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Volumn 77, Issue 9, 2009, Pages 3533-3541

Amino acid changes in elongation factor Tu of Mycoplasma pneumoniae and Mycoplasma genitalium influence fibronectin binding

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR TU; ESSENTIAL AMINO ACID; FIBRONECTIN; RECOMBINANT PROTEIN;

EID: 69049083513     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00081-09     Document Type: Article
Times cited : (32)

References (57)
  • 1
    • 0033638335 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A: EEF1Balpha
    • Andersen, G. R., L. Pedersen, L. Valente, I. Chatterjee, T. G. Kinzy, M. Kjeldgaard, and J. Nyborg. 2000. Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A: eEF1Balpha. Mol. Cell 6:1261-1266.
    • (2000) Mol. Cell , vol.6 , pp. 1261-1266
    • Andersen, G.R.1    Pedersen, L.2    Valente, L.3    Chatterjee, I.4    Kinzy, T.G.5    Kjeldgaard, M.6    Nyborg, J.7
  • 2
    • 0034708342 scopus 로고    scopus 로고
    • High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP
    • Andersen, G. R., S. Thirup, L. L. Spremulli, and J. Nyborg. 2000. High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP. J. Mol. Biol. 297:421-436.
    • (2000) J. Mol. Biol , vol.297 , pp. 421-436
    • Andersen, G.R.1    Thirup, S.2    Spremulli, L.L.3    Nyborg, J.4
  • 3
    • 46449125693 scopus 로고    scopus 로고
    • The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin
    • Balasubramanian, S., T. R. Kannan, and J. B. Baseman. 2008. The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin. Infect. Immun. 76:3116-3123.
    • (2008) Infect. Immun , vol.76 , pp. 3116-3123
    • Balasubramanian, S.1    Kannan, T.R.2    Baseman, J.B.3
  • 5
    • 0020466617 scopus 로고
    • Molecular basis for cytadsorption of Mycoplasma pneumoniae
    • Baseman, J. B., R. M. Cole, D. C. Krause, and D. K. Leith. 1982. Molecular basis for cytadsorption of Mycoplasma pneumoniae. J. Bacteriol. 151:1514-1522.
    • (1982) J. Bacteriol , vol.151 , pp. 1514-1522
    • Baseman, J.B.1    Cole, R.M.2    Krause, D.C.3    Leith, D.K.4
  • 6
    • 0023757349 scopus 로고
    • Isolation and characterization of Mycoplasma genitalium strains from the human respiratory tract
    • Baseman, J. B., S. F. Dallo, J. G. Tully, and D. L. Rose. 1988. Isolation and characterization of Mycoplasma genitalium strains from the human respiratory tract. J. Clin. Microbiol. 26:2266-2269.
    • (1988) J. Clin. Microbiol , vol.26 , pp. 2266-2269
    • Baseman, J.B.1    Dallo, S.F.2    Tully, J.G.3    Rose, D.L.4
  • 7
    • 0032512429 scopus 로고    scopus 로고
    • Functional role of the noncatalytic domains of elongation factor Tu in the interactions with ligands
    • Cetin, R., P. H. Anborgh, R. H. Cool, and A. Parmeggiani. 1998. Functional role of the noncatalytic domains of elongation factor Tu in the interactions with ligands. Biochemistry 37:486-495.
    • (1998) Biochemistry , vol.37 , pp. 486-495
    • Cetin, R.1    Anborgh, P.H.2    Cool, R.H.3    Parmeggiani, A.4
  • 9
    • 0033679277 scopus 로고    scopus 로고
    • Intracellular DNA replication and long-term survival of pathogenic mycoplasmas
    • Dallo, S. F., and J. B. Baseman. 2000. Intracellular DNA replication and long-term survival of pathogenic mycoplasmas. Microb. Pathog. 29:301-309.
    • (2000) Microb. Pathog , vol.29 , pp. 301-309
    • Dallo, S.F.1    Baseman, J.B.2
  • 10
    • 0025610222 scopus 로고
    • Characterization of the gene for a 30-kilodalton adhesion-related protein of Mycoplasma pneumoniae
    • Dallo, S. F., A. Chavoya, and J. B. Baseman. 1990. Characterization of the gene for a 30-kilodalton adhesion-related protein of Mycoplasma pneumoniae. Infect. Immun. 58:4163-4165.
