate with Cryptococcus neoformans glucuronoxylomannan to form a glycan complex with previously unknown properties. Eukaryot Cell.
    • (2012) Eukaryot Cell.
    • Ramos, C.L.1    Fonseca, F.L.2    Rodrigues, J.3    Guimaraes, A.J.4    Cinelli, L.P.5
  • 6
    • 77951109730 scopus 로고    scopus 로고
    • On the road to systems biology of host-pathogen interactions
    • Fruh K, Finlay B, McFadden G, (2010) On the road to systems biology of host-pathogen interactions. Future Microbiol 5: 131-133.
    • (2010) Future Microbiol , vol.5 , pp. 131-133
    • Fruh, K.1    Finlay, B.2    McFadden, G.3
  • 7
    • 0006052194 scopus 로고
    • Carbohydrates in protein: The carbohydrate component of crystalline egg albumin
    • Neuberger A, (1938) Carbohydrates in protein: The carbohydrate component of crystalline egg albumin. Biochem J 32: 1435-1451.
    • (1938) Biochem J , vol.32 , pp. 1435-1451
    • Neuberger, A.1
  • 8
    • 0030825124 scopus 로고    scopus 로고
    • Glycoproteins in prokaryotes
    • Moens S, Vanderleyden J, (1997) Glycoproteins in prokaryotes. Arch Microbiol 168: 169-175.
    • (1997) Arch Microbiol , vol.168 , pp. 169-175
    • Moens, S.1    Vanderleyden, J.2
  • 9
    • 0017278612 scopus 로고
    • Purification and characterization of a prokaryotic glucoprotein from the cell envelope of Halobacterium salinarium
    • Mescher MF, Strominger JL, (1976) Purification and characterization of a prokaryotic glucoprotein from the cell envelope of Halobacterium salinarium. J Biol Chem 251: 2005-2014.
    • (1976) J Biol Chem , vol.251 , pp. 2005-2014
    • Mescher, M.F.1    Strominger, J.L.2
  • 10
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski CM, Wren BW, (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
  • 11
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: glycoproteins in bacterial pathogens
    • Schmidt MA, Riley LW, 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
  • 12
    • 0036067107 scopus 로고    scopus 로고
    • Never say never again: protein glycosylation in pathogenic bacteria
    • Benz I, Schmidt MA, (2002) Never say never again: protein glycosylation in pathogenic bacteria. Mol Microbiol 45: 267-276.
    • (2002) Mol Microbiol , vol.45 , pp. 267-276
    • Benz, I.1    Schmidt, M.A.2
  • 13
    • 72949093996 scopus 로고    scopus 로고
    • Modification of N-glycosylation sites allows secretion of bacterial chondroitinase ABC from mammalian cells
    • Muir EM, Fyfe I, Gardiner S, Li L, Warren P, et al. (2010) Modification of N-glycosylation sites allows secretion of bacterial chondroitinase ABC from mammalian cells. J Biotechnol 145: 103-110.
    • (2010) J Biotechnol , vol.145 , pp. 103-110
    • Muir, E.M.1    Fyfe, I.2    Gardiner, S.3    Li, L.4    Warren, P.5
  • 14
    • 79951634140 scopus 로고    scopus 로고
    • Glycosylation is required for outer membrane localization of the lectin LecB in Pseudomonas aeruginosa
    • Bartels KM, Funken H, Knapp A, Brocker M, Bott M, et al. (2011) Glycosylation is required for outer membrane localization of the lectin LecB in Pseudomonas aeruginosa. J Bacteriol 193: 1107-1113.
    • (2011) J Bacteriol , vol.193 , pp. 1107-1113
    • Bartels, K.M.1    Funken, H.2    Knapp, A.3    Brocker, M.4    Bott, M.5
  • 15
    • 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, Schmidt MA, (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
  • 16
    • 0032783142 scopus 로고    scopus 로고
    • Identification of a glycoprotein produced by enterotoxigenic Escherichia coli
    • Lindenthal C, Elsinghorst EA, (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
  • 17
    • 33644769605 scopus 로고    scopus 로고
    • Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein
    • Sherlock O, Dobrindt U, Jensen JB, Munk Vejborg R, 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    Munk Vejborg, R.4    Klemm, P.5
  • 18
    • 0037387036 scopus 로고    scopus 로고
    • Bacterial glycoproteins: functions, biosynthesis and applications
    • Upreti RK, Kumar M, Shankar V, (2003) Bacterial glycoproteins: functions, biosynthesis and applications. Proteomics 3: 363-379.
    • (2003) Proteomics , vol.3 , pp. 363-379
    • Upreti, R.K.1    Kumar, M.2    Shankar, V.3
  • 19
    • 61649089277 scopus 로고    scopus 로고
    • Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli
    • Zhang J, Sprung R, Pei J, Tan X, Kim S, et al. (2009) Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics 8: 215-225.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 215-225
    • Zhang, J.1    Sprung, R.2    Pei, J.3    Tan, X.4    Kim, S.5
  • 20
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang Q, Zhang Y, Yang C, Xiong H, Lin Y, et al. (2010) Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 327: 1004-1007.
