메뉴 건너뛰기




Volumn 77, Issue 7, 2009, Pages 2703-2711

Glyceraldehyde-3-phosphate dehydrogenase is a surface-associated, fibronectin-binding protein of Trichomonas vaginalis

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; FIBRONECTIN; FIBRONECTIN BINDING PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; IRON; MONOCLONAL ANTIBODY; PLASMINOGEN; RECOMBINANT ENZYME;

EID: 67650032436     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00157-09     Document Type: Article
Times cited : (84)

References (47)
  • 1
    • 0020671996 scopus 로고
    • Antigen analysis of several pathogenic stains of Trichomonas vaginalis
    • Alderete, J. F. 1983. Antigen analysis of several pathogenic stains of Trichomonas vaginalis. Infect. Immun. 39:1041-1047.
    • (1983) Infect. Immun , vol.39 , pp. 1041-1047
    • Alderete, J.F.1
  • 2
    • 0032765417 scopus 로고    scopus 로고
    • Iron modulates phenotypic variation and phosphorylation of P270 in double-stranded RNA virus-infected Trichomonas vaginalis
    • Alderete, J. F. 1999. Iron modulates phenotypic variation and phosphorylation of P270 in double-stranded RNA virus-infected Trichomonas vaginalis. Infect. Immun. 67:4298-4302.
    • (1999) Infect. Immun , vol.67 , pp. 4298-4302
    • Alderete, J.F.1
  • 3
    • 0022535810 scopus 로고
    • Monoclonal antibody to a major glycoprotein immunogen mediates differential complement-independent lysis of Trichomonas vaginalis
    • Alderete, J. F., and L. Kasmala. 1986. Monoclonal antibody to a major glycoprotein immunogen mediates differential complement-independent lysis of Trichomonas vaginalis. Infect. Immun. 53:697-699.
    • (1986) Infect. Immun , vol.53 , pp. 697-699
    • Alderete, J.F.1    Kasmala, L.2
  • 4
    • 0028827837 scopus 로고
    • Iron mediates Trichomonas vaginalis resistance to complement lysis
    • Alderete, J. F., D. Provenzano, and M. W. Lehker. 1995. Iron mediates Trichomonas vaginalis resistance to complement lysis. Microb. Pathog. 19:93-103.
    • (1995) Microb. Pathog , vol.19 , pp. 93-103
    • Alderete, J.F.1    Provenzano, D.2    Lehker, M.W.3
  • 5
    • 0029151459 scopus 로고
    • Cloning and molecular characterization of two genes encoding adhesion proteins involved in Trichomonas vaginalis cytoadherence
    • Alderete, J. F., J. L. O'Brien, R. Arroyo, J. A. Engbring, O. Musatovova, O. Lopez, C. Lauriano, and J. Nguyen. 1995. Cloning and molecular characterization of two genes encoding adhesion proteins involved in Trichomonas vaginalis cytoadherence. Mol. Microbiol. 17:69-83.
    • (1995) Mol. Microbiol , vol.17 , pp. 69-83
    • Alderete, J.F.1    O'Brien, J.L.2    Arroyo, R.3    Engbring, J.A.4    Musatovova, O.5    Lopez, O.6    Lauriano, C.7    Nguyen, J.8
  • 6
    • 1642328128 scopus 로고    scopus 로고
    • Heme-iron increases levels of AP65-mediated adherence by Trichomonas vaginalis
    • Alderete, J. F., J. Nguyen, V. Mundodi, and M. W. Lehker. 2004. Heme-iron increases levels of AP65-mediated adherence by Trichomonas vaginalis. Microb. Pathog. 36:263-271.
    • (2004) Microb. Pathog , vol.36 , pp. 263-271
    • Alderete, J.F.1    Nguyen, J.2    Mundodi, V.3    Lehker, M.W.4
  • 7
    • 0022516743 scopus 로고
    • Phenotypic variation and diversity among Trichomonas vaginalis and correlation of phenotype with contact-dependent host cell cytotoxicity
    • Alderete, J. F., L. Kasmala, E. C. Metcalfe, and G. E. Garza. 1986. Phenotypic variation and diversity among Trichomonas vaginalis and correlation of phenotype with contact-dependent host cell cytotoxicity. Infect. Immun. 53:285-293.
