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Volumn 410, Issue 2, 2011, Pages 339-344

Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation

Author keywords

Actin dynamics; Protein structure; Tuberculosis

Indexed keywords

G ACTIN; HEMAGGLUTININ; HEPARIN BINDING PROTEIN;

EID: 79959729031     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.05.159     Document Type: Article
Times cited : (31)

References (40)
  • 2
    • 77952356637 scopus 로고    scopus 로고
    • Tuberculosis: what we don't know can, and does, hurt us
    • Russell D.G., Barry C.E., Flynn J.L. Tuberculosis: what we don't know can, and does, hurt us. Science 2010, 328:852-856.
    • (2010) Science , vol.328 , pp. 852-856
    • Russell, D.G.1    Barry, C.E.2    Flynn, J.L.3
  • 4
    • 39149104645 scopus 로고    scopus 로고
    • The role of resuscitation promoting factors in pathogenesis and reactivation of Mycobacterium tuberculosis during intra-peritoneal infection in mice
    • Biketov S., Potapov V., Ganina E., Downing K., Kana B.D., Kaprelyants A. The role of resuscitation promoting factors in pathogenesis and reactivation of Mycobacterium tuberculosis during intra-peritoneal infection in mice. BMC Infect. Dis. 2007, 7:146.
    • (2007) BMC Infect. Dis. , vol.7 , pp. 146
    • Biketov, S.1    Potapov, V.2    Ganina, E.3    Downing, K.4    Kana, B.D.5    Kaprelyants, A.6
  • 5
    • 31344441136 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis heparin-binding haemagglutinin adhesin (HBHA) triggers receptor-mediated transcytosis without altering the integrity of tight junctions
    • Menozzi F.D., Reddy V.M., Cayet D., Raze D., Debrie A.S., Dehouck M.P., Cecchelli R., Locht C. Mycobacterium tuberculosis heparin-binding haemagglutinin adhesin (HBHA) triggers receptor-mediated transcytosis without altering the integrity of tight junctions. Microbes Infect. 2006, 8:1-9.
    • (2006) Microbes Infect. , vol.8 , pp. 1-9
    • Menozzi, F.D.1    Reddy, V.M.2    Cayet, D.3    Raze, D.4    Debrie, A.S.5    Dehouck, M.P.6    Cecchelli, R.7    Locht, C.8
  • 7
    • 0032514676 scopus 로고    scopus 로고
    • Molecular characterization of the mycobacterial heparin-binding hemagglutinin a mycobacterial adhesin
    • Menozzi F.D., Bischoff R., Fort E., Brennan M.J., Locht C. Molecular characterization of the mycobacterial heparin-binding hemagglutinin a mycobacterial adhesin. Proc. Natl. Acad. Sci. USA 1998, 95:12625-12630.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12625-12630
    • Menozzi, F.D.1    Bischoff, R.2    Fort, E.3    Brennan, M.J.4    Locht, C.5
  • 8
    • 0035849873 scopus 로고    scopus 로고
    • The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination
    • Pethe K., Alonso S., Biet F., Delogu G., Brennan M.J., Locht C., Menozzi F.D. The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination. Nature 2001, 412:190-194.
    • (2001) Nature , vol.412 , pp. 190-194
    • Pethe, K.1    Alonso, S.2    Biet, F.3    Delogu, G.4    Brennan, M.J.5    Locht, C.6    Menozzi, F.D.7
  • 9
    • 0034640509 scopus 로고    scopus 로고
    • Characterization of the heparin-binding site of the mycobacterial heparin-binding hemagglutinin adhesin
    • Pethe K., Aumercier M., Fort E., Gatot C., Locht C., Menozzi F.D. Characterization of the heparin-binding site of the mycobacterial heparin-binding hemagglutinin adhesin. J. Biol. Chem. 2000, 275:14273-14280.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14273-14280
    • Pethe, K.1    Aumercier, M.2    Fort, E.3    Gatot, C.4    Locht, C.5    Menozzi, F.D.6
  • 10
    • 0032763725 scopus 로고    scopus 로고
    • Functional domains present in the mycobacterial hemagglutinin HBHA
    • Delogu G., Brennan M.J. Functional domains present in the mycobacterial hemagglutinin HBHA. J. Bacteriol. 1999, 181:7464-7469.
    • (1999) J. Bacteriol. , vol.181 , pp. 7464-7469
    • Delogu, G.1    Brennan, M.J.2
  • 11
    • 46049101224 scopus 로고    scopus 로고
    • Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis
    • Esposito C., Pethoukov M.V., Svergun D.I., Ruggiero A., Pedone C., Pedone E., Berisio R. Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis. J. Bacteriol. 2008, 190:4749-4753.
    • (2008) J. Bacteriol. , vol.190 , pp. 4749-4753