    • (1990) Infect. Immun , vol.58 , pp. 4163-4165
    • Dallo, S.F.1    Chavoya, A.2    Baseman, J.B.3
  • 11
    • 0036434714 scopus 로고    scopus 로고
    • Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae
    • Dallo, S. F., T. R. Kannan, M. W. Blaylock, and J. B. Baseman. 2002. Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae. Mol. Microbiol. 46:1041-1051.
    • (2002) Mol. Microbiol , vol.46 , pp. 1041-1051
    • Dallo, S.F.1    Kannan, T.R.2    Blaylock, M.W.3    Baseman, J.B.4
  • 12
    • 0024382180 scopus 로고
    • Common themes in microbial pathogenicity
    • Finlay, B. B., and S. Falkow. 1989. Common themes in microbial pathogenicity. Microbiol. Rev. 53:210-230.
    • (1989) Microbiol. Rev , vol.53 , pp. 210-230
    • Finlay, B.B.1    Falkow, S.2
  • 13
    • 0030045743 scopus 로고    scopus 로고
    • Adherence, fibronectin binding, and induction of cytoskeleton reorganization in cultured human cells by Mycoplasma penetrans
    • Giron, J. A., M. Lange, and J. B. Baseman. 1996. Adherence, fibronectin binding, and induction of cytoskeleton reorganization in cultured human cells by Mycoplasma penetrans. Infect. Immun. 64:197-208.
    • (1996) Infect. Immun , vol.64 , pp. 197-208
    • Giron, J.A.1    Lange, M.2    Baseman, J.B.3
  • 15
  • 16
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    • Granato, D., G. E. Bergonzelli, R. D. Pridmore, L. Marvin, M. Rouvet, and I. E. Corthesy-Theulaz. 2004. Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins. Infect. Immun. 72:2160-2169.
    • (2004) Infect. Immun , vol.72 , pp. 2160-2169
    • Granato, D.1    Bergonzelli, G.E.2    Pridmore, R.D.3    Marvin, L.4    Rouvet, M.5    Corthesy-Theulaz, I.E.6
  • 17
    • 0018409165 scopus 로고
    • Isolation of mutants of Mycoplasma pneumoniae defective in hemadsorption
    • Hansen, E. J., R. M. Wilson, and J. B. Baseman. 1979. Isolation of mutants of Mycoplasma pneumoniae defective in hemadsorption. Infect. Immun. 23:903-906.
    • (1979) Infect. Immun , vol.23 , pp. 903-906
    • Hansen, E.J.1    Wilson, R.M.2    Baseman, J.B.3
  • 18
    • 0019476544 scopus 로고
    • Characterization of hemadsorption-negative mutants of Mycoplasma pneumoniae
    • Hansen, E. J., R. M. Wilson, W. A. Clyde, Jr., and J. B. Baseman. 1981. Characterization of hemadsorption-negative mutants of Mycoplasma pneumoniae. Infect. Immun. 32:127-136.
    • (1981) Infect. Immun , vol.32 , pp. 127-136
    • Hansen, E.J.1    Wilson, R.M.2    Clyde Jr., W.A.3    Baseman, J.B.4
  • 19
    • 0032173602 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae and Mycoplasma genitalium: A comparison of two closely related bacterial species
    • Herrmann, R., and B. Reiner. 1998. Mycoplasma pneumoniae and Mycoplasma genitalium: a comparison of two closely related bacterial species. Curr. Opin. Microbiol. 1:572-579.
    • (1998) Curr. Opin. Microbiol , vol.1 , pp. 572-579
    • Herrmann, R.1    Reiner, B.2
  • 21
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 22
    • 0002859240 scopus 로고
    • Interactions of pathogenic microorganisms with fibronectin
    • D. E. Mosher ed, Academic Press, Inc, New York, NY
    • Höök, M., L. M. Switalski, T. Wadström, and M. Lindberg. 1989. Interactions of pathogenic microorganisms with fibronectin. In D. E. Mosher (ed.), Fibronectin. Academic Press, Inc., New York, NY.
