메뉴 건너뛰기




Volumn 189, Issue 24, 2007, Pages 8880-8889

O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; ADHESIN INVOLVED IN DIFFUSE ADHERENCE 1 PROTEIN; GLUTATHIONE TRANSFERASE; HEPTOSE; PROTEIN; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 37449026606     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00969-07     Document Type: Article
Times cited : (61)

References (42)
  • 1
    • 0024517699 scopus 로고
    • Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli
    • Benz, I., and M. A. Schmidt. 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 M. A. Schmidt. 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
    • 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., F. Berthiaume, and M. Mourez. 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
  • 4
    • 37449035041 scopus 로고    scopus 로고
    • 3a.Charbonneau, M.-E., and M. Mourez. 2007. Functional organization of the autotransporter adhesin involved in diffuse adherence. J. Bacteriol. 189: 9020-9029.
    • 3a.Charbonneau, M.-E., and M. Mourez. 2007. Functional organization of the autotransporter adhesin involved in diffuse adherence. J. Bacteriol. 189: 9020-9029.
  • 5
    • 0029965091 scopus 로고    scopus 로고
    • Definition of the full extent of glycosylation of the 45-kilodalton gly coprotein of Mycobacterium tuberculosis
    • Dobos, K. M., K. H. Khoo, K. M. Swiderek, P. J. Brennan, and J. T. Belisle. 1996. Definition of the full extent of glycosylation of the 45-kilodalton gly coprotein 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
  • 6
    • 33646108350 scopus 로고    scopus 로고
    • The role of O-linked and N-linked oligosaccharides on the structure-function of glycoprotein hormones: Development of agonists and antagonists
    • Fares, F. 2006. The role of O-linked and N-linked oligosaccharides on the structure-function of glycoprotein hormones: development of agonists and antagonists. Biochim. Biophys. Acta 1760:560-567.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 560-567
    • Fares, F.1
  • 7
    • 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., J. P. Kamerling, J. F. Vliegenthart, E. Morag, R. Lamed, and E. A. Bayer. 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.P.2    Vliegenthart, J.F.3    Morag, E.4    Lamed, R.5    Bayer, E.A.6
  • 8
    • 0037673430 scopus 로고    scopus 로고
    • Grass, S., A. Z. Buscher, W. E. Swords, M. A. Apicella, S. J. Barenkamp, N. Ozchlewski, and J. W. St. Geme III. 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.
    • Grass, S., A. Z. Buscher, W. E. Swords, M. A. Apicella, S. J. Barenkamp, N. Ozchlewski, and J. W. St. Geme III. 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.
  • 9
    • 33748945006 scopus 로고    scopus 로고
    • Structure of the Escherichia coli heptosyltransferase WaaC: Binary complexes with ADP and ADP-2-deoxy-2-fluoro heptose
    • Grizot, S., M. Salem, V. Vongsouthi, L. Durand, F. Moreau, H. Dohi, S. Vincent, S. Escaich, and A. Ducruix. 2006. Structure of the Escherichia coli heptosyltransferase WaaC: binary complexes with ADP and ADP-2-deoxy-2-fluoro heptose. J. Mol. Biol. 363:383-394.
    • (2006) J. Mol. Biol , vol.363 , pp. 383-394
    • Grizot, S.1    Salem, M.2    Vongsouthi, V.3    Durand, L.4    Moreau, F.5    Dohi, H.6    Vincent, S.7    Escaich, S.8    Ducruix, A.9
  • 11
    • 0041382375 scopus 로고    scopus 로고
    • Prevalence of a gene encoding adhesin involved in diffuse adherence among Escherichia coli isolates in pigs with postweaning diarrhea or edema disease
    • Ha, S. K., C. Choi, and C. Chae. 2003. Prevalence of a gene encoding adhesin involved in diffuse adherence among Escherichia coli isolates in pigs with postweaning diarrhea or edema disease. J. Vet. Diagn. Investig. 15:378-381.