    • Esposito, C.1    Pethoukov, M.V.2    Svergun, D.I.3    Ruggiero, A.4    Pedone, C.5    Pedone, E.6    Berisio, R.7
  • 12
    • 77950371492 scopus 로고    scopus 로고
    • Dimerisation and structural integrity of heparin binding hemagglutinin A from Mycobacterium tuberculosis: implications for bacterial agglutination
    • Esposito C., Carullo P., Pedone E., Graziano G., Del Vecchio P., Berisio R. Dimerisation and structural integrity of heparin binding hemagglutinin A from Mycobacterium tuberculosis: implications for bacterial agglutination. FEBS Lett. 2010, 584:1091-1096.
    • (2010) FEBS Lett. , vol.584 , pp. 1091-1096
    • Esposito, C.1    Carullo, P.2    Pedone, E.3    Graziano, G.4    Del Vecchio, P.5    Berisio, R.6
  • 14
  • 16
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard T.D., Cooper J.A. Actin, a central player in cell shape and movement. Science 2009, 326:1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 17
    • 38349062512 scopus 로고    scopus 로고
    • Exit strategies of intracellular pathogens
    • Hybiske K., Stephens R.S. Exit strategies of intracellular pathogens. Nat. Rev. Microbiol. 2008, 6:99-110.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 99-110
    • Hybiske, K.1    Stephens, R.S.2
  • 18
    • 63449109253 scopus 로고    scopus 로고
    • Cell biology the art of making an exit
    • Carlsson F., Brown E.J. Cell biology the art of making an exit. Science 2009, 323:1678-1679.
    • (2009) Science , vol.323 , pp. 1678-1679
    • Carlsson, F.1    Brown, E.J.2
  • 20
    • 63449091213 scopus 로고    scopus 로고
    • Infection by tubercular mycobacteria is spread by nonlytic ejection from their amoeba hosts
    • Hagedorn M., Rohde K.H., Russell D.G., Soldati T. Infection by tubercular mycobacteria is spread by nonlytic ejection from their amoeba hosts. Science 2009, 323:1729-1733.
    • (2009) Science , vol.323 , pp. 1729-1733
    • Hagedorn, M.1    Rohde, K.H.2    Russell, D.G.3    Soldati, T.4
  • 21
    • 57349200310 scopus 로고    scopus 로고
    • Interaction of the mycobacterial heparin-binding hemagglutinin with actin as evidenced by single-molecule force spectroscopy
    • Verbelen C., Dupres V., Raze D., Bompard C., Locht C., Dufrene Y.F. Interaction of the mycobacterial heparin-binding hemagglutinin with actin as evidenced by single-molecule force spectroscopy. J. Bacteriol. 2008, 190:7614-7620.
    • (2008) J. Bacteriol. , vol.190 , pp. 7614-7620
    • Verbelen, C.1    Dupres, V.2    Raze, D.3    Bompard, C.4    Locht, C.5    Dufrene, Y.F.6
  • 22
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson B., Lofas S., Lindquist G. Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 1991, 198:268-277.
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Lofas, S.2    Lindquist, G.3
  • 23
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein L.R., Graceffa P., Dominguez R. The crystal structure of uncomplexed actin in the ADP state. Science 2001, 293:708-711.
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 24
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991, 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 25
    • 34247095612 scopus 로고    scopus 로고
    • Mutation analysis of the short cytoplasmic domain of the cell-cell adhesion molecule CEACAM1 identifies residues that orchestrate actin binding and lumen formation
    • Chen C.J., Kirshner J., Sherman M.A., Hu W., Nguyen T., Shively J.E. Mutation analysis of the short cytoplasmic domain of the cell-cell adhesion molecule CEACAM1 identifies residues that orchestrate actin binding and lumen formation. J. Biol. Chem. 2007, 282:5749-5760.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5749-5760
    • Chen, C.J.1    Kirshner, J.2    Sherman, M.A.3    Hu, W.4    Nguyen, T.5    Shively, J.E.6
  • 26
    • 36949021795 scopus 로고    scopus 로고
    • Molecular interactions in the insulin-like growth factor (IGF) axis: a surface plasmon resonance (SPR) based biosensor study
    • Beattie J., Phillips K., Shand J.H., Szymanowska M., Flint D.J., Allan G.J. Molecular interactions in the insulin-like growth factor (IGF) axis: a surface plasmon resonance (SPR) based biosensor study. Mol. Cell Biochem. 2008, 307:221-236.
    • (2008) Mol. Cell Biochem. , vol.307 , pp. 221-236