    • (1986) Infect. Immun , vol.53 , pp. 285-293
    • Alderete, J.F.1    Kasmala, L.2    Metcalfe, E.C.3    Garza, G.E.4
  • 8
    • 0036756764 scopus 로고    scopus 로고
    • The complex fibronectin-Trichomonas vaginalis interactions and trichomoniasis
    • Alderete, J. F., M. Benchimol, M. W. Lehker, and M. Crouch. 2002. The complex fibronectin-Trichomonas vaginalis interactions and trichomoniasis. Parasitol. Int. 51:285-292.
    • (2002) Parasitol. Int , vol.51 , pp. 285-292
    • Alderete, J.F.1    Benchimol, M.2    Lehker, M.W.3    Crouch, M.4
  • 9
    • 0027454897 scopus 로고
    • Signalling of Trichomonas vaginalis for amoeboid transformation and adhesin synthesis follows cytoadherence
    • Arroyo, R., A. Gonzalez-Robles, A. Martinez-Palomo, and J. F. Alderete. 1993. Signalling of Trichomonas vaginalis for amoeboid transformation and adhesin synthesis follows cytoadherence. Mol. Microbiol. 7:299-309.
    • (1993) Mol. Microbiol , vol.7 , pp. 299-309
    • Arroyo, R.1    Gonzalez-Robles, A.2    Martinez-Palomo, A.3    Alderete, J.F.4
  • 10
    • 0026533051 scopus 로고
    • Molecular basis of host epithelial cell recognition by Trichomonas vaginalis
    • Arroyo, R., J. Engbring, and J. F. Alderete. 1992. Molecular basis of host epithelial cell recognition by Trichomonas vaginalis. Mol. Microbiol. 6:853-862.
    • (1992) Mol. Microbiol , vol.6 , pp. 853-862
    • Arroyo, R.1    Engbring, J.2    Alderete, J.F.3
  • 11
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann, S., M. Rohde, and S. Hammerschmidt. 2004. Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infect. Immun. 72:2416-2419.
    • (2004) Infect. Immun , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 12
    • 0034931519 scopus 로고    scopus 로고
    • Alpha-enolase of Streptococcus pneumoniae is a plasmin(ogen)- binding protein displayed on the bacterial cell surface
    • Bergmann, S., M. Rohde, G. S. Chhatwal, and S. Hammerschmidt. 2001. Alpha-enolase of Streptococcus pneumoniae is a plasmin(ogen)- binding protein displayed on the bacterial cell surface. Mol. Microbiol. 40:1273-1287.
    • (2001) Mol. Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 13
    • 0036568587 scopus 로고    scopus 로고
    • Anchorless adhesins and invasins of gram-positive bacteria: A new class of virulence factors
    • Chhatwal, G. S. 2002. Anchorless adhesins and invasins of gram-positive bacteria: a new class of virulence factors. Trends Microbiol. 10:205-208.
    • (2002) Trends Microbiol , vol.10 , pp. 205-208
    • Chhatwal, G.S.1
  • 14
    • 0032866063 scopus 로고    scopus 로고
    • Trichomonas vaginalis interactions with fibronectin and laminin
    • Crouch, M. L., and J. F. Alderete. 1999. Trichomonas vaginalis interactions with fibronectin and laminin. Microbiology 145:2835-2845.
    • (1999) Microbiology , vol.145 , pp. 2835-2845
    • Crouch, M.L.1    Alderete, J.F.2
  • 15
    • 0034866226 scopus 로고    scopus 로고
    • Binding of fibronectin by Trichomonas vaginalis is influenced by iron and calcium
    • Crouch, M. L., M. Benchimol, and J. F. Alderete. 2001. Binding of fibronectin by Trichomonas vaginalis is influenced by iron and calcium. Microb. Pathog. 31:131-144.
    • (2001) Microb. Pathog , vol.31 , pp. 131-144
    • Crouch, M.L.1    Benchimol, M.2    Alderete, J.F.3
  • 16
    • 0035024050 scopus 로고    scopus 로고
    • Trichomonas vaginalis has two fibronectin-like iron-regulated genes
    • Crouch, M. L., and J. F. Alderete. 2001. Trichomonas vaginalis has two fibronectin-like iron-regulated genes. Arch. Med. Res. 32:102-107.