    • (1989) Fibronectin
    • Höök, M.1    Switalski, L.M.2    Wadström, T.3    Lindberg, M.4
  • 24
    • 0023902667 scopus 로고
    • Nucleotide sequence of the P1 attachment-protein gene of Mycoplasma pneumoniae
    • Inamine, J. M., T. P. Denny, S. Loechel, U. Schaper, C. H. Huang, K. F. Bott, and P. C. Hu. 1988. Nucleotide sequence of the P1 attachment-protein gene of Mycoplasma pneumoniae. Gene 64:217-229.
    • (1988) Gene , vol.64 , pp. 217-229
    • Inamine, J.M.1    Denny, T.P.2    Loechel, S.3    Schaper, U.4    Huang, C.H.5    Bott, K.F.6    Hu, P.C.7
  • 25
    • 0024468731 scopus 로고
    • Nucleotide sequence of the MgPa (mgp) operon of Mycoplasma genitalium and comparison to the P1 (mpp) operon of Mycoplasma pneumoniae
    • Inamine, J. M., S. Loechel, A. M. Collier, M. F. Barile, and P. C. Hu. 1989. Nucleotide sequence of the MgPa (mgp) operon of Mycoplasma genitalium and comparison to the P1 (mpp) operon of Mycoplasma pneumoniae. Gene 82:259-267.
    • (1989) Gene , vol.82 , pp. 259-267
    • Inamine, J.M.1    Loechel, S.2    Collier, A.M.3    Barile, M.F.4    Hu, P.C.5
  • 26
    • 0026130399 scopus 로고
    • Comparison of host responses after intranasal infection of guinea-pigs with Mycoplasma genitalium or with Mycoplasma pneumoniae
    • Jacobs, E., T. Watter, H. E. Schaefer, and W. Bredt. 1991. Comparison of host responses after intranasal infection of guinea-pigs with Mycoplasma genitalium or with Mycoplasma pneumoniae. Microb. Pathog. 10:221-229.
    • (1991) Microb. Pathog , vol.10 , pp. 221-229
    • Jacobs, E.1    Watter, T.2    Schaefer, H.E.3    Bredt, W.4
  • 27
    • 0842329803 scopus 로고    scopus 로고
    • Mycoplasma genitalium: The aetiological agent of urethritis and other sexually transmitted diseases
    • Jensen, J. S. 2004. Mycoplasma genitalium: the aetiological agent of urethritis and other sexually transmitted diseases. J. Eur. Acad. Dermatol. Venereol. 18:1-11.
    • (2004) J. Eur. Acad. Dermatol. Venereol , vol.18 , pp. 1-11
    • Jensen, J.S.1
  • 28
    • 0029882910 scopus 로고    scopus 로고
    • Phylogeny based on elongation factor Tu reflects the phenotypic features of mycoplasmas better than that based on 16S rRNA
    • Kamla, V., B. Henrich, and U. Hadding. 1996. Phylogeny based on elongation factor Tu reflects the phenotypic features of mycoplasmas better than that based on 16S rRNA. Gene 171:83-87.
    • (1996) Gene , vol.171 , pp. 83-87
    • Kamla, V.1    Henrich, B.2    Hadding, U.3
  • 29
    • 33646271152 scopus 로고    scopus 로고
    • ADP-ribosylating and vacuolating cytotoxin of Mycoplasma pneumoniae represents unique virulence determinant among bacterial pathogens
    • Kannan, T. R., and J. B. Baseman. 2006. ADP-ribosylating and vacuolating cytotoxin of Mycoplasma pneumoniae represents unique virulence determinant among bacterial pathogens. Proc. Natl. Acad. Sci. USA 103:6724-6729.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6724-6729
    • Kannan, T.R.1    Baseman, J.B.2
  • 33
    • 36448991500 scopus 로고    scopus 로고
    • Larkin, M. A, G. Blackshields, N. P. Brown, R. Chenna, P. A. McGettigan, H. McWilliam, F. Valentin, I. M. Wallace, A. Wilm, R. Lopez, J. D. Thompson, T. J. Gibson, and D. G. Higgins. 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23:2847-2948
    • Larkin, M. A., G. Blackshields, N. P. Brown, R. Chenna, P. A. McGettigan, H. McWilliam, F. Valentin, I. M. Wallace, A. Wilm, R. Lopez, J. D. Thompson, T. J. Gibson, and D. G. Higgins. 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23:2847-2948.
