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Volumn 1804, Issue 11, 2010, Pages 2111-2120

Surface localized and extracellular Glyceraldehyde-3-phosphate dehydrogenase of Bacillus anthracis is a plasminogen binding protein

Author keywords

Affinity; Bacillus anthracis; GAPDH; GAPDH isoform; Invasion; Plasminogen; Surface

Indexed keywords

BINDING PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; ISOENZYME; ISOPROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PLASMINOGEN; PLASMINOGEN BINDING PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 77956649845     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.08.004     Document Type: Article
Times cited : (68)

References (32)
  • 1
    • 18044377210 scopus 로고    scopus 로고
    • Presence of fibronectin binding protein gene prtF2 in invasive group A streptococci in tropical Australia is associated with increased internalization efficiency
    • Gorton D., Norton R., Layton R., Smith H., Ketheesan N. Presence of fibronectin binding protein gene prtF2 in invasive group A streptococci in tropical Australia is associated with increased internalization efficiency. Microbes Infect. 2005, 7:421-426.
    • (2005) Microbes Infect. , vol.7 , pp. 421-426
    • Gorton, D.1    Norton, R.2    Layton, R.3    Smith, H.4    Ketheesan, N.5
  • 2
    • 0032831831 scopus 로고    scopus 로고
    • Recognition of fibronectin by Penicillium marneffei conidia via a sialic acid-dependent process and its relationship to the interaction between conidia and laminin
    • Hamilton A.J., Jeavons L., Youngchim S., Vanittanakom N. Recognition of fibronectin by Penicillium marneffei conidia via a sialic acid-dependent process and its relationship to the interaction between conidia and laminin. Infect. Immun. 1999, 67:5200-5205.
    • (1999) Infect. Immun. , vol.67 , pp. 5200-5205
    • Hamilton, A.J.1    Jeavons, L.2    Youngchim, S.3    Vanittanakom, N.4
  • 3
    • 29644437769 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein involved in fungal adhesion to extracellular matrix proteins and interaction with cells
    • Barbosa M.S., Báo S.N., Andreotti P.F., de Faria F.P., Felipe M.S., dos Santos Feitosa L., Mendes-Giannini M.J., Soares C.M. Glyceraldehyde-3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein involved in fungal adhesion to extracellular matrix proteins and interaction with cells. Infect. Immun. 2006, 74:382-389.
    • (2006) Infect. Immun. , vol.74 , pp. 382-389
    • Barbosa, M.S.1    Báo, S.N.2    Andreotti, P.F.3    de Faria, F.P.4    Felipe, M.S.5    dos Santos Feitosa, L.6    Mendes-Giannini, M.J.7    Soares, C.M.8
  • 4
    • 0347753321 scopus 로고    scopus 로고
    • Housekeeping enzymes as virulence factors for pathogens
    • Pancholi V., Chhatwal G.S. Housekeeping enzymes as virulence factors for pathogens. Int. J. Med. Microbiol. 2003, 293:391-401.
    • (2003) Int. J. Med. Microbiol. , vol.293 , pp. 391-401
    • Pancholi, V.1    Chhatwal, G.S.2
  • 5
    • 0029691198 scopus 로고    scopus 로고
    • Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells
    • Sirover M. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. Life Sci. 1996, 58:2271-2272.
    • (1996) Life Sci. , vol.58 , pp. 2271-2272
    • Sirover, M.1
  • 6
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover M.A. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta 1999, 1432:159-184.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 7
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: its role in diseases
    • Pancholi V. Multifunctional alpha-enolase: its role in diseases. Cell. Mol. Life Sci. 2001, 58:902-920.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 8
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi V., Fischetti V.A. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J. Exp. Med. 1992, 176:415-426.
    • (1992) J. Exp. Med. , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 10
    • 52449135569 scopus 로고    scopus 로고
    • Alpha-Enolase binds to human plasminogen on the surface of Bacillus anthracis
    • Agarwal S., Kulshreshtha P., Mukku D.B., Bhatnagar R. alpha-Enolase binds to human plasminogen on the surface of Bacillus anthracis. Biochim. Biophys. Acta 2008, 1784:986-994.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 986-994
    • Agarwal, S.1    Kulshreshtha, P.2    Mukku, D.B.3    Bhatnagar, R.4
  • 12
