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Volumn 3, Issue 2, 2012, Pages

Characterization of cleavage events in the multifunctional cilium adhesin Mhp684 (P146) reveals a mechanism by which Mycoplasma hyopneumoniae regulates surface topography

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; PLASMINOGEN; PROTEOME;

EID: 84860528192     PISSN: None     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00282-11     Document Type: Article
Times cited : (57)

References (55)
  • 2
    • 0025772456 scopus 로고
    • The Vlp system of Mycoplasma hyorhinis: Combinatorial expression of distinct size variant lipoproteins generating high-frequency surface antigenic variation
    • Rosengarten R, Wise KS. 1991. The Vlp system of Mycoplasma hyorhinis: combinatorial expression of distinct size variant lipoproteins generating high-frequency surface antigenic variation. J. Bacteriol. 173:4782-4793.
    • (1991) J. Bacteriol , vol.173 , pp. 4782-4793
    • Rosengarten, R.1    Wise, K.S.2
  • 3
    • 0033953803 scopus 로고    scopus 로고
    • Gene families encoding phaseand size-variable surface lipoproteins of Mycoplasma hyorhinis
    • Citti C, Watson-McKown R, Droesse M, Wise KS. 2000. Gene families encoding phaseand size-variable surface lipoproteins of Mycoplasma hyorhinis. J. Bacteriol. 182:1356-1363.
    • (2000) J. Bacteriol , vol.182 , pp. 1356-1363
    • Citti, C.1    Watson-McKown, R.2    Droesse, M.3    Wise, K.S.4
  • 4
    • 0030965130 scopus 로고    scopus 로고
    • Mycoplasma synoviae has two distinct phase-variable major membrane antigens, one of which is a putative hemagglutinin
    • Noormohammadi AH, et al. 1997. Mycoplasma synoviae has two distinct phase-variable major membrane antigens, one of which is a putative hemagglutinin. Infect. Immun. 65:2542-2547.
    • (1997) Infect Immun , vol.65 , pp. 2542-2547
    • Noormohammadi, A.H.1
  • 5
    • 79551493695 scopus 로고    scopus 로고
    • Complete genome sequence of Mycoplasma hyopneumoniae strain 168
    • Liu W, et al. 2011. Complete genome sequence of Mycoplasma hyopneumoniae strain 168. J. Bacteriol. 193:1016-1017.
    • (2011) J. Bacteriol , vol.193 , pp. 1016-1017
    • Liu, W.1
  • 6
    • 6044238249 scopus 로고    scopus 로고
    • The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of swine mycoplasmosis
    • Minion FC, et al. 2004. The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of swine mycoplasmosis. J. Bacteriol. 186: 7123-7133.
    • (2004) J. Bacteriol , vol.186 , pp. 7123-7133
    • Minion, F.C.1
  • 7
    • 23644457964 scopus 로고    scopus 로고
    • Swine and poultry pathogens: The complete genome sequences of two strains of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae
    • Vasconcelos AT, et al. 2005. Swine and poultry pathogens: the complete genome sequences of two strains of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae. J. Bacteriol. 187:5568-5577.
    • (2005) J. Bacteriol , vol.187 , pp. 5568-5577
    • Vasconcelos, A.T.1
  • 8
    • 0001621314 scopus 로고
    • Investigating the transmission of Mycoplasma hyopneumoniae in a swine herd with enzootic pneumonia
    • Clark LK, et al. 1991. Investigating the transmission of Mycoplasma hyopneumoniae in a swine herd with enzootic pneumonia. Vet. Med. 86: 543-550.
    • (1991) Vet Med , vol.86 , pp. 543-550
    • Clark, L.K.1
  • 9
    • 2442484041 scopus 로고    scopus 로고
    • Efficacy of vaccines against bacterial diseases in swine: What can we expect?
    • Haesebrouck F, et al. 2004. Efficacy of vaccines against bacterial diseases in swine: what can we expect? Vet. Microbiol. 100:255-268.
    • (2004) Vet. Microbiol , vol.100 , pp. 255-268
    • Haesebrouck, F.1
  • 10
    • 80055087421 scopus 로고    scopus 로고
    • Transmission of swine pathogens: Different means, different needs
    • Desrosiers R. 2011. Transmission of swine pathogens: different means, different needs. Anim. Health Res. Rev. 12:1-13.
