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Volumn 76, Issue 3, 2008, Pages 1093-1104

Novel adhesin from Pasteurella multocida that binds to the integrin-binding fibronectin FnIII9-10 repeats

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; AMINO ACID; ANTISERUM; BACTERIAL DNA; FIBRONECTIN; FIBRONECTIN BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; INTEGRIN; RECOMBINANT PROTEIN; FIBRONECTIN BINDING PROTEIN, BACTERIA; FIBRONECTIN-BINDING PROTEIN, BACTERIA; MEMBRANE PROTEIN; PEPTIDE LIBRARY; UNCLASSIFIED DRUG;

EID: 40749111917     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.01349-07     Document Type: Article
Times cited : (18)

References (27)
  • 2
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner, S. D., D. P. Norman, and G. L. Verdine. 2000. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 403:859-866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.2    Verdine, G.L.3
  • 3
    • 0041976985 scopus 로고    scopus 로고
    • Molecular and immunological characterization of Pasteurella multocida serotype A:3 OmpA: Evidence of its role in Pasteurella multocida interaction with extracellular matrix molecules
    • Dabo, S. M., A. W. Confer, and R. A. Quijano-Blas. 2003. Molecular and immunological characterization of Pasteurella multocida serotype A:3 OmpA: evidence of its role in Pasteurella multocida interaction with extracellular matrix molecules. Microb. Pathog. 35:147-157.
    • (2003) Microb. Pathog , vol.35 , pp. 147-157
    • Dabo, S.M.1    Confer, A.W.2    Quijano-Blas, R.A.3
  • 4
    • 25444495988 scopus 로고    scopus 로고
    • Adherence of Pasteurella multocida to fibronectin
    • Dabo, S. M., A. W. Confer, and S. D. Hartson. 2005. Adherence of Pasteurella multocida to fibronectin. Vet. Microbiol. 110:265-275.
    • (2005) Vet. Microbiol , vol.110 , pp. 265-275
    • Dabo, S.M.1    Confer, A.W.2    Hartson, S.D.3
  • 5
    • 0033950869 scopus 로고    scopus 로고
    • The type 4 fimbrial subunit gene of Pasteurella multocida
    • Doughty, S. W., C. G. Ruffolo, and B. Adler. 2000. The type 4 fimbrial subunit gene of Pasteurella multocida. Vet. Microbiol. 72:79-90.
    • (2000) Vet. Microbiol , vol.72 , pp. 79-90
    • Doughty, S.W.1    Ruffolo, C.G.2    Adler, B.3
  • 7
    • 0027620603 scopus 로고
    • Epidemiology of human infections by Pasteurella and related groups in France
    • Escande, F., and C. Lion. 1993. Epidemiology of human infections by Pasteurella and related groups in France. Int. J. Med. Microbiol. 279:131-139.
    • (1993) Int. J. Med. Microbiol , vol.279 , pp. 131-139
    • Escande, F.1    Lion, C.2
  • 8
    • 0023150590 scopus 로고    scopus 로고
    • Hemagglutination by Pasteurella multocida of porcine origin
    • Fortin, M., and M. Jacques. 2006. Hemagglutination by Pasteurella multocida of porcine origin. J. Clin. Microbiol. 25:938-939.
    • (2006) J. Clin. Microbiol , vol.25 , pp. 938-939
    • Fortin, M.1    Jacques, M.2
  • 9
    • 0033976798 scopus 로고    scopus 로고
    • The molecular biology of Pasteurella multocida
    • Hunt, M. L., B. Adler, and K. M. Townsend. 2000. The molecular biology of Pasteurella multocida. Vet. Microbiol. 72:3-25.
    • (2000) Vet. Microbiol , vol.72 , pp. 3-25
    • Hunt, M.L.1    Adler, B.2    Townsend, K.M.3
  • 10
    • 0023666065 scopus 로고
    • Integrins: A family of cell surface receptors
    • Hynes, R. O. 1987. Integrins: a family of cell surface receptors. Cell 48:549-554.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 11
    • 2942720646 scopus 로고    scopus 로고
    • Identification and characterization of bacterial-binding property in the type III repeat domain of fibronectin
    • Ito, H. O., S. Soutome, K. Nokihara, and M. Inoue. 2004. Identification and characterization of bacterial-binding property in the type III repeat domain of fibronectin. Biochem. Biophys. Res. Commun. 320:347-353.
    • (2004) Biochem. Biophys. Res. Commun , vol.320 , pp. 347-353