    • (2003) J. Vet. Diagn. Investig , vol.15 , pp. 378-381
    • Ha, S.K.1    Choi, C.2    Chae, C.3
  • 12
    • 3242770758 scopus 로고    scopus 로고
    • Genotypic prevalence of the adhesin involved in diffuse adherence in Escherichia coli isolates in pre-weaned pigs with diarrhoea in Korea
    • Ha, S. K., C. Choi, K. Jung, J. Kim, D. U. Han, Y. Ha, S. D. Lee, S. H. Kim, and C. Chae. 2004. Genotypic prevalence of the adhesin involved in diffuse adherence in Escherichia coli isolates in pre-weaned pigs with diarrhoea in Korea. J. Vet. Med. B Infect. Dis. Vet. Public Health 51:166-168.
    • (2004) J. Vet. Med. B Infect. Dis. Vet. Public Health , vol.51 , pp. 166-168
    • Ha, S.K.1    Choi, C.2    Jung, K.3    Kim, J.4    Han, D.U.5    Ha, Y.6    Lee, S.D.7    Kim, S.H.8    Chae, C.9
  • 13
    • 0028983813 scopus 로고
    • Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman, U., C. Wernstedt, J. Gonez, and C. H. Heldin. 1995. Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal. Biochem. 224:451-455.
    • (1995) Anal. Biochem , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 15
    • 0029896457 scopus 로고    scopus 로고
    • Bacterial glycoproteins: A link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis
    • Herrmann, J. L., P. O'Gaora, A. Gallagher, J. E. Thole, and D. B. Young. 1996. Bacterial glycoproteins: a link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis. EMBO J. 15:3547-3554.
    • (1996) EMBO J , vol.15 , pp. 3547-3554
    • Herrmann, J.L.1    O'Gaora, P.2    Gallagher, A.3    Thole, J.E.4    Young, D.B.5
  • 16
    • 0019877201 scopus 로고
    • A gas-liquid solid phase peptide and protein sequenator
    • Hewick, R. M., M. W. Hunkapiller, L. E. Hood, and W. J. Dreyer. 1981. A gas-liquid solid phase peptide and protein sequenator. J. Biol. Chem. 256: 7990-7997.
    • (1981) J. Biol. Chem , vol.256 , pp. 7990-7997
    • Hewick, R.M.1    Hunkapiller, M.W.2    Hood, L.E.3    Dreyer, W.J.4
  • 17
    • 0032727842 scopus 로고    scopus 로고
    • Effect of N-linked glycosylation on glycopeptide and glycoprotein structure
    • Imperiali, B., and S. E. O'Connor. 1999. Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. Curr. Opin. Chem. Biol. 3:643-649.
    • (1999) Curr. Opin. Chem. Biol , vol.3 , pp. 643-649
    • Imperiali, B.1    O'Connor, S.E.2
  • 18
    • 33745875356 scopus 로고    scopus 로고
    • Self-associating autotransporters, SAATs: Functional and structural similarities
    • Klemm, P., R. M. Vejborg, and O. Sherlock. 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
  • 19
    • 0030455618 scopus 로고    scopus 로고
    • An N-linked high-mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to HeLa cells
    • Kuo, C., N. Takahashi, A. F. Swanson, Y. Ozeki, and S. Hakomori. 1996. An N-linked high-mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to HeLa cells. J. Clin. Investig. 98:2813-2818.
    • (1996) J. Clin. Investig , vol.98 , pp. 2813-2818
    • Kuo, C.1    Takahashi, N.2    Swanson, A.F.3    Ozeki, Y.4    Hakomori, S.5
  • 20
    • 0038148631 scopus 로고    scopus 로고
    • The Escherichia coli AIDA autotransporter adhesin recognizes an integral membrane glycoprotein as receptor
    • Laarmann, S., and M. A. Schmidt. 2003. The Escherichia coli AIDA autotransporter adhesin recognizes an integral membrane glycoprotein as receptor. Microbiology 149:1871-1882.