    • (2011) Anim. Health Res. Rev , vol.12 , pp. 1-13
    • Desrosiers, R.1
  • 11
    • 0019989764 scopus 로고
    • Interaction of Mycoplasma hyopneumoniae with the porcine respiratory epithelium as observed by electron microscopy
    • Tajima M, Yagihashi T. 1982. Interaction of Mycoplasma hyopneumoniae with the porcine respiratory epithelium as observed by electron microscopy. Infect. Immun. 37:1162-1169.
    • (1982) Infect. Immun , vol.37 , pp. 1162-1169
    • Tajima, M.1    Yagihashi, T.2
  • 12
    • 0028090196 scopus 로고
    • Ciliostasis and loss of cilia induced by Mycoplasma hyopneumoniae in porcine tracheal organ cultures
    • DeBey MC, Ross RF. 1994. Ciliostasis and loss of cilia induced by Mycoplasma hyopneumoniae in porcine tracheal organ cultures. Infect. Immun. 62:5312-5318.
    • (1994) Infect. Immun , vol.62 , pp. 5312-5318
    • Debey, M.C.1    Ross, R.F.2
  • 13
    • 0028280640 scopus 로고
    • Microtiter plate adherence assay and receptor analogs for Mycoplasma hyopneumoniae
    • Zhang Q, Young TF, Ross RF. 1994. Microtiter plate adherence assay and receptor analogs for Mycoplasma hyopneumoniae. Infect. Immun. 62: 1616-1622.
    • (1994) Infect. Immun , vol.62 , pp. 1616-1622
    • Zhang, Q.1    Young, T.F.2    Ross, R.F.3
  • 14
    • 0029128604 scopus 로고
    • Glycosaminoglycans in porcine lung: An ultrastructural study using cupromeronic blue
    • Erlinger R. 1995. Glycosaminoglycans in porcine lung: an ultrastructural study using cupromeronic blue. Cell Tissue Res. 281:473-483.
    • (1995) Cell Tissue Res , vol.281 , pp. 473-483
    • Erlinger, R.1
  • 15
    • 0033867661 scopus 로고    scopus 로고
    • Interaction of Bordetella pertussis with human respiratory mucosa in vitro
    • Soane MC, et al. 2000. Interaction of Bordetella pertussis with human respiratory mucosa in vitro. Respir. Med. 94:791-799.
    • (2000) Respir. Med , vol.94 , pp. 791-799
    • Soane, M.C.1
  • 16
    • 19744370931 scopus 로고    scopus 로고
    • Bordetella bronchiseptica adherence to cilia is mediated by multiple adhesin factors and blocked by surfactant protein A
    • Edwards JA, Groathouse NA, Boitano S. 2005. Bordetella bronchiseptica adherence to cilia is mediated by multiple adhesin factors and blocked by surfactant protein A. Infect. Immun. 73:3618-3626.
    • (2005) Infect. Immun , vol.73 , pp. 3618-3626
    • Edwards, J.A.1    Groathouse, N.A.2    Boitano, S.3
  • 17
    • 79551552340 scopus 로고    scopus 로고
    • Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1
    • Kuespert K, Roth A, Hauck CR. 2011. Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1. PLoS One 6:e14609.
    • (2011) PLoS One , vol.6 , pp. 14609
    • Kuespert, K.1    Roth, A.2    Hauck, C.R.3
  • 18
    • 77953076127 scopus 로고    scopus 로고
    • Proteoglycans in host-pathogen interactions: Molecular mechanisms and therapeutic implications
    • Bartlett AH, Park PW. 2010. Proteoglycans in host-pathogen interactions: molecular mechanisms and therapeutic implications. Expert Rev. Mol. Med. 12:e5.
    • (2010) Expert Rev. Mol. Med , vol.e5 , pp. 12
    • Bartlett, A.H.1    Park, P.W.2
  • 19
    • 33645835366 scopus 로고    scopus 로고
    • P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: Defined domains of P159 bind heparin and promote adherence to eukaryote cells
    • Burnett TA, et al. 2006. P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells. Mol. Microbiol. 60:669-686.