    • 33748760583 scopus 로고    scopus 로고
    • Proteomic profiling and identification of immunodominant spore antigens of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis
    • DelVecchio D.V.G., Connolly J.P., Alefantis T.G., Walz A., Quan M.A., Patra G. Proteomic profiling and identification of immunodominant spore antigens of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis. Appl. Environ. Microbiol. 2006, 72:6355-6363.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 6355-6363
    • DelVecchio, D.V.G.1    Connolly, J.P.2    Alefantis, T.G.3    Walz, A.4    Quan, M.A.5    Patra, G.6
  • 13
    • 0013770850 scopus 로고
    • The isolation and specific activity of rabbit muscle glyceraldehyde phosphate dehydrogenase
    • Ferdinand W. The isolation and specific activity of rabbit muscle glyceraldehyde phosphate dehydrogenase. Biochem. J. 1964, 92:578-585.
    • (1964) Biochem. J. , vol.92 , pp. 578-585
    • Ferdinand, W.1
  • 14
    • 44449137547 scopus 로고    scopus 로고
    • Isolation and solubilization of cellular membrane proteins from bacteria
    • Zuobi-Hasona K., Brady L.J. Isolation and solubilization of cellular membrane proteins from bacteria. Methods Mol. Biol. 2008, 425:287-293.
    • (2008) Methods Mol. Biol. , vol.425 , pp. 287-293
    • Zuobi-Hasona, K.1    Brady, L.J.2
  • 16
    • 0002381906 scopus 로고
    • Separation and purification of NAD- and NADP-linked GAPDH from higher plants
    • Elsevier/North Holland, Amsterdam, M.E. Edelman, R.B. Hallick, N.H. Chua (Eds.)
    • Cerff R. Separation and purification of NAD- and NADP-linked GAPDH from higher plants. Methods in Chloroplast Molecular Biology 1982, 683-694. Elsevier/North Holland, Amsterdam. M.E. Edelman, R.B. Hallick, N.H. Chua (Eds.).
    • (1982) Methods in Chloroplast Molecular Biology , pp. 683-694
    • Cerff, R.1
  • 17
    • 0024698882 scopus 로고
    • Cloning and sequence analysis of cDNAs encoding the cytosolic precursors of subunits GapA and GapB of chloroplast glyceraldehyde-3-phosphate dehydrogenase from pea and spinach
    • Brinkmann H., Cerff R., Salomon M., Soll J. Cloning and sequence analysis of cDNAs encoding the cytosolic precursors of subunits GapA and GapB of chloroplast glyceraldehyde-3-phosphate dehydrogenase from pea and spinach. Plant Mol. Biol. 1989, 13:81-94.
    • (1989) Plant Mol. Biol. , vol.13 , pp. 81-94
    • Brinkmann, H.1    Cerff, R.2    Salomon, M.3    Soll, J.4
  • 18
    • 0027729858 scopus 로고
    • ATP-driven transhydrogenation and ionization of water in a reconstituted glyceraldehyde-3-phosphate dehydrogenase (phosphorylating and non-phosphorylating) model system
    • Serrano A., Maetos M.I., Losada M. ATP-driven transhydrogenation and ionization of water in a reconstituted glyceraldehyde-3-phosphate dehydrogenase (phosphorylating and non-phosphorylating) model system. Biochem. Biophys. Res. Commun. 1993, 197:1348-1356.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1348-1356
    • Serrano, A.1    Maetos, M.I.2    Losada, M.3
  • 19
    • 0034640272 scopus 로고    scopus 로고
    • Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium
    • Fillinger S., Boschi-Muller S., Azza S., Dervyn E., Branlant G., Aymerich S. Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J. Biol. Chem. 2000, 275:14031-14037.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14031-14037
    • Fillinger, S.1    Boschi-Muller, S.2    Azza, S.3    Dervyn, E.4    Branlant, G.5    Aymerich, S.6
  • 20
    • 0037150030 scopus 로고    scopus 로고
    • A phosphate-stimulated NAD(P)+-dependent glyceraldehyde-3-phosphate dehydrogenase in Bacillus cereus
    • Iddar A., Serrano A., Soukri A. A phosphate-stimulated NAD(P)+-dependent glyceraldehyde-3-phosphate dehydrogenase in Bacillus cereus. FEMS Microbiol. Lett. 2002, 211:29-35.
    • (2002) FEMS Microbiol. Lett. , vol.211 , pp. 29-35
    • Iddar, A.1    Serrano, A.2    Soukri, A.3
  • 21
    • 31144469460 scopus 로고    scopus 로고
    • Widespread occurrence of non- phosphorylating glyceraldehyde-3-phosphate dehydrogenase among gram-positive bacteria
    • Iddar A., Valverde F., Assobhei O., Serrano A., Soukri A. Widespread occurrence of non- phosphorylating glyceraldehyde-3-phosphate dehydrogenase among gram-positive bacteria. Int. Microbiol. 2005, 8:251-258.
    • (2005) Int. Microbiol. , vol.8 , pp. 251-258
    • Iddar, A.1    Valverde, F.2    Assobhei, O.3    Serrano, A.4    Soukri, A.5