  • 34
    • 33644767983 scopus 로고    scopus 로고
    • Identification of fibronectin-binding proteins in Mycoplasma gallisepticum strain R
    • May, M., L. Papazisi, T. S. Gorton, and S. J. Geary. 2006. Identification of fibronectin-binding proteins in Mycoplasma gallisepticum strain R. Infect. Immun. 74:1777-1785.
    • (2006) Infect. Immun , vol.74 , pp. 1777-1785
    • May, M.1    Papazisi, L.2    Gorton, T.S.3    Geary, S.J.4
  • 35
    • 0023072984 scopus 로고
    • Shared epitopes between Mycoplasma pneumoniae major adhesin protein P1 and a 140-kilodalton protein of Mycoplasma genitalium
    • Morrison-Plummer, J., A. Lazzell, and J. B. Baseman. 1987. Shared epitopes between Mycoplasma pneumoniae major adhesin protein P1 and a 140-kilodalton protein of Mycoplasma genitalium. Infect. Immun. 55:49-56.
    • (1987) Infect. Immun , vol.55 , pp. 49-56
    • Morrison-Plummer, J.1    Lazzell, A.2    Baseman, J.B.3
  • 37
    • 32344436283 scopus 로고    scopus 로고
    • Proximal region of the gene encoding cytadherence-related protein permits molecular typing of Mycoplasma genitalium clinical strains by PCR-restriction fragment length polymorphism
    • Musatovova, O., C. Herrera, and J. B. Baseman. 2006. Proximal region of the gene encoding cytadherence-related protein permits molecular typing of Mycoplasma genitalium clinical strains by PCR-restriction fragment length polymorphism. J. Clin. Microbiol. 44:598-603.
    • (2006) J. Clin. Microbiol , vol.44 , pp. 598-603
    • Musatovova, O.1    Herrera, C.2    Baseman, J.B.3
  • 38
    • 0029789824 scopus 로고    scopus 로고
    • A minimal gene set for cellular life derived by comparison of complete bacterial genomes
    • Mushegian, A. R., and E. V. Koonin. 1996. A minimal gene set for cellular life derived by comparison of complete bacterial genomes. Proc. Natl. Acad. Sci. USA 93:10268-10273.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10268-10273
    • Mushegian, A.R.1    Koonin, E.V.2
  • 39
    • 0021246975 scopus 로고
    • Fibronectin receptors on Trypanosoma cruzi trypomastigotes and their biological function
    • Ouaissi, M. A., D. Afchain, A. Capron, and J. A. Grimaud. 1984. Fibronectin receptors on Trypanosoma cruzi trypomastigotes and their biological function. Nature 308:380-382.
    • (1984) Nature , vol.308 , pp. 380-382
    • Ouaissi, M.A.1    Afchain, D.2    Capron, A.3    Grimaud, J.A.4
  • 40
    • 33744951325 scopus 로고    scopus 로고
    • Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu
    • Parmeggiani, A., I. M. Krab, S. Okamura, R. C. Nielsen, J. Nyborg, and P. Nissen. 2006. Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu. Biochemistry 45:6846-6857.
    • (2006) Biochemistry , vol.45 , pp. 6846-6857
    • Parmeggiani, A.1    Krab, I.M.2    Okamura, S.3    Nielsen, R.C.4    Nyborg, J.5    Nissen, P.6
  • 42
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., and T. L. Blundell. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 45
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Söding, J. 2005. Protein homology detection by HMM-HMM comparison. Bioinformatics 21:951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Söding, J.1
  • 46
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding, J., A. Biegert, and A. N. Lupas. 2005. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33:W244-W248.