    • (2006) Mol. Microbiol , vol.60 , pp. 669-686
    • Burnett, T.A.1
  • 21
    • 58449115242 scopus 로고    scopus 로고
    • Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae
    • Wilton J, et al. 2009. Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae. Mol. Microbiol. 71:566-582.
    • (2009) Mol. Microbiol , vol.71 , pp. 566-582
    • Wilton, J.1
  • 22
    • 82355164186 scopus 로고    scopus 로고
    • Sequence TTKF 2 QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae
    • Bogema DR, et al. 2011. Sequence TTKF 2 QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae. J. Biol. Chem. 286: 41217-41229.
    • (2011) J. Biol. Chem , vol.286 , pp. 41217-41229
    • Bogema, D.R.1
  • 23
    • 0028928377 scopus 로고
    • Identification and characterization of a Mycoplasma hyopneumoniae adhesin
    • Zhang Q, Young TF, Ross RF. 1995. Identification and characterization of a Mycoplasma hyopneumoniae adhesin. Infect. Immun. 63:1013-1019.
    • (1995) Infect. Immun , vol.63 , pp. 1013-1019
    • Zhang, Q.1    Young, T.F.2    Ross, R.F.3
  • 24
    • 78649343270 scopus 로고    scopus 로고
    • Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Mycoplasma hyopneumoniae bind heparin, fibronectin and porcine cilia
    • Deutscher AT, et al. 2010. Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Mycoplasma hyopneumoniae bind heparin, fibronectin and porcine cilia. Mol. Microbiol. 78:444-458.
    • (2010) Mol. Microbiol , vol.78 , pp. 444-458
    • Deutscher, A.T.1
  • 25
    • 77958599627 scopus 로고    scopus 로고
    • A processed multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia
    • Seymour LM, et al. 2010. A processed multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia. J. Biol. Chem. 285:33971-33978.
    • (2010) J. Biol. Chem , vol.285 , pp. 33971-33978
    • Seymour, L.M.1
  • 26
    • 79953219413 scopus 로고    scopus 로고
    • Mhp107 is a member of the multifunctional adhesin family of Mycoplasma hyopneumoniae
    • Seymour LM, et al. 2011. Mhp107 is a member of the multifunctional adhesin family of Mycoplasma hyopneumoniae. J. Biol. Chem. 286: 10097-10104.
    • (2011) J. Biol. Chem , vol.286 , pp. 10097-10104
    • Seymour, L.M.1
  • 27
    • 83655163689 scopus 로고    scopus 로고
    • Mhp182 (P102) binds fibronectin and contributes to the recruitment of plasmin(ogen) to the Mycoplasma hyopneumoniae cell surface
    • Seymour LM, et al. 2012. Mhp182 (P102) binds fibronectin and contributes to the recruitment of plasmin(ogen) to the Mycoplasma hyopneumoniae cell surface. Cell. Microbiol. 14:81-94.
    • (2012) Cell. Microbiol , vol.14 , pp. 81-94
    • Seymour, L.M.1
  • 28
    • 33847306478 scopus 로고    scopus 로고
    • Proteomic survey of the pathogenic Mycoplasma hyopneumoniae strain 7448 and identification of novel posttranslationally modified and antigenic proteins
    • Pinto PM, et al. 2007. Proteomic survey of the pathogenic Mycoplasma hyopneumoniae strain 7448 and identification of novel posttranslationally modified and antigenic proteins. Vet. Microbiol. 121: 83-93.
    • (2007) Vet Microbiol , vol.121 , pp. 83-93
    • Pinto, P.M.1
  • 29
    • 76649129580 scopus 로고    scopus 로고
    • Comparative proteomic analysis of pathogenic and non-pathogenic strains from the swine pathogen Mycoplasma hyopneumoniae
    • Pinto PM, Klein CS, Zaha A, Ferreira HB. 2009. Comparative proteomic analysis of pathogenic and non-pathogenic strains from the swine pathogen Mycoplasma hyopneumoniae. Proteome Sci. 7:45.
    • (2009) Proteome Sci , vol.7 , pp. 45
    • Pinto, P.M.1    Klein, C.S.2    Zaha, A.3    Ferreira, H.B.4
  • 30
    • 27744499733 scopus 로고    scopus 로고
    • In vivo expression analysis of the P97 and P102 paralog families of Mycoplasma hyopneumoniae
    • Adams C, Pitzer J, Minion FC. 2005. In vivo expression analysis of the P97 and P102 paralog families of Mycoplasma hyopneumoniae. Infect. Immun. 73:7784-7787.
