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Volumn 2, Issue 7, 2005, Pages 515-520

Nanoscale mapping and functional analysis of individual adhesins on living bacteria

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; GLYCOCONJUGATE; HEMAGGLUTININ; HEPARIN; HEPARIN BINDING PROTEIN;

EID: 23644447180     PISSN: 15487091     EISSN: None     Source Type: Journal    
DOI: 10.1038/nmeth769     Document Type: Article
Times cited : (308)

References (31)
  • 1
    • 0029838994 scopus 로고    scopus 로고
    • Identification of a heparin-binding hemagglutinin present in mycobacteria
    • Menozzi, F.D. et al. Identification of a heparin-binding hemagglutinin present in mycobacteria. J. Exp. Med. 184, 993-1001 (1996).
    • (1996) J. Exp. Med. , vol.184 , pp. 993-1001
    • Menozzi, F.D.1
  • 2
    • 0034640509 scopus 로고    scopus 로고
    • Characterization of the heparin-binding site of the mycobacterial heparin-binding hemagglutinin adhesin
    • Pethe, K. et al. Characterization of the heparin-binding site of the mycobacterial heparin-binding hemagglutinin adhesin. J. Biol. Chem. 275, 14273-14280 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14273-14280
    • Pethe, K.1
  • 3
    • 0034114217 scopus 로고    scopus 로고
    • Interaction of Mycobacterium avium complex with human respiratory epithelial cells
    • Reddy, V.M. & Kumar, B. Interaction of Mycobacterium avium complex with human respiratory epithelial cells. J. Infect. Dis. 181, 1189-1193 (2000).
    • (2000) J. Infect. Dis. , vol.181 , pp. 1189-1193
    • Reddy, V.M.1    Kumar, B.2
  • 4
    • 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 95, 12625-12630 (1998).
    • (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
  • 5
    • 0035849873 scopus 로고    scopus 로고
    • The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination
    • Pethe, K. et al. The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination. Nature 412, 190-194 (2001).
    • (2001) Nature , vol.412 , pp. 190-194
    • Pethe, K.1
  • 6
    • 0036892211 scopus 로고    scopus 로고
    • Decreased infectivity despite unaltered C3 binding by a ΔhbhA mutant of Mycobacterium tuberculosis
    • Mueller-Ortiz, S.L. et al. Decreased infectivity despite unaltered C3 binding by a ΔhbhA mutant of Mycobacterium tuberculosis. Infect. Immun. 70, 6751-6760 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 6751-6760
    • Mueller-Ortiz, S.L.1
  • 7
    • 0032763725 scopus 로고    scopus 로고
    • Functional domains in the mycobacterial hemagglutinin, HBHA
    • Delogu, G. & Brennan, M.J. Functional domains in the mycobacterial hemagglutinin, HBHA. J. Bacteriol. 181, 7464-7469 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 7464-7469
    • Delogu, G.1    Brennan, M.J.2
  • 9
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel, A. & Müller, D.J. Observing single biomolecules at work with the atomic force microscope. Nat. Struct. Biol. 7, 715-718 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 715-718
    • Engel, A.1    Müller, D.J.2
  • 10
    • 2942602100 scopus 로고    scopus 로고
    • Scanning probe evolution in biology
    • Hörber, J.K. & Miles, M.J. Scanning probe evolution in biology. Science 302, 1002-1005 (2003).
    • (2003) Science , vol.302 , pp. 1002-1005
    • Hörber, J.K.1    Miles, M.J.2
  • 11
    • 4444233817 scopus 로고    scopus 로고
    • Using nanotechniques to explore microbial surfaces
    • Dufrêne, Y.F. Using nanotechniques to explore microbial surfaces. Nat. Rev. Microbiol. 2, 451-460 (2004).
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 451-460
    • Dufrêne, Y.F.1
  • 12
    • 0028007197 scopus 로고
    • Direct measurement of the forces between complementary strands of DNA
