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Volumn 194, Issue 20, 2012, Pages 5564-5575

The accessory sec protein Asp2 modulates GlcNAc deposition onto the serine-rich repeat glycoprotein GspB

Author keywords

[No Author keywords available]

Indexed keywords

ACCESSORY SEC PROTEIN 2; ADHESIN; BACTERIAL PROTEIN; GLCNAC PROTEIN; GLUCOSAMINE; GLYCOPROTEIN; GSPB PROTEIN; MONOSACCHARIDE; UNCLASSIFIED DRUG;

EID: 84868564460     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01000-12     Document Type: Article
Times cited : (26)

References (48)
  • 1
    • 0034704990 scopus 로고    scopus 로고
    • Overproduction in Escherichia coli, purification and characterization of a family I.3 lipase from Pseudomonas sp
    • Amada K, Haruki M, Imanaka T, Morikawa M, Kanaya S. 2000. Overproduction in Escherichia coli, purification and characterization of a family I.3 lipase from Pseudomonas sp. MIS38. Biochim. Biophys. Acta 1478:201-210.
    • (2000) MIS38. Biochim. Biophys. Acta. , vol.1478 , pp. 201-210
    • Amada, K.1    Haruki, M.2    Imanaka, T.3    Morikawa, M.4    Kanaya, S.5
  • 2
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: classification and properties
    • Arpigny JL, Jaeger KE. 1999. Bacterial lipolytic enzymes: classification and properties. Biochem. J. 343(Pt 1):177-183.
    • (1999) Biochem. J. , vol.343 , Issue.PART 1 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 3
    • 1642459169 scopus 로고    scopus 로고
    • The Streptococcus gordonii platelet binding protein GspB undergoes glycosylation independently of export
    • Bensing BA, Gibson BW, Sullam PM. 2004. The Streptococcus gordonii platelet binding protein GspB undergoes glycosylation independently of export. J. Bacteriol. 186:638-645.
    • (2004) J. Bacteriol. , vol.186 , pp. 638-645
    • Bensing, B.A.1    Gibson, B.W.2    Sullam, P.M.3
  • 4
    • 7044249443 scopus 로고    scopus 로고
    • The Streptococcus gordonii surface proteins GspB and Hsa mediate binding to sialylated carbohydrate epitopes on the platelet membrane glycoprotein Ibalpha
    • Bensing BA, Lopez JA, Sullam PM. 2004. The Streptococcus gordonii surface proteins GspB and Hsa mediate binding to sialylated carbohydrate epitopes on the platelet membrane glycoprotein Ibalpha. Infect. Immun. 72:6528-6537.
    • (2004) Infect. Immun. , vol.72 , pp. 6528-6537
    • Bensing, B.A.1    Lopez, J.A.2    Sullam, P.M.3
  • 5
    • 0036091006 scopus 로고    scopus 로고
    • An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets
    • Bensing BA, Sullam PM. 2002. An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets. Mol. Microbiol. 44:1081-1094.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1081-1094
    • Bensing, B.A.1    Sullam, P.M.2
  • 6
    • 66149157283 scopus 로고    scopus 로고
    • Characterization of Streptococcus gordonii SecA2 as a paralogue of SecA
    • Bensing BA, Sullam PM. 2009. Characterization of Streptococcus gordonii SecA2 as a paralogue of SecA. J. Bacteriol. 191:3482-3491.
    • (2009) J. Bacteriol. , vol.191 , pp. 3482-3491
    • Bensing, B.A.1    Sullam, P.M.2
  • 7
    • 28244483290 scopus 로고    scopus 로고
    • Determinants of the streptococcal surface glycoprotein GspB that facilitate export by the accessory Sec system
    • Bensing BA, Takamatsu D, Sullam PM. 2005. Determinants of the streptococcal surface glycoprotein GspB that facilitate export by the accessory Sec system. Mol. Microbiol. 58:1468-1481.