    • (2001) Arch. Med. Res , vol.32 , pp. 102-107
    • Crouch, M.L.1    Alderete, J.F.2
  • 17
    • 34249332380 scopus 로고    scopus 로고
    • Role of secreted glyceraldehyde-3- phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: Interaction of the extracellular enzyme with human plasminogen and fibrinogen
    • Egea, L., L. Aguilera, R. Giménez, M. A. Sorolla, J. Aguilar, J. Badía, and L. Baldoma. 2007. Role of secreted glyceraldehyde-3- phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: interaction of the extracellular enzyme with human plasminogen and fibrinogen. Int. J. Biochem. Cell Biol. 39:1190-1203.
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 1190-1203
    • Egea, L.1    Aguilera, L.2    Giménez, R.3    Sorolla, M.A.4    Aguilar, J.5    Badía, J.6    Baldoma, L.7
  • 18
    • 0031768784 scopus 로고    scopus 로고
    • Characterization of Trichomonas vaginalis AP33 adhesin and cell surface interactive domains
    • Engbring, J. A., and J. F. Alderete. 1998. Characterization of Trichomonas vaginalis AP33 adhesin and cell surface interactive domains. Microbiology 144:3011-3018.
    • (1998) Microbiology , vol.144 , pp. 3011-3018
    • Engbring, J.A.1    Alderete, J.F.2
  • 19
    • 38849141960 scopus 로고    scopus 로고
    • Characterization of the Trichomonas vaginalis surface-associated AP65 and binding domain interacting with trichomonads and host cells
    • Garcia, A. F., and J. F. Alderete. 2007. Characterization of the Trichomonas vaginalis surface-associated AP65 and binding domain interacting with trichomonads and host cells. BMC Microbiol. 25:116.
    • (2007) BMC Microbiol , vol.25 , pp. 116
    • Garcia, A.F.1    Alderete, J.F.2
  • 20
    • 17644422236 scopus 로고    scopus 로고
    • Trichomonas vaginalis polyamine metabolism is linked to host cell adherence and cytotoxicity
    • Garcia, A. F., M. Benchimol, and J. F. Alderete. 2005. Trichomonas vaginalis polyamine metabolism is linked to host cell adherence and cytotoxicity. Infect. Immun. 73:2602-2610.
    • (2005) Infect. Immun , vol.73 , pp. 2602-2610
    • Garcia, A.F.1    Benchimol, M.2    Alderete, J.F.3
  • 21
    • 0037338699 scopus 로고    scopus 로고
    • Iron and contact with host cells induce expression of adhesins on surface of Trichomonas vaginalis
    • García, A. F., T. H. Chang, M. Benchimol, D. J. Klumpp, M. W. Lehker, and J. F. Alderete. 2003. Iron and contact with host cells induce expression of adhesins on surface of Trichomonas vaginalis. Mol. Microbiol. 47:1207-1224.
    • (2003) Mol. Microbiol , vol.47 , pp. 1207-1224
    • García, A.F.1    Chang, T.H.2    Benchimol, M.3    Klumpp, D.J.4    Lehker, M.W.5    Alderete, J.F.6
  • 22
    • 0031896903 scopus 로고    scopus 로고
    • The cell wall-associated glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is also a fibronectin and laminin binding protein
    • Gozalbo, D., I. Gil-Navarro, I. Azorín, J. Renau-Piqueras, J. P. Martínez, and M. L. Gil. 1998. The cell wall-associated glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is also a fibronectin and laminin binding protein. Infect. Immun. 66:2052-2059.
    • (1998) Infect. Immun , vol.66 , pp. 2052-2059
    • Gozalbo, D.1    Gil-Navarro, I.2    Azorín, I.3    Renau-Piqueras, J.4    Martínez, J.P.5    Gil, M.L.6
  • 23
    • 0032767986 scopus 로고    scopus 로고
    • Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells
    • Joh, D., E. R. Wann, B. Kreikemeyer, P. Speziale, and M. Hook. 1999. Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells. Matrix Biol. 18:211-223.
    • (1999) Matrix Biol , vol.18 , pp. 211-223
    • Joh, D.1    Wann, E.R.2    Kreikemeyer, B.3    Speziale, P.4    Hook, M.5
  • 24
    • 0043030106 scopus 로고    scopus 로고
    • Binding of Candida albicans enolase to plasmin(ogen) results in enhanced invasion of human brain microvascular endothelial cells
    • Jong, A. Y., S. H. Chen, M. F. Stins, K. S. Kim, T. L. Tuan, and S. H. Huang. 2003. Binding of Candida albicans enolase to plasmin(ogen) results in enhanced invasion of human brain microvascular endothelial cells. J. Med. Microbiol. 52:615-622.