    • Lee, G.U., Chrisey, L.A. & Colton, R.J. Direct measurement of the forces between complementary strands of DNA. Science 266, 771-773 (1994).
    • (1994) Science , vol.266 , pp. 771-773
    • Lee, G.U.1    Chrisey, L.A.2    Colton, R.J.3
  • 13
    • 0029883621 scopus 로고    scopus 로고
    • Detection and localization of individual antibody-antigen recognition events by atomic force microscopy
    • Hinterdorfer, P., Baumgartner, W., Gruber, H.J., Schilcher, K. & Schindler, H. Detection and localization of individual antibody-antigen recognition events by atomic force microscopy. Proc. Natl. Acad. Sci. USA 93, 3477-3481 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3477-3481
    • Hinterdorfer, P.1    Baumgartner, W.2    Gruber, H.J.3    Schilcher, K.4    Schindler, H.5
  • 14
    • 0035907067 scopus 로고    scopus 로고
    • Bacterial recognition of mineral surfaces: Nanoscale interactions between Shewanella and α-Fe00H
    • Lower, S.K., Hochella, M.F. & Beveridge, T.J. Bacterial recognition of mineral surfaces: nanoscale interactions between Shewanella and α-Fe00H. Science 292, 1360-1363 (2001).
    • (2001) Science , vol.292 , pp. 1360-1363
    • Lower, S.K.1    Hochella, M.F.2    Beveridge, T.J.3
  • 15
    • 0037076617 scopus 로고    scopus 로고
    • Elasticity of Pseudomonas putida KT2442 surface polymers probed with single-molecule force microscopy
    • Abu-Lail, N.I. & Camesano, T.A. Elasticity of Pseudomonas putida KT2442 surface polymers probed with single-molecule force microscopy. Langmuir 18, 4071-4081 (2002).
    • (2002) Langmuir , vol.18 , pp. 4071-4081
    • Abu-Lail, N.I.1    Camesano, T.A.2
  • 16
    • 0031019894 scopus 로고    scopus 로고
    • Atomic force microscope imaging contrast based on molecular recognition
    • Ludwig, M., Dettmann, W. & Gaub, H.E. Atomic force microscope imaging contrast based on molecular recognition. Biophys. J. 72, 445-448 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 445-448
    • Ludwig, M.1    Dettmann, W.2    Gaub, H.E.3
  • 17
    • 0033121032 scopus 로고    scopus 로고
    • Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope
    • Heinz, W.F. & Hoh, J.H. Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope. Trends Biotechnol. 17, 143-150 (1999).
    • (1999) Trends Biotechnol. , vol.17 , pp. 143-150
    • Heinz, W.F.1    Hoh, J.H.2
  • 18
    • 0034097199 scopus 로고    scopus 로고
    • Affinity imaging of red blood cells using an atomic force microscope
    • Grandbois, M., Dettmann, W., Benoit, M. & Gaub, H.E. Affinity imaging of red blood cells using an atomic force microscope. J. Histochem. Cytochem. 48, 719-724 (2000).
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 719-724
    • Grandbois, M.1    Dettmann, W.2    Benoit, M.3    Gaub, H.E.4
  • 20
    • 1542345480 scopus 로고    scopus 로고
    • Elasticity and adhesion force mapping reveals real-time clustering of growth factor receptors and associated changes in local cellular rheological properties
    • Almqvist, N. et al. Elasticity and adhesion force mapping reveals real-time clustering of growth factor receptors and associated changes in local cellular rheological properties. Biophys. J. 86, 1753-1762 (2004).
    • (2004) Biophys. J. , vol.86 , pp. 1753-1762
    • Almqvist, N.1
  • 21
    • 0037418505 scopus 로고    scopus 로고
    • Using liquid crystals to amplify protein-receptor interactions: Design of surfaces with nanometer-scale topography that present histidine-tagged protein receptors
    • Luk, Y-Y. et al. Using liquid crystals to amplify protein-receptor interactions: design of surfaces with nanometer-scale topography that present histidine-tagged protein receptors. Langmuir 19, 1671-1680 (2003).