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4    Lin, Y.5
  • 21
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu H, Bilgin M, Bangham R, Hall D, Casamayor A, et al. (2001) Global analysis of protein activities using proteome chips. Science 293: 2101-2105.
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1    Bilgin, M.2    Bangham, R.3    Hall, D.4    Casamayor, A.5
  • 22
    • 37749048465 scopus 로고    scopus 로고
    • A proteome chip approach reveals new DNA damage recognition activities in Escherichia coli
    • Chen CS, Korobkova E, Chen H, Zhu J, Jian X, et al. (2008) A proteome chip approach reveals new DNA damage recognition activities in Escherichia coli. Nat Methods 5: 69-74.
    • (2008) Nat Methods , vol.5 , pp. 69-74
    • Chen, C.S.1    Korobkova, E.2    Chen, H.3    Zhu, J.4    Jian, X.5
  • 25
    • 79958285205 scopus 로고    scopus 로고
    • A functional protein microarray approach to characterizing posttranslational modifications on lysine residues
    • Jeong JS, Rho HS, Zhu H, (2011) A functional protein microarray approach to characterizing posttranslational modifications on lysine residues. Methods Mol Biol 723: 213-223.
    • (2011) Methods Mol Biol , vol.723 , pp. 213-223
    • Jeong, J.S.1    Rho, H.S.2    Zhu, H.3
  • 26
  • 28
    • 62149143727 scopus 로고    scopus 로고
    • Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis
    • Lin YY, Lu JY, Zhang J, Walter W, Dang W, et al. (2009) Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell 136: 1073-1084.
    • (2009) Cell , vol.136 , pp. 1073-1084
    • Lin, Y.Y.1    Lu, J.Y.2    Zhang, J.3    Walter, W.4    Dang, W.5
  • 29
    • 0037249501 scopus 로고    scopus 로고
    • PANTHER: a browsable database of gene products organized by biological function, using curated protein family and subfamily classification
    • Thomas PD, Kejariwal A, Campbell MJ, Mi H, Diemer K, et al. (2003) PANTHER: a browsable database of gene products organized by biological function, using curated protein family and subfamily classification. Nucleic Acids Res 31: 334-341.
    • (2003) Nucleic Acids Res , vol.31 , pp. 334-341
    • Thomas, P.D.1    Kejariwal, A.2    Campbell, M.J.3    Mi, H.4    Diemer, K.5
  • 30
    • 78651324347 scopus 로고    scopus 로고
    • The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored
    • Szklarczyk D, Franceschini A, Kuhn M, Simonovic M, Roth A, et al. (2011) The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored. Nucleic Acids Res 39: D561-568.
    • (2011) Nucleic Acids Res , vol.39
    • Szklarczyk, D.1    Franceschini, A.2    Kuhn, M.3    Simonovic, M.4    Roth, A.5
  • 31
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O, Brunak S, von Heijne G, Nielsen H, (2007) Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protocols 2: 953-971.
    • (2007) Nat Protocols , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 33
    • 75549084894 scopus 로고    scopus 로고
    • PANTHER version 7: improved phylogenetic trees, orthologs and collaboration with the Gene Ontology Consortium
    • Mi H, Dong Q, Muruganujan A, Gaudet P, Lewis S, et al. (2010) PANTHER version 7: improved phylogenetic trees, orthologs and collaboration with the Gene Ontology Consortium. Nucleic Acids Res 38: D204-210.
    • (2010) Nucleic Acids Res , vol.38
    • Mi, H.1    Dong, Q.2    Muruganujan, A.3    Gaudet, P.4    Lewis, S.5
  • 35
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H, (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 37
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F, (1999) Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol 10: 411-421.
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 38
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • Choi JH, Lee SY, (2004) Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol 64: 625-635.
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 39
    • 84862321638 scopus 로고    scopus 로고
    • Rapid identification of monospecific monoclonal antibodies using a human proteome microarray
    • Jeong JS, Jiang L, Albino E, Marrero J, Rho HS, et al. (2012) Rapid identification of monospecific monoclonal antibodies using a human proteome microarray. Mol Cell Proteomics.
    • (2012) Mol Cell Proteomics.
    • Jeong, J.S.1    Jiang, L.2    Albino, E.3    Marrero, J.4    Rho, H.S.5
  • 40
    • 0029779295 scopus 로고    scopus 로고
    • Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid
    • Stevenson G, Andrianopoulos K, Hobbs M, Reeves PR, (1996) Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid. J Bacteriol 178: 4885-4893.
    • (1996) J Bacteriol , vol.178 , pp. 4885-4893
    • Stevenson, G.1    Andrianopoulos, K.2    Hobbs, M.3    Reeves, P.R.4
  • 41
    • 0028102534 scopus 로고
    • The leucine-responsive regulatory protein binds to the fim switch to control phase variation of type 1 fimbrial expression in Escherichia coli K-12
    • Gally DL, Rucker TJ, Blomfield IC, (1994) The leucine-responsive regulatory protein binds to the fim switch to control phase variation of type 1 fimbrial expression in Escherichia coli K-12. J Bacteriol 176: 5665-5672.