    • (2003) Microbiology , vol.149 , pp. 1871-1882
    • Laarmann, S.1    Schmidt, M.A.2
  • 21
    • 0032783142 scopus 로고    scopus 로고
    • Identification of a glycoprotein produced by enterotoxigenic Escherichia coli
    • Lindenthal, C., and E. A. Elsinghorst. 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
  • 22
    • 0036428656 scopus 로고    scopus 로고
    • Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins
    • Logan, S. M., J. F. Kelly, P. Thibault, C. P. Ewing, and P. Guerry. 2002. Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins. Mol. Microbiol. 46:587-597.
    • (2002) Mol. Microbiol , vol.46 , pp. 587-597
    • Logan, S.M.1    Kelly, J.F.2    Thibault, P.3    Ewing, C.P.4    Guerry, P.5
  • 23
    • 0037166020 scopus 로고    scopus 로고
    • DNA sequences coding for the F18 fimbriae and AIDA adhesin are localised on the same plasmid in Escherichia coli isolates from piglets
    • Mainil, J. G., E. Jacquemin, P. Pohl, A. Kaeckenbeeck, and I. Benz. 2002. DNA sequences coding for the F18 fimbriae and AIDA adhesin are localised on the same plasmid in Escherichia coli isolates from piglets. Vet. Microbiol. 86:303-311.
    • (2002) Vet. Microbiol , vol.86 , pp. 303-311
    • Mainil, J.G.1    Jacquemin, E.2    Pohl, P.3    Kaeckenbeeck, A.4    Benz, I.5
  • 24
    • 22144495426 scopus 로고    scopus 로고
    • Interactions between folding factors and bacterial outer membrane proteins
    • Mogensen, J. E., and D. E. Otzen. 2005. Interactions between folding factors and bacterial outer membrane proteins. Mol. Microbiol. 57:326-346.
    • (2005) Mol. Microbiol , vol.57 , pp. 326-346
    • Mogensen, J.E.1    Otzen, D.E.2
  • 25
    • 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., I. Benz, and M. A. Schmidt. 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
  • 26
    • 0030695203 scopus 로고    scopus 로고
    • Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli
    • Mourez, M., S. Skouloubris, J. M. Betton, and E. Dassa. 1997. Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli. Mol. Microbiol. 26:821-831.
    • (1997) Mol. Microbiol , vol.26 , pp. 821-831
    • Mourez, M.1    Skouloubris, S.2    Betton, J.M.3    Dassa, E.4
  • 27
    • 0038314479 scopus 로고    scopus 로고
    • Isolation and association of Escherichia coli AIDA-I/STb, rather than EAST1 pathotype, with diarrhea in piglets and antibiotic sensitivity of isolates
    • Ngeleka, M., J. Pritchard, G. Appleyard, D. M. Middleton, and J. M. Fairbrother. 2003. Isolation and association of Escherichia coli AIDA-I/STb, rather than EAST1 pathotype, with diarrhea in piglets and antibiotic sensitivity of isolates. J. Vet. Diagn. Investig. 15:242-252.
    • (2003) J. Vet. Diagn. Investig , vol.15 , pp. 242-252
    • Ngeleka, M.1    Pritchard, J.2    Appleyard, G.3    Middleton, D.M.4    Fairbrother, J.M.5
  • 28
    • 0035161265 scopus 로고    scopus 로고
    • The AIDA autotransporter system is associated will F18 and stx2e in Escherichia coli isolates from pigs diagnosed with edema disease and postweaning diarrhea
    • Niewerth, U., A. Frey, T. Voss, C. Le Bouguenec, G. Baljer. S. Franke, and M. A. Schmidt. 2001. The AIDA autotransporter system is associated will 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    Le Bouguenec, C.4    Baljer, G.5    Franke, S.6    Schmidt, M.A.7
  • 29
    • 0037338681 scopus 로고    scopus 로고
    • A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain
    • Oliver, D. C., G. Huang, E. Nodel, S. Pleasance, and R. C. Fernandez. 2003. A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain. Mol. Microbiol. 47:1367-1383.