  • 22
    • 0015757283 scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase of Bacillus stearothermophilus
    • Suzuki K., Imahori K. Glyceraldehyde 3-phosphate dehydrogenase of Bacillus stearothermophilus. J. Biochem. 1973, 74:955-970.
    • (1973) J. Biochem. , vol.74 , pp. 955-970
    • Suzuki, K.1    Imahori, K.2
  • 23
    • 0019490781 scopus 로고
    • Concentration of plasminogen and antiplasmin in plasma and serum
    • Cederholm-williams S. Concentration of plasminogen and antiplasmin in plasma and serum. J. Clin. Pathol. 1981, 34:979-981.
    • (1981) J. Clin. Pathol. , vol.34 , pp. 979-981
    • Cederholm-williams, S.1
  • 24
    • 0032486286 scopus 로고    scopus 로고
    • α-Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi V., Fischetti V.A. α-Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J. Biol. Chem. 1998, 273:14503-14515.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 25
    • 0031661935 scopus 로고    scopus 로고
    • R. Lottenberg., Site-directed mutagenesis of streptococcal plasmin receptor protein (Plr) identifies the C-terminal Lys334 as essential for plasmin binding, but mutation of the plr gene does not reduce plasmin binding to group A streptococci
    • Winramt S.B. R. Lottenberg., Site-directed mutagenesis of streptococcal plasmin receptor protein (Plr) identifies the C-terminal Lys334 as essential for plasmin binding, but mutation of the plr gene does not reduce plasmin binding to group A streptococci. Microbiology 1998, 144:2025-2035.
    • (1998) Microbiology , vol.144 , pp. 2025-2035
    • Winramt, S.B.1
  • 26
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann S., Rohde M., Hammerschmidt S. Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infect. Immun. 2004, 72:2416-2419.
    • (2004) Infect. Immun. , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 27
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae
    • Bergmann S., Wild D., Diekmann O., Frank R., Bracht D., Chhatwal G.S., Hammerschmidt S. Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol. Microbiol. 2003, 49:411-423.
    • (2003) Mol. Microbiol. , vol.49 , pp. 411-423
    • Bergmann, S.1    Wild, D.2    Diekmann, O.3    Frank, R.4    Bracht, D.5    Chhatwal, G.S.6    Hammerschmidt, S.7
  • 28
    • 34249332380 scopus 로고    scopus 로고
    • R. Gim'enez, M.A. Sorolla, J. Aguilar, J. Bad'ia, L. Baldomaa, 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., Aguilera L. R. Gim'enez, M.A. Sorolla, J. Aguilar, J. Bad'ia, L. Baldomaa, 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. 2007, 39:1190-1203.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1190-1203
    • Egea, L.1    Aguilera, L.2
  • 29
    • 67349091654 scopus 로고    scopus 로고
    • Identification and characterization of immunodominant B-cell epitope of the C-terminus of protective antigen of B. anthracis
    • Kaur M., Chug H., Singh H., Chandra S., Mishra M., Sharma M., Bhatnagar R. Identification and characterization of immunodominant B-cell epitope of the C-terminus of protective antigen of B. anthracis. Mol. Immunol. 2009, 46:2107-2115.
    • (2009) Mol. Immunol. , vol.46 , pp. 2107-2115
    • Kaur, M.1    Chug, H.2    Singh, H.3    Chandra, S.4    Mishra, M.5    Sharma, M.6    Bhatnagar, R.7
  • 31
    • 0034719105 scopus 로고    scopus 로고
    • Conversion of fibrinogen to fibrin: mechanism of exposure of tPA- and plasminogen-binding sites
    • Yakovlev S., Makogonenko E., Kurochkina N., Nieuwenhuizen W., Ingham K., Medved L. Conversion of fibrinogen to fibrin: mechanism of exposure of tPA- and plasminogen-binding sites. Biochemistry 2000, 39:15730-15741.
    • (2000) Biochemistry , vol.39 , pp. 15730-15741
    • Yakovlev, S.1    Makogonenko, E.2    Kurochkina, N.3    Nieuwenhuizen, W.4    Ingham, K.5    Medved, L.6
  • 32
    • 0029149950 scopus 로고
    • Bacterial plasminogen receptors: in vitro evidence for a role in degradation of the mammalian extracellular matrix
    • Lahteenmaki K., Virkola R., Pouttu R., Kuusela P., Kukkonen M., Korhonen T. Bacterial plasminogen receptors: in vitro evidence for a role in degradation of the mammalian extracellular matrix. Infect. Immun. 1995, 63:3659-3664.
    • (1995) Infect. Immun. , vol.63 , pp. 3659-3664
    • Lahteenmaki, K.1    Virkola, R.2    Pouttu, R.3    Kuusela, P.4    Kukkonen, M.5    Korhonen, T.6


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