    • (2005) Mol. Microbiol. , vol.58 , pp. 1468-1481
    • Bensing, B.A.1    Takamatsu, D.2    Sullam, P.M.3
  • 8
    • 0033812734 scopus 로고    scopus 로고
    • Improved vectors for nisin-controlled expression in Gram-positive bacteria
    • Bryan EM, Bae T, Kleerebezem M, Dunny GM. 2000. Improved vectors for nisin-controlled expression in Gram-positive bacteria. Plasmid 44: 183-190.
    • (2000) Plasmid , vol.44 , pp. 183-190
    • Bryan, E.M.1    Bae, T.2    Kleerebezem, M.3    Dunny, G.M.4
  • 9
    • 38949153119 scopus 로고    scopus 로고
    • Interaction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin
    • Bu S, et al. 2008. Interaction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin. J. Bacteriol. 190:1256-1266.
    • (2008) J. Bacteriol. , vol.190 , pp. 1256-1266
    • Bu, S.1
  • 10
    • 73549116509 scopus 로고    scopus 로고
    • Impaired lysosomal trimming of N-linked oligosaccharides leads to hyperglycosylation of native lysosomal proteins in mice with alpha-mannosidosis
    • Damme M, et al. 2010. Impaired lysosomal trimming of N-linked oligosaccharides leads to hyperglycosylation of native lysosomal proteins in mice with alpha-mannosidosis. Mol. Cell. Biol. 30:273-283.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 273-283
    • Damme, M.1
  • 11
    • 3142514373 scopus 로고    scopus 로고
    • The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus
    • de Graffenried CL, Bertozzi CR. 2004. The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus. Curr. Opin. Cell Biol. 16:356-363.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 356-363
    • Graffenried, D.C.L.1    Bertozzi, C.R.2
  • 12
    • 0036899975 scopus 로고    scopus 로고
    • Oligosaccharyl transferase: gatekeeper to the secretory pathway
    • Dempski RE, Jr, Imperiali B. 2002. Oligosaccharyl transferase: gatekeeper to the secretory pathway. Curr. Opin. Chem. Biol. 6:844-850.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 844-850
    • Dempski, R.E.Jr.1    Imperiali, B.2
  • 13
    • 84872428133 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 14
    • 56749154097 scopus 로고    scopus 로고
    • Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration
    • Ekici OD, Paetzel M, Dalbey RE. 2008. Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration. Protein Sci. 17:2023-2037.
    • (2008) Protein Sci. , vol.17 , pp. 2023-2037
    • Ekici, O.D.1    Paetzel, M.2    Dalbey, R.E.3
  • 15
    • 84857792795 scopus 로고    scopus 로고
    • Bacterial hydrolysis of host glycoproteins- powerful protein modification and efficient nutrient acquisition
    • Garbe J, Collin M. 2012. Bacterial hydrolysis of host glycoproteins- powerful protein modification and efficient nutrient acquisition. J. Innate Immun. 4:121-131.
    • (2012) J. Innate Immun. , vol.4 , pp. 121-131
    • Garbe, J.1    Collin, M.2
  • 16
    • 80052631636 scopus 로고    scopus 로고
    • Glycoside hydrolase activities of thermophilic bacterial consortia adapted to switchgrass
    • Gladden JM, et al. 2011. Glycoside hydrolase activities of thermophilic bacterial consortia adapted to switchgrass. Appl. Environ. Microbiol. 77: 5804-5812.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 5804-5812
    • Gladden, J.M.1
  • 17
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert DN, Foellmer B, Helenius A. 1995. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81:425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 19
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ. 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4:363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 20
    • 3242887695 scopus 로고    scopus 로고
    • Protein structure prediction and analysis using the Robetta server
    • doi:10.1093/nar/gkh468
    • Kim DE, Chivian D, Baker D. 2004. Protein structure prediction and analysis using the Robetta server. Nucleic Acids Res. 32:W526-W531. doi:10.1093/nar/gkh468.
    • (2004) Nucleic Acids Res. , vol.32
    • Kim, D.E.1    Chivian, D.2    Baker, D.3
  • 21
    • 79958165964 scopus 로고    scopus 로고
    • The expanding horizons of asparaginelinked glycosylation
    • Larkin A, Imperiali B. 2011. The expanding horizons of asparaginelinked glycosylation. Biochemistry 50:4411-4426.