    • (2003) J. Med. Microbiol , vol.52 , pp. 615-622
    • Jong, A.Y.1    Chen, S.H.2    Stins, M.F.3    Kim, K.S.4    Tuan, T.L.5    Huang, S.H.6
  • 26
    • 25444509858 scopus 로고    scopus 로고
    • Heterologous expression in Tritrichomonas foetus of functional Trichomonas vaginalis AP65 adhesin
    • Kucknoor, A. S., V. Mundodi, and J. F. Alderete. 2005. Heterologous expression in Tritrichomonas foetus of functional Trichomonas vaginalis AP65 adhesin. BMC Mol. Biol. 4:5.
    • (2005) BMC Mol. Biol , vol.4 , pp. 5
    • Kucknoor, A.S.1    Mundodi, V.2    Alderete, J.F.3
  • 27
    • 34848847880 scopus 로고    scopus 로고
    • The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65
    • Kucknoor, A. S., V. Mundodi, and J. F. Alderete. 2007. The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65. Cell. Microbiol. 11:2586-2597.
    • (2007) Cell. Microbiol , vol.11 , pp. 2586-2597
    • Kucknoor, A.S.1    Mundodi, V.2    Alderete, J.F.3
  • 28
    • 0032825036 scopus 로고    scopus 로고
    • Trichomonad invasion of the mucous layer requires adhesins, mucinases, and motility
    • Lehker, M. W., and D. Sweeney. 1999. Trichomonad invasion of the mucous layer requires adhesins, mucinases, and motility. Sex. Transm. Infect. 75:231-238.
    • (1999) Sex. Transm. Infect , vol.75 , pp. 231-238
    • Lehker, M.W.1    Sweeney, D.2
  • 29
    • 0025766755 scopus 로고
    • The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis
    • Lehker, M. W., R. Arroyo, and J. F. Alderete. 1991. The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis. J. Exp. Med. 174:311-318.
    • (1991) J. Exp. Med , vol.174 , pp. 311-318
    • Lehker, M.W.1    Arroyo, R.2    Alderete, J.F.3
  • 31
    • 4544381795 scopus 로고    scopus 로고
    • Characterization of binding of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase to Porphyromonas gingivalis major fimbriae
    • Maeda, K., H. Nagata, M. Kuboniwa, K. Kataoka, N. Nishida, M. Tanaka, and S. Shizukuishi. 2004. Characterization of binding of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase to Porphyromonas gingivalis major fimbriae. Infect. Immun. 72:5475-5477.
    • (2004) Infect. Immun , vol.72 , pp. 5475-5477
    • Maeda, K.1    Nagata, H.2    Kuboniwa, M.3    Kataoka, K.4    Nishida, N.5    Tanaka, M.6    Shizukuishi, S.7
  • 32
    • 0027423316 scopus 로고
    • A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis
    • Markos, A., A. Miretsky, and M. Müller. 1993. A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis. J. Mol. Evol. 37:631-643.
    • (1993) J. Mol. Evol , vol.37 , pp. 631-643
    • Markos, A.1    Miretsky, A.2    Müller, M.3
  • 34
    • 0030903802 scopus 로고    scopus 로고
    • The fibronectin binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells
    • Molinari, G., S. R. Talay, P. Valentin-Weigand, M. Rhode, and G. S. Chhatwal. 1997. The fibronectin binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells. Infect. Immun. 65:1357-1363.
    • (1997) Infect. Immun , vol.65 , pp. 1357-1363
    • Molinari, G.1    Talay, S.R.2    Valentin-Weigand, P.3    Rhode, M.4    Chhatwal, G.S.5
  • 35
    • 39149123184 scopus 로고    scopus 로고
    • Immunogenic and plasminogen-binding surface-associated α-enolase of Trichomonas vaginalis
    • Mundodi, V., A. S. Kucknoor, and J. F. Alderete. 2008. Immunogenic and plasminogen-binding surface-associated α-enolase of Trichomonas vaginalis. Infect. Immun. 76:523-531.
    • (2008) Infect. Immun , vol.76 , pp. 523-531
    • Mundodi, V.1    Kucknoor, A.S.2    Alderete, J.F.3
  • 36
    • 34447648775 scopus 로고    scopus 로고
    • Antisense RNA decreases AP33 gene expression and cytoadherence by T. vaginalis
    • Mundodi, V., A. S. Kucknoor, and J. F. Alderete. 2007. Antisense RNA decreases AP33 gene expression and cytoadherence by T. vaginalis. BMC Microbiol. 3:64.