    • (1994) J Bacteriol , vol.176 , pp. 5665-5672
    • Gally, D.L.1    Rucker, T.J.2    Blomfield, I.C.3
  • 42
    • 77952491040 scopus 로고    scopus 로고
    • In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz
    • Woodward R, Yi W, Li L, Zhao G, Eguchi H, et al. (2010) In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat Chem Biol 6: 418-423.
    • (2010) Nat Chem Biol , vol.6 , pp. 418-423
    • Woodward, R.1    Yi, W.2    Li, L.3    Zhao, G.4    Eguchi, H.5
  • 44
    • 0024517699 scopus 로고
    • Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli
    • Benz I, Schmidt MA, (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
  • 45
    • 37449026606 scopus 로고    scopus 로고
    • O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence
    • Charbonneau ME, Girard V, Nikolakakis A, Campos M, Berthiaume F, et al. (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
  • 46
    • 0028037936 scopus 로고
    • Epithelial cell invasion and adherence directed by the enterotoxigenic Escherichia coli tib locus is associated with a 104-kilodalton outer membrane protein
    • Elsinghorst EA, Weitz JA, (1994) Epithelial cell invasion and adherence directed by the enterotoxigenic Escherichia coli tib locus is associated with a 104-kilodalton outer membrane protein. Infect Immun 62: 3463-3471.
    • (1994) Infect Immun , vol.62 , pp. 3463-3471
    • Elsinghorst, E.A.1    Weitz, J.A.2
  • 47
    • 0035159696 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli TibA glycoprotein adheres to human intestine epithelial cells
    • Lindenthal C, Elsinghorst EA, (2001) Enterotoxigenic Escherichia coli TibA glycoprotein adheres to human intestine epithelial cells. Infect Immun 69: 52-57.
    • (2001) Infect Immun , vol.69 , pp. 52-57
    • Lindenthal, C.1    Elsinghorst, E.A.2
  • 48
    • 0018829161 scopus 로고
    • flu, a metastable gene controlling surface properties of Escherichia coli
    • Diderichsen B, (1980) flu, a metastable gene controlling surface properties of Escherichia coli. J Bacteriol 141: 858-867.
    • (1980) J Bacteriol , vol.141 , pp. 858-867
    • Diderichsen, B.1
  • 49
    • 0032816696 scopus 로고    scopus 로고
    • Antigen-43-mediated autoaggregation of Escherichia coli is blocked by fimbriation
    • Hasman H, Chakraborty T, Klemm P, (1999) Antigen-43-mediated autoaggregation of Escherichia coli is blocked by fimbriation. J Bacteriol 181: 4834-4841.
    • (1999) J Bacteriol , vol.181 , pp. 4834-4841
    • Hasman, H.1    Chakraborty, T.2    Klemm, P.3
  • 50
    • 0032940207 scopus 로고    scopus 로고
    • The major phase-variable outer membrane protein of Escherichia coli structurally resembles the immunoglobulin A1 protease class of exported protein and is regulated by a novel mechanism involving Dam and oxyR
    • Henderson IR, Owen P, (1999) The major phase-variable outer membrane protein of Escherichia coli structurally resembles the immunoglobulin A1 protease class of exported protein and is regulated by a novel mechanism involving Dam and oxyR. J Bacteriol 181: 2132-2141.
    • (1999) J Bacteriol , vol.181 , pp. 2132-2141
    • Henderson, I.R.1    Owen, P.2
  • 51
    • 80052479968 scopus 로고    scopus 로고
    • Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes
    • Dell A, Galadari A, Sastre F, Hitchen P, (2010) Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes. Int J Microbiol 2010: 148178.
    • (2010) Int J Microbiol , vol.2010 , pp. 148178
    • Dell, A.1    Galadari, A.2    Sastre, F.3    Hitchen, P.4
  • 52
    • 0034088763 scopus 로고    scopus 로고
    • Bacterial adhesins: function and structure
    • Klemm P, Schembri MA, (2000) Bacterial adhesins: function and structure. Int J Med Microbiol 290: 27-35.
    • (2000) Int J Med Microbiol , vol.290 , pp. 27-35
    • Klemm, P.1    Schembri, M.A.2
  • 53
    • 0346964245 scopus 로고    scopus 로고
    • Structure-function analysis of the self-recognizing Antigen 43 autotransporter protein from Escherichia coli
    • Klemm P, Hjerrild L, Gjermansen M, Schembri MA, (2004) Structure-function analysis of the self-recognizing Antigen 43 autotransporter protein from Escherichia coli. Mol Microbiol 51: 283-296.
    • (2004) Mol Microbiol , vol.51 , pp. 283-296
    • Klemm, P.1    Hjerrild, L.2    Gjermansen, M.3    Schembri, M.A.4
  • 54
  • 55
    • 0038128166 scopus 로고    scopus 로고
    • Where and why are 10 million children dying every year?
    • Black RE, Morris SS, Bryce J, (2003) Where and why are 10 million children dying every year? Lancet 361: 2226-2234.
    • (2003) Lancet , vol.361 , pp. 2226-2234
    • Black, R.E.1    Morris, S.S.2    Bryce, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.