    • (2011) Biochemistry , vol.50 , pp. 4411-4426
    • Larkin, A.1    Imperiali, B.2
  • 22
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: recent updates and new developments
    • doi:10.1093/nar/gkn808
    • Letunic I, Doerks T, Bork P. 2009. SMART 6: recent updates and new developments. Nucleic Acids Res. 37:D229-D232. doi:10.1093/nar/gkn808.
    • (2009) Nucleic Acids Res. , vol.37
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 23
    • 55349084760 scopus 로고    scopus 로고
    • A conserved domain of previously unknown function in Gap1 mediates protein-protein interaction and is required for biogenesis of a serine-rich streptococcal adhesin
    • Li Y, et al. 2008. A conserved domain of previously unknown function in Gap1 mediates protein-protein interaction and is required for biogenesis of a serine-rich streptococcal adhesin. Mol. Microbiol. 70: 1094-1104.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1094-1104
    • Li, Y.1
  • 24
    • 78651457518 scopus 로고    scopus 로고
    • Cellular interactions by LPxTG-anchored pneumococcal adhesins and their streptococcal homologues
    • Lofling J, Vimberg V, Battig P, Henriques-Normark B. 2011. Cellular interactions by LPxTG-anchored pneumococcal adhesins and their streptococcal homologues. Cell. Microbiol. 13:186-197.
    • (2011) Cell. Microbiol. , vol.13 , pp. 186-197
    • Lofling, J.1    Vimberg, V.2    Battig, P.3    Henriques-Normark, B.4
  • 25
    • 0029865960 scopus 로고    scopus 로고
    • Group B streptococci escape host immunity by deletion of tandem repeat elements of the alpha C protein
    • U. S. A.
    • Madoff LC, Michel JL, Gong EW, Kling DE, Kasper DL. 1996. Group B streptococci escape host immunity by deletion of tandem repeat elements of the alpha C protein. Proc. Natl. Acad. Sci. U. S. A. 93:4131-4136.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 4131-4136
    • Madoff, L.C.1    Michel, J.L.2    Gong, E.W.3    Kling, D.E.4    Kasper, D.L.5
  • 26
    • 67649404854 scopus 로고    scopus 로고
    • Molecular dissection of the secA2 locus of group B Streptococcus reveals that glycosylation of the Srr1 LPXTG protein is required for full virulence
    • Mistou MY, Dramsi S, Brega S, Poyart C, Trieu-Cuot P. 2009. Molecular dissection of the secA2 locus of group B Streptococcus reveals that glycosylation of the Srr1 LPXTG protein is required for full virulence. J. Bacteriol. 191:4195-4206.
    • (2009) J. Bacteriol. , vol.191 , pp. 4195-4206
    • Mistou, M.Y.1    Dramsi, S.2    Brega, S.3    Poyart, C.4    Trieu-Cuot, P.5
  • 27
    • 0037137471 scopus 로고    scopus 로고
    • Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals
    • Moremen KW. 2002. Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals. Biochim. Biophys. Acta 1573:225-235.
    • (2002) Biochim. Biophys. Acta. , vol.1573 , pp. 225-235
    • Moremen, K.W.1
  • 28
    • 70349307294 scopus 로고    scopus 로고
    • Role played by psrP-secY2A2 (accessory region 34) in the invasive disease potential of Streptococcus pneumoniae
    • Orihuela CJ. 2009. Role played by psrP-secY2A2 (accessory region 34) in the invasive disease potential of Streptococcus pneumoniae. J. Infect. Dis. 200:1180-1181.
    • (2009) J. Infect. Dis. , vol.200 , pp. 1180-1181
    • Orihuela, C.J.1
  • 29
    • 42549106474 scopus 로고    scopus 로고
    • Identification of critical residues in Gap3 of Streptococcus parasanguinis involved in Fap1 glycosylation, fimbrial formation and in vitro adhesion
    • doi:10.1186/ 1471-2180-8-52
    • Peng Z, et al. 2008. Identification of critical residues in Gap3 of Streptococcus parasanguinis involved in Fap1 glycosylation, fimbrial formation and in vitro adhesion. BMC Microbiol. 8:52. doi:10.1186/ 1471-2180-8-52.