    • (2005) Infect Immun , vol.73 , pp. 7784-7787
    • Adams, C.1    Pitzer, J.2    Minion, F.C.3
  • 31
    • 29644440331 scopus 로고    scopus 로고
    • Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin
    • Jenkins C, et al. 2006. Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin. Infect. Immun. 74:481-487.
    • (2006) Infect. Immun , vol.74 , pp. 481-487
    • Jenkins, C.1
  • 32
    • 33745156051 scopus 로고    scopus 로고
    • Comparison of molecular techniques for the typing of Mycoplasma hyopneumoniae isolates
    • Stakenborg T, et al. 2006. Comparison of molecular techniques for the typing of Mycoplasma hyopneumoniae isolates. J. Microbiol. Methods 66: 263-275.
    • (2006) J. Microbiol. Methods , vol.66 , pp. 263-275
    • Stakenborg, T.1
  • 33
    • 33747133970 scopus 로고    scopus 로고
    • Variable number of tandem amino acid repeats in adhesion-related CDS products in Mycoplasma hyopneumoniae strains
    • de Castro LA, et al. 2006. Variable number of tandem amino acid repeats in adhesion-related CDS products in Mycoplasma hyopneumoniae strains. Vet. Microbiol. 116:258-269.
    • (2006) Vet. Microbiol , vol.116 , pp. 258-269
    • de Castro, L.A.1
  • 34
    • 0037261861 scopus 로고    scopus 로고
    • Characterization of LppS, an adhesin of Mycoplasma conjunctivae
    • Belloy L, Vilei EM, Giacometti M, Frey J. 2003. Characterization of LppS, an adhesin of Mycoplasma conjunctivae. Microbiology 149:185-193.
    • (2003) Microbiology , vol.149 , pp. 185-193
    • Belloy, L.1    Vilei, E.M.2    Giacometti, M.3    Frey, J.4
  • 35
    • 32144456009 scopus 로고    scopus 로고
    • Paircoil2: Improved prediction of coiled coils from sequence
    • McDonnell AV, Jiang T, Keating AE, Berger B. 2006. Paircoil2: improved prediction of coiled coils from sequence. Bioinformatics 22: 356-358.
    • (2006) Bioinformatics , vol.22 , pp. 356-358
    • McDonnell, A.V.1    Jiang, T.2    Keating, A.E.3    Berger, B.4
  • 36
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Van Dyke M, Stock J. 1991. Predicting coiled coils from protein sequences. Science 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    van Dyke, M.2    Stock, J.3
  • 37
    • 30344485673 scopus 로고    scopus 로고
    • Exploiting heterogeneous sequence properties improves prediction of protein disorder
    • Obradovic Z, et al. 2005. Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins 61(Suppl. 7):176-182.
    • (2005) Proteins , vol.61 , Issue.7 SUPPL. , pp. 176-182
    • Obradovic, Z.1
  • 39
    • 84857880464 scopus 로고    scopus 로고
    • Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs
    • Deutscher AT, et al. 2012. Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs. J. Proteome Res. 11:1924-1936.
    • (2012) J. Proteome Res , vol.11 , pp. 1924-1936
    • Deutscher, A.T.1
  • 40
    • 33846929584 scopus 로고    scopus 로고
    • The plasminogen-binding group A streptococcal M protein-related protein Prp binds plasminogen via arginine and histidine residues
    • Sanderson-Smith ML, Dowton M, Ranson M, Walker MJ. 2007. The plasminogen-binding group A streptococcal M protein-related protein Prp binds plasminogen via arginine and histidine residues. J. Bacteriol. 189:1435-1440.
    • (2007) J. Bacteriol , vol.189 , pp. 1435-1440
    • Sanderson-Smith, M.L.1    Dowton, M.2    Ranson, M.3    Walker, M.J.4
  • 41
    • 0027475969 scopus 로고
    • The kinetics of plasminogen activation by thrombin-cleaved pro-urokinase and promotion of its activity by fibrin fragment E-2 and by tissue plasminogen activator
    • Liu JN, Gurewich V. 1993. The kinetics of plasminogen activation by thrombin-cleaved pro-urokinase and promotion of its activity by fibrin fragment E-2 and by tissue plasminogen activator. Blood 81:980-987.