    • Beattie, J.1    Phillips, K.2    Shand, J.H.3    Szymanowska, M.4    Flint, D.J.5    Allan, G.J.6
  • 27
    • 0030804033 scopus 로고    scopus 로고
    • A correlative analysis of actin filament assembly structure and dynamics
    • Steinmetz M.O., Goldie K.N., Aebi U. A correlative analysis of actin filament assembly structure and dynamics. J. Cell Biol. 1997, 138:559-574.
    • (1997) J. Cell Biol. , vol.138 , pp. 559-574
    • Steinmetz, M.O.1    Goldie, K.N.2    Aebi, U.3
  • 28
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coue M., Brenner S.L., Spector I., Korn E.D. Inhibition of actin polymerization by latrunculin A. FEBS Lett. 1987, 213:316-318.
    • (1987) FEBS Lett. , vol.213 , pp. 316-318
    • Coue, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4
  • 32
    • 0036678138 scopus 로고    scopus 로고
    • Mycobacterial heparin-binding hemagglutinin and laminin-binding protein share antigenic methyllysines that confer resistance to proteolysis
    • Pethe K., Bifani P., Drobecq H., Sergheraert C., Debrie A.S., Locht C., Menozzi F.D. Mycobacterial heparin-binding hemagglutinin and laminin-binding protein share antigenic methyllysines that confer resistance to proteolysis. Proc. Natl. Acad. Sci. USA 2002, 99:10759-10764.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10759-10764
    • Pethe, K.1    Bifani, P.2    Drobecq, H.3    Sergheraert, C.4    Debrie, A.S.5    Locht, C.6    Menozzi, F.D.7
  • 33
    • 0023644588 scopus 로고
    • The mechanisms of ATP hydrolysis accompanying the polymerization of Mg-actin and Ca-actin
    • Carlier M.F., Pantaloni D., Korn E.D. The mechanisms of ATP hydrolysis accompanying the polymerization of Mg-actin and Ca-actin. J. Biol. Chem. 1987, 262:3052-3059.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3052-3059
    • Carlier, M.F.1    Pantaloni, D.2    Korn, E.D.3
  • 34
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T., Iwasa M., Aihara T., Maeda Y., Narita A. The nature of the globular- to fibrous-actin transition. Nature 2009, 457:441-445.
    • (2009) Nature , vol.457 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maeda, Y.4    Narita, A.5
  • 35
    • 58749101334 scopus 로고    scopus 로고
    • Structural biology: actin in a twist
    • Holmes K.C. Structural biology: actin in a twist. Nature 2009, 457:389-390.
    • (2009) Nature , vol.457 , pp. 389-390
    • Holmes, K.C.1
  • 36
    • 77949758115 scopus 로고    scopus 로고
    • Cell biology: actin filaments up against a wall
    • Sykes C., Plastino J. Cell biology: actin filaments up against a wall. Nature 2010, 464:365-366.
    • (2010) Nature , vol.464 , pp. 365-366
    • Sykes, C.1    Plastino, J.2
  • 37
    • 0041589208 scopus 로고    scopus 로고
    • Depolymerization of actin filaments by profilin effects of profilin on capping protein function
    • Bubb M.R., Yarmola E.G., Gibson B.G., Southwick F.S. Depolymerization of actin filaments by profilin effects of profilin on capping protein function. J. Biol. Chem. 2003, 278:24629-24635.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24629-24635
    • Bubb, M.R.1    Yarmola, E.G.2    Gibson, B.G.3    Southwick, F.S.4
  • 38
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta 4
    • Pantaloni D., Carlier M.F. How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell 1993, 75:1007-1014.
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 39
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins profilin
    • Kovar D.R., Harris E.S., Mahaffy R., Higgs H.N., Pollard T.D. Control of the assembly of ATP- and ADP-actin by formins profilin. Cell 2006, 124:423-435.
    • (2006) Cell , vol.124 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 40
    • 0037482886 scopus 로고    scopus 로고
    • A crucial role for profilin-actin in the intracellular motility of Listeria monocytogenes
    • Grenklo S., Geese M., Lindberg U., Wehland J., Karlsson R., Sechi A.S. A crucial role for profilin-actin in the intracellular motility of Listeria monocytogenes. EMBO Rep. 2003, 4:523-529.
    • (2003) EMBO Rep. , vol.4 , pp. 523-529
    • Grenklo, S.1    Geese, M.2    Lindberg, U.3    Wehland, J.4    Karlsson, R.5    Sechi, A.S.6


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