    • (2008) BMC Microbiol. , vol.8 , pp. 52
    • Peng, Z.1
  • 30
    • 65649143489 scopus 로고    scopus 로고
    • The accessory SecA2 system of mycobacteria requires ATP binding and the canonical SecA1
    • Rigel NW, et al. 2009. The accessory SecA2 system of mycobacteria requires ATP binding and the canonical SecA1. J. Biol. Chem. 284:9927-9936.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9927-9936
    • Rigel, N.W.1
  • 33
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • U. S. A.
    • Schultz J, Milpetz F, Bork P, Ponting CP. 1998. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. U. S. A. 95:5857-5864.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 34
    • 78649377975 scopus 로고    scopus 로고
    • Asp3 mediates multiple protein-protein interactions within the accessory Sec system of Streptococcus gordonii
    • Seepersaud R, Bensing BA, Yen YT, Sullam PM. 2010. Asp3 mediates multiple protein-protein interactions within the accessory Sec system of Streptococcus gordonii. Mol. Microbiol. 78:490-505.
    • (2010) Mol. Microbiol. , vol.78 , pp. 490-505
    • Seepersaud, R.1    Bensing, B.A.2    Yen, Y.T.3    Sullam, P.M.4
  • 35
    • 70350168050 scopus 로고    scopus 로고
    • The Streptococcus pneumoniae adhesin PsrP binds to keratin 10 on lung cells
    • Shivshankar P, Sanchez C, Rose LF, Orihuela CJ. 2009. The Streptococcus pneumoniae adhesin PsrP binds to keratin 10 on lung cells. Mol. Microbiol. 73:663-679.
    • (2009) Mol. Microbiol. , vol.73 , pp. 663-679
    • Shivshankar, P.1    Sanchez, C.2    Rose, L.F.3    Orihuela, C.J.4
  • 36
    • 16244372364 scopus 로고    scopus 로고
    • Role of SraP, a serine-rich surface protein of Staphylococcus aureus, in binding to human platelets
    • Siboo IR, Chambers HF, Sullam PM. 2005. Role of SraP, a serine-rich surface protein of Staphylococcus aureus, in binding to human platelets. Infect. Immun. 73:2273-2280.
    • (2005) Infect. Immun. , vol.73 , pp. 2273-2280
    • Siboo, I.R.1    Chambers, H.F.2    Sullam, P.M.3
  • 37
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • doi:10.1093/nar/gki408
    • Soding J, Biegert A, Lupas AN. 2005. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33:W244-W248. doi:10.1093/nar/gki408.
    • (2005) Nucleic Acids Res. , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 38
    • 0023387522 scopus 로고
    • Mechanisms of platelet aggregation by viridans group streptococci
    • Sullam PM, Valone FH, Mills J. 1987. Mechanisms of platelet aggregation by viridans group streptococci. Infect. Immun. 55:1743-1750.
    • (1987) Infect. Immun. , vol.55 , pp. 1743-1750
    • Sullam, P.M.1    Valone, F.H.2    Mills, J.3
  • 39
    • 6044253695 scopus 로고    scopus 로고
    • Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii mediate the intracellular glycosylation of the platelet-binding protein GspB
    • Takamatsu D, Bensing BA, Sullam PM. 2004. Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii mediate the intracellular glycosylation of the platelet-binding protein GspB. J. Bacteriol. 186: 7100-7111.
    • (2004) J. Bacteriol. , vol.186 , pp. 7100-7111
    • Takamatsu, D.1    Bensing, B.A.2    Sullam, P.M.3
  • 40
    • 1942423779 scopus 로고    scopus 로고
    • Genes in the accessory sec locus of Streptococcus gordonii have three functionally distinct effects on the expression of the platelet-binding protein GspB
    • Takamatsu D, Bensing BA, Sullam PM. 2004. Genes in the accessory sec locus of Streptococcus gordonii have three functionally distinct effects on the expression of the platelet-binding protein GspB. Mol. Microbiol. 52: 189-203.