    • (2003) Langmuir , vol.19 , pp. 1671-1680
    • Luk, Y.-Y.1
  • 22
    • 0031042739 scopus 로고    scopus 로고
    • Single molecule force spectroscopy on polysaccharides by atomic force microscopy
    • Rief, M., Oesterhelt, F., Heymann, B. & Gaub, H.E. Single molecule force spectroscopy on polysaccharides by atomic force microscopy. Science 275, 1295-1297 (1997).
    • (1997) Science , vol.275 , pp. 1295-1297
    • Rief, M.1    Oesterhelt, F.2    Heymann, B.3    Gaub, H.E.4
  • 23
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel, R., Nassoy, P., Leung, A., Ritchie, K. & Evans, E. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397, 50-53 (1999).
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 24
    • 0034636032 scopus 로고    scopus 로고
    • Cadherin interaction probed by atomic force microscopy
    • Baumgartner, W. et al. Cadherin interaction probed by atomic force microscopy. Proc. Natl. Acad. Sci. USA 97, 4005-4010 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4005-4010
    • Baumgartner, W.1
  • 25
    • 10744229173 scopus 로고    scopus 로고
    • β-Cyclodextrin host-guest complexes probed under thermodynamic equilibrium: Thermodynamics and AFM force spectroscopy
    • Auletta, T. β-Cyclodextrin host-guest complexes probed under thermodynamic equilibrium: thermodynamics and AFM force spectroscopy. J. Am. Chem. Soc. 126, 1577-1584 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1577-1584
    • Auletta, T.1
  • 26
    • 0026079261 scopus 로고
    • Surface morphology of Mycobacterium bovis BCG: Relation to mechanisms of cellular aggregation
    • Devadoss, P., Klegerman, M.E. & Groves, M.J. Surface morphology of Mycobacterium bovis BCG: relation to mechanisms of cellular aggregation. Microbios. 65, 111-125 (1991).
    • (1991) Microbios , vol.65 , pp. 111-125
    • Devadoss, P.1    Klegerman, M.E.2    Groves, M.J.3
  • 27
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E.L., Moy, V.T. & Gaub, H.E. Adhesion forces between individual ligand-receptor pairs. Science 264, 415-417 (1994).
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.L.1    Moy, V.T.2    Gaub, H.E.3
  • 28
    • 0027327277 scopus 로고
    • Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues
    • Margalit, H., Fischer, N. & Ben-Sasson, S.A. Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues. J. Biol. Chem. 268, 19228-19231 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 19228-19231
    • Margalit, H.1    Fischer, N.2    Ben-Sasson, S.A.3
  • 29
    • 0032851160 scopus 로고    scopus 로고
    • Functions of cell surface heparan sulfate proteoglycans
    • Bernfield, M. et al. Functions of cell surface heparan sulfate proteoglycans. Annu. Rev. Biochem. 68, 729-777 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 729-777
    • Bernfield, M.1
  • 30
    • 0037205432 scopus 로고    scopus 로고
    • Clustering induces redistribution of syndecan-4 core protein into raft membrane domains
    • Tkachenko, E. & Simons, M. Clustering induces redistribution of syndecan-4 core protein into raft membrane domains. J. Biol. Chem. 277, 19946-19951 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 19946-19951
    • Tkachenko, E.1    Simons, M.2
  • 31
    • 0142042801 scopus 로고    scopus 로고
    • Anti-adhesion therapy of bacterial diseases: Prospects and problems
    • Ofek, I., Hasty, D.L. & Sharon, N. Anti-adhesion therapy of bacterial diseases: prospects and problems. FEMS Immunol. Med. Microbiol. 38, 181-191 (2003).
    • (2003) FEMS Immunol. Med. Microbiol. , vol.38 , pp. 181-191
    • Ofek, I.1    Hasty, D.L.2    Sharon, N.3


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