    • (1993) Blood , vol.81 , pp. 980-987
    • Liu, J.N.1    Gurewich, V.2
  • 42
    • 0026333563 scopus 로고
    • Ligand specificity of human plasminogen kringle 4
    • Rejante MR, Byeon IJ, Llinás M. 1991. Ligand specificity of human plasminogen kringle 4. Biochemistry 30:11081-11092.
    • (1991) Biochemistry , vol.30 , pp. 11081-11092
    • Rejante, M.R.1    Byeon, I.J.2    Llinás, M.3
  • 43
    • 67650529851 scopus 로고    scopus 로고
    • Defining the structural basis of human plasminogen binding by streptococcal surface enolase
    • Cork AJ, et al. 2009. Defining the structural basis of human plasminogen binding by streptococcal surface enolase. J. Biol. Chem. 284:17129-17137.
    • (2009) J. Biol. Chem , vol.284 , pp. 17129-17137
    • Cork, A.J.1
  • 44
    • 53149141067 scopus 로고    scopus 로고
    • Real-time PCR assays to address genetic diversity among strains of Mycoplasma hyopneumoniae
    • Strait EL, et al. 2008. Real-time PCR assays to address genetic diversity among strains of Mycoplasma hyopneumoniae. J. Clin. Microbiol. 46: 2491-2498.
    • (2008) J. Clin. Microbiol , vol.46 , pp. 2491-2498
    • Strait, E.L.1
  • 45
    • 0031057336 scopus 로고    scopus 로고
    • Identification of novel species-specific antigens of Mycoplasma hyopneumoniae by preparative SDS-PAGE ELISA profiling
    • Scarman AL, et al. 1997. Identification of novel species-specific antigens of Mycoplasma hyopneumoniae by preparative SDS-PAGE ELISA profiling. Microbiology 143(Part 2):663-673.
    • (1997) Microbiology , vol.143 , Issue.2 PART. , pp. 663-673
    • Scarman, A.L.1
  • 46
    • 76749149598 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the Campylobacter jejuni adherence factor CadF reveals post-translational processing that removes immunogenicity while retaining fibronectin binding
    • Scott NE, et al. 2010. Mass spectrometric characterization of the Campylobacter jejuni adherence factor CadF reveals post-translational processing that removes immunogenicity while retaining fibronectin binding. Proteomics 10:277-288.
    • (2010) Proteomics , vol.10 , pp. 277-288
    • Scott, N.E.1
  • 47
    • 38149142479 scopus 로고    scopus 로고
    • Identification of membrane-associated proteins from Campylobacter jejuni strains using complementary proteomics technologies
    • Cordwell SJ, et al. 2008. Identification of membrane-associated proteins from Campylobacter jejuni strains using complementary proteomics technologies. Proteomics 8:122-139.
    • (2008) Proteomics , vol.8 , pp. 122-139
    • Cordwell, S.J.1
  • 51
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification and analysis tools on the ExPASy server
    • Walker JM (ed), Humana Press, New York, NY
    • Gasteiger E, et al. 2005. Protein identification and analysis tools on the ExPASy server, p 571-607. In Walker JM (ed), The proteomics protocols handbook. Humana Press, New York, NY.
    • (2005) The Proteomics Protocols Handbook , pp. 571-607
    • Gasteiger, E.1
  • 52
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL. 2001. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:567-580.
    • (2001) J. Mol. Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 53
    • 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
  • 54
    • 70350029185 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the surfaceassociated 42 kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni
    • Scott NE, et al. 2009. Mass spectrometric characterization of the surfaceassociated 42 kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni. J. Proteome Res. 8:4654-4664.
    • (2009) J. Proteome Res , vol.8 , pp. 4654-4664
    • Scott, N.E.1
  • 55
    • 84984933232 scopus 로고    scopus 로고
    • Immunoblot affinity purification
    • Nature Publishing Group
    • Nature Publishing Group. 2005. Immunoblot affinity purification. Nat. Methods 2:797-798
    • (2005) Nat. Methods , vol.2 , pp. 797-798


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