    • (2007) BMC Microbiol , vol.3 , pp. 64
    • Mundodi, V.1    Kucknoor, A.S.2    Alderete, J.F.3
  • 37
    • 4344563422 scopus 로고    scopus 로고
    • Silencing the ap65 gene reduces adherence to vaginal epithelial cells by Trichomonas vaginalis
    • Mundodi, V., A. S. Kucknoor, D. J. Klumpp, T. H. Chang, and J. F. Alderete. 2004. Silencing the ap65 gene reduces adherence to vaginal epithelial cells by Trichomonas vaginalis. Mol. Microbiol. 53:1099-1108.
    • (2004) Mol. Microbiol , vol.53 , pp. 1099-1108
    • Mundodi, V.1    Kucknoor, A.S.2    Klumpp, D.J.3    Chang, T.H.4    Alderete, J.F.5
  • 38
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate dehydrogenase with multiple binding activity
    • Pancholi, V., and V. A. Fischetti. 1992. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate dehydrogenase with multiple binding activity. J. Exp. Med. 176:415-426.
    • (1992) J. Exp. Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 39
    • 0032486286 scopus 로고    scopus 로고
    • α-Enolase, a novel strong plasmin-(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi, V., and V. A. Fischetti. 1998. α-Enolase, a novel strong plasmin-(ogen) binding protein on the surface of pathogenic streptococci. J. Biol. Chem. 273:14503-14515.
    • (1998) J. Biol. Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 40
    • 58749083705 scopus 로고    scopus 로고
    • Peterman, T. A., L. H. Tian, C. A. Metcalf, C. K. Malotte, S. M. Paul, and J. M. Douglas, Jr. 2009. Persistent, undetected Trichomonas vaginalis infections? Clin. Infect. Dis. 48:259-260.
    • Peterman, T. A., L. H. Tian, C. A. Metcalf, C. K. Malotte, S. M. Paul, and J. M. Douglas, Jr. 2009. Persistent, undetected Trichomonas vaginalis infections? Clin. Infect. Dis. 48:259-260.
  • 41
    • 0035052105 scopus 로고    scopus 로고
    • Effect of iron on the virulence of Trichomonas vaginalis
    • Ryu, J. S., H. K. Choi, D. Y. Min, S. E. Ha, and M. H. Ahn. 2001. Effect of iron on the virulence of Trichomonas vaginalis. J. Parasitol. 87:457-460.
    • (2001) J. Parasitol , vol.87 , pp. 457-460
    • Ryu, J.S.1    Choi, H.K.2    Min, D.Y.3    Ha, S.E.4    Ahn, M.H.5
  • 42
    • 0029691198 scopus 로고    scopus 로고
    • Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells
    • Sirover, M. A. 1996. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. Life Sci. 58:2271-2277.
    • (1996) Life Sci , vol.58 , pp. 2271-2277
    • Sirover, M.A.1
  • 44
    • 0037085285 scopus 로고    scopus 로고
    • Characterization of an ironresponsive promoter in the protozoan pathogen Trichomonas vaginalis
    • Tsai, C. D., H. W. Liu, and J. H. Tai. 2002. Characterization of an ironresponsive promoter in the protozoan pathogen Trichomonas vaginalis. J. Biol. Chem. 277:5153-5162.
    • (2002) J. Biol. Chem , vol.277 , pp. 5153-5162
    • Tsai, C.D.1    Liu, H.W.2    Tai, J.H.3
  • 46
    • 0034003078 scopus 로고    scopus 로고
    • Gynecological infections as risk determinants of subsequent cervical neoplasia
    • Vikki, M., E. Pukkala, P. Nieminen, and M. Hakama. 2000. Gynecological infections as risk determinants of subsequent cervical neoplasia. Acta Oncol. 39:71-75.
    • (2000) Acta Oncol , vol.39 , pp. 71-75
    • Vikki, M.1    Pukkala, E.2    Nieminen, P.3    Hakama, M.4
  • 47
    • 0003514452 scopus 로고    scopus 로고
    • Global prevalence and incidence of selected curable sexually transmitted infections. Overview and estimates. WHO, Geneva, Switzerland
    • World Health Organization. 2001. Global prevalence and incidence of selected curable sexually transmitted infections. Overview and estimates. WHO, Geneva, Switzerland.
    • (2001) World Health Organization


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.