    • (2004) Mol. Microbiol. , vol.52 , pp. 189-203
    • Takamatsu, D.1    Bensing, B.A.2    Sullam, P.M.3
  • 41
    • 18944368165 scopus 로고    scopus 로고
    • Two additional components of the accessory sec system mediating export of the Streptococcus gordonii platelet-binding protein GspB
    • Takamatsu D, Bensing BA, Sullam PM. 2005. Two additional components of the accessory sec system mediating export of the Streptococcus gordonii platelet-binding protein GspB. J. Bacteriol. 187:3878-3883.
    • (2005) J. Bacteriol. , vol.187 , pp. 3878-3883
    • Takamatsu, D.1    Bensing, B.A.2    Sullam, P.M.3
  • 42
    • 65549095152 scopus 로고    scopus 로고
    • The group B streptococcal serine-rich repeat glycoprotein mediates penetration of the blood-brain barrier
    • van Sorge NM, et al. 2009. The group B streptococcal serine-rich repeat glycoprotein mediates penetration of the blood-brain barrier. J. Infect. Dis. 199:1479-1487.
    • (2009) J. Infect. Dis. , vol.199 , pp. 1479-1487
    • Sorge, N.M.V.1
  • 43
    • 34247542105 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, a serine esterase with a Ser-His-Asp catalytic triad
    • Weadge JT, Clarke AJ. 2007. Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, a serine esterase with a Ser-His-Asp catalytic triad. Biochemistry 46: 4932-4941.
    • (2007) Biochemistry , vol.46 , pp. 4932-4941
    • Weadge, J.T.1    Clarke, A.J.2
  • 44
    • 33846895628 scopus 로고    scopus 로고
    • Two gene determinants are differentially involved in the biogenesis of Fap1 precursors in Streptococcus parasanguis
    • Wu H, Bu S, Newell P, Chen Q, Fives-Taylor P. 2007. Two gene determinants are differentially involved in the biogenesis of Fap1 precursors in Streptococcus parasanguis. J. Bacteriol. 189:1390-1398.
    • (2007) J. Bacteriol. , vol.189 , pp. 1390-1398
    • Wu, H.1    Bu, S.2    Newell, P.3    Chen, Q.4    Fives-Taylor, P.5
  • 45
    • 50949085085 scopus 로고    scopus 로고
    • Role of the serine-rich surface glycoprotein GspB of Streptococcus gordonii in the pathogenesis of infective endocarditis
    • Xiong YQ, Bensing BA, Bayer AS, Chambers HF, Sullam PM. 2008. Role of the serine-rich surface glycoprotein GspB of Streptococcus gordonii in the pathogenesis of infective endocarditis. Microb. Pathog. 45:297-301.
    • (2008) Microb. Pathog. , vol.45 , pp. 297-301
    • Xiong, Y.Q.1    Bensing, B.A.2    Bayer, A.S.3    Chambers, H.F.4    Sullam, P.M.5
  • 46
    • 79959360177 scopus 로고    scopus 로고
    • Asp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec system
    • Yen YT, Seepersaud R, Bensing BA, Sullam PM. 2011. Asp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec system. J. Bacteriol. 193:3165-3174.
    • (2011) J. Bacteriol. , vol.193 , pp. 3165-3174
    • Yen, Y.T.1    Seepersaud, R.2    Bensing, B.A.3    Sullam, P.M.4
  • 47
    • 62249166648 scopus 로고    scopus 로고
    • Glycosylation and biogenesis of a family of serinerich bacterial adhesins
    • Zhou M, Wu H. 2009. Glycosylation and biogenesis of a family of serinerich bacterial adhesins. Microbiology 155:317-327.
    • (2009) Microbiology , vol.155 , pp. 317-327
    • Zhou, M.1    Wu, H.2
  • 48
    • 77951246027 scopus 로고    scopus 로고
    • A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinis
    • Zhou M, Zhu F, Dong S, Pritchard DG, Wu H. 2010. A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinis. J. Biol. Chem. 285: 12140-12148.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12140-12148
    • Zhou, M.1    Zhu, F.2    Dong, S.3    Pritchard, D.G.4    Wu, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.