    • (2005) Nucleic Acids Res , vol.33
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 47
    • 34547912457 scopus 로고    scopus 로고
    • Mapping phosphoproteins in Mycoplasma genitalium and Mycoplasma pneumoniae
    • Su, H. C., C. A. Hutchison III, and M. C. Giddings. 2007. Mapping phosphoproteins in Mycoplasma genitalium and Mycoplasma pneumoniae. BMC Microbiol. 7:63.
    • (2007) BMC Microbiol , vol.7 , pp. 63
    • Su, H.C.1    Hutchison III, C.A.2    Giddings, M.C.3
  • 48
    • 0032964297 scopus 로고    scopus 로고
    • BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences
    • Tatusova, T. A., and T. L. Madden. 1999. BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences. FEMS Microbiol. Lett. 174:247-250.
    • (1999) FEMS Microbiol. Lett , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 49
    • 0021945840 scopus 로고
    • Fibronectin mediates Treponema pallidum cytadherence through recognition of fibronectin cell-binding domain
    • Thomas, D. D., J. B. Baseman, and J. F. Alderete. 1985. Fibronectin mediates Treponema pallidum cytadherence through recognition of fibronectin cell-binding domain. J. Exp. Med. 161:514-525.
    • (1985) J. Exp. Med , vol.161 , pp. 514-525
    • Thomas, D.D.1    Baseman, J.B.2    Alderete, J.F.3
  • 51
    • 0019473954 scopus 로고
    • A newly discovered mycoplasma in the human urogenital tract
    • Tully, J. G., D. Taylor-Robinson, R. M. Cole, and D. L. Rose. 1981. A newly discovered mycoplasma in the human urogenital tract. Lancet 13:1288-1291.
    • (1981) Lancet , vol.13 , pp. 1288-1291
    • Tully, J.G.1    Taylor-Robinson, D.2    Cole, R.M.3    Rose, D.L.4
  • 53
    • 0035477797 scopus 로고    scopus 로고
    • The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchange
    • Vitagliano, L., M. Masullo, F. Sica, A. Zagari, and V. Bocchini. 2001. The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchange. EMBO J. 20:5305-5311.
    • (2001) EMBO J , vol.20 , pp. 5305-5311
    • Vitagliano, L.1    Masullo, M.2    Sica, F.3    Zagari, A.4    Bocchini, V.5
  • 54
    • 5644300391 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae and its role as a human pathogen
    • Waites, K. B., and D. F. Talkington. 2004. Mycoplasma pneumoniae and its role as a human pathogen. Clin. Microbiol. Rev. 17:697-728.
    • (2004) Clin. Microbiol. Rev , vol.17 , pp. 697-728
    • Waites, K.B.1    Talkington, D.F.2
  • 55
    • 0021807753 scopus 로고
    • In vitro parasite-monocyte interactions in human leishmaniasis: Possible role of fibronectin in parasite attachment
    • Wyler, D. J., J. P. Sypek, and J. A. McDonald. 1985. In vitro parasite-monocyte interactions in human leishmaniasis: possible role of fibronectin in parasite attachment. Infect. Immun. 49:305-311.
    • (1985) Infect. Immun , vol.49 , pp. 305-311
    • Wyler, D.J.1    Sypek, J.P.2    McDonald, J.A.3
  • 56
    • 0019250261 scopus 로고
    • Structure and function of the fibronectins
    • Yamada, K. M., L. H. Hahn, and K. Olden. 1980. Structure and function of the fibronectins. Prog. Clin. Biol. Res. 41:797-819.
    • (1980) Prog. Clin. Biol. Res , vol.41 , pp. 797-819
    • Yamada, K.M.1    Hahn, L.H.2    Olden, K.3
  • 57
    • 1842425660 scopus 로고    scopus 로고
    • Internalization and intracellular survival of Mycoplasma pneumoniae by nonphagocytic cells
    • Yavlovich, A., M. Tarshis, and S. Rottem. 2004. Internalization and intracellular survival of Mycoplasma pneumoniae by nonphagocytic cells. FEMS Microbiol. Lett. 233:241-246.
    • (2004) FEMS Microbiol. Lett , vol.233 , pp. 241-246
    • Yavlovich, A.1    Tarshis, M.2    Rottem, S.3


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