    • (2003) Mol. Microbiol , vol.47 , pp. 1367-1383
    • Oliver, D.C.1    Huang, G.2    Nodel, E.3    Pleasance, S.4    Fernandez, R.C.5
  • 30
    • 30544433136 scopus 로고    scopus 로고
    • Methods in enzymology: O-glycosylation of proteins
    • Peter-Katalinic, J. 2005. Methods in enzymology: O-glycosylation of proteins. Methods Enzymol. 405:139-171.
    • (2005) Methods Enzymol , vol.405 , pp. 139-171
    • Peter-Katalinic, J.1
  • 31
    • 0028920231 scopus 로고
    • The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli
    • Raina, S., D. Missiakas, and C. Georgopoulos. 1995. The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli. EMBO J. 14:1043-1055.
    • (1995) EMBO J , vol.14 , pp. 1043-1055
    • Raina, S.1    Missiakas, D.2    Georgopoulos, C.3
  • 32
    • 0032757323 scopus 로고    scopus 로고
    • Deglycosylation of the 45/47-kilodalton antigen complex of Mycobacterium tuberculosis decreases its capacity to elicit in vivo or in vitro cellular immune responses
    • Romain, F., C. Horn, P. Pescher, A. Namane, M. Riviere, G. Puzo, O. Barzu, and G. Marchal. 1999. Deglycosylation of the 45/47-kilodalton antigen complex of Mycobacterium tuberculosis decreases its capacity to elicit in vivo or in vitro cellular immune responses. Infect. Immun. 67:5567-5572.
    • (1999) Infect. Immun , vol.67 , pp. 5567-5572
    • Romain, F.1    Horn, C.2    Pescher, P.3    Namane, A.4    Riviere, M.5    Puzo, G.6    Barzu, O.7    Marchal, G.8
  • 33
    • 33744746602 scopus 로고    scopus 로고
    • The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation
    • Rutherford, N., M. E. Charbonneau, F. Berthiaume, J. M. Betton, and M. Mourez. 2006. The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation. J. Bacteriol. 188:4111-4116.
    • (2006) J. Bacteriol , vol.188 , pp. 4111-4116
    • Rutherford, N.1    Charbonneau, M.E.2    Berthiaume, F.3    Betton, J.M.4    Mourez, M.5
  • 34
    • 0037560879 scopus 로고    scopus 로고
    • Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori
    • Schirm, M., E. C. Soo, A. J. Aubry, J. Austin, P. Thibault, and S. M. Logan. 2003. Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori. Mol. Microbiol. 48:1579-1592.
    • (2003) Mol. Microbiol , vol.48 , pp. 1579-1592
    • Schirm, M.1    Soo, E.C.2    Aubry, A.J.3    Austin, J.4    Thibault, P.5    Logan, S.M.6
  • 35
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: Glycoproteins in bacterial pathogens
    • Schmidt, M. A., L. W. Riley, and I. Benz. 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
  • 36
    • 33644769605 scopus 로고    scopus 로고
    • Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein
    • Sherlock, O., U. Dobrindt, J. B. Jensen, R. Munk Vejborg, and P. Klemm. 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
  • 37
    • 9244250348 scopus 로고    scopus 로고
    • Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: Cell aggregation and biofilm formation
    • Sherlock, O., M. A. Schembri, A. Reisner, and P. Klemm. 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
  • 38
    • 0029846536 scopus 로고    scopus 로고
    • Processing of the AIDA-I precursor: Removal of AIDAc and evidence for the outer membrane anchoring as a beta-barrel structure
    • Suhr, M., I. Benz, and M. A. Schmidt. 1996. Processing of the AIDA-I precursor: removal of AIDAc and evidence for the outer membrane anchoring as a beta-barrel structure. Mol. Microbiol. 22:31-42.
    • (1996) Mol. Microbiol , vol.22 , pp. 31-42
    • Suhr, M.1    Benz, I.2    Schmidt, M.A.3
  • 39
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski, C. M., and B. W. Wren. 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
  • 40
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski, C. M., R. Yao, C. P. Ewing, T. J. Trust, and P. Guerry. 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.P.3    Trust, T.J.4    Guerry, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.