    • Ito, H.O.1    Soutome, S.2    Nokihara, K.3    Inoue, M.4
  • 12
    • 0027422155 scopus 로고
    • Virulence of capsulated and noncapsulated isolates of Pasteurella multocida and their adherence to porcine respiratory tract cells and mucus
    • Jacques, M., M. Kobisch, M. Belanger, and F. Dugal. 1993. Virulence of capsulated and noncapsulated isolates of Pasteurella multocida and their adherence to porcine respiratory tract cells and mucus. Infect. Immun. 61:4785-4792.
    • (1993) Infect. Immun , vol.61 , pp. 4785-4792
    • Jacques, M.1    Kobisch, M.2    Belanger, M.3    Dugal, F.4
  • 14
    • 11144281971 scopus 로고    scopus 로고
    • The Bacillus megaterium comE locus encodes a functional DNA uptake protein
    • Lammers, M., H. Nahrstedt, and F. Meinhardt, 2004. The Bacillus megaterium comE locus encodes a functional DNA uptake protein. J. Basic Microbiol. 44:451-458.
    • (2004) J. Basic Microbiol , vol.44 , pp. 451-458
    • Lammers, M.1    Nahrstedt, H.2    Meinhardt, F.3
  • 15
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy, D. J., I. Aukhil, and H. P. Erickson. 1996. 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84:155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 16
    • 0036225306 scopus 로고    scopus 로고
    • Isolation and characterization of a new succinic acid-producing bacterium, Mannheimia succiniciproducens MBEL55E, from bovine rumen
    • Lee, P. C., S. Y. Lee, S. H. Hong, and H. N. Chang. 2002. Isolation and characterization of a new succinic acid-producing bacterium, Mannheimia succiniciproducens MBEL55E, from bovine rumen. Appl. Microbiol. Biotechnol. 58:663-668.
    • (2002) Appl. Microbiol. Biotechnol , vol.58 , pp. 663-668
    • Lee, P.C.1    Lee, S.Y.2    Hong, S.H.3    Chang, H.N.4
  • 17
    • 34447334797 scopus 로고    scopus 로고
    • Multiple interactions among the competence proteins of Bacillus subtilis
    • Kramer, N., J. Hahn, and D. Dubnau. 2007. Multiple interactions among the competence proteins of Bacillus subtilis. Mol. Microbiol. 65:454-464.
    • (2007) Mol. Microbiol , vol.65 , pp. 454-464
    • Kramer, N.1    Hahn, J.2    Dubnau, D.3
  • 18
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main, A. L., T. S. Harvey, M. Baron, J. Boyd, and I. D. Campbell. 1992. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 71:671-678.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 19
    • 34247091939 scopus 로고    scopus 로고
    • Comparative functional genomic analysis of Pasteurellaceae genomes using phage display
    • Mullen, L. M., S. P. Nair, J. M. Ward, A. N. Rycroft, R. J. Williams, and B. Henderson. 2007. Comparative functional genomic analysis of Pasteurellaceae genomes using phage display. Vet. Microbiol. 122:123-134.
    • (2007) Vet. Microbiol , vol.122 , pp. 123-134
    • Mullen, L.M.1    Nair, S.P.2    Ward, J.M.3    Rycroft, A.N.4    Williams, R.J.5    Henderson, B.6
  • 20
    • 0001511468 scopus 로고
    • Variants of the cell recognition site of fibronectin that retain attachment-promoting activity
    • Pierschbacher, M. D., and E. Ruoslahti. 1984. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc. Natl. Acad. Sci. USA 81:5985-5988.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5985-5988
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 21
    • 21444441457 scopus 로고    scopus 로고
    • Borrelia burgdorferi binds fibronectin through a tandem beta-zipper, a common mechanism of fibronectin binding in staphylococci, streptococci, and spirochetes
    • Raibaud, S., U. Schwarz-Linek, J. H. Kim, H. T. Jenkins, E. R. Baines, S. Gurusiddappa, M. Hook, and J. R. Potts. 2006. Borrelia burgdorferi binds fibronectin through a tandem beta-zipper, a common mechanism of fibronectin binding in staphylococci, streptococci, and spirochetes. J. Biol. Chem. 280:18803-18809.
    • (2006) J. Biol. Chem , vol.280 , pp. 18803-18809
    • Raibaud, S.1    Schwarz-Linek, U.2    Kim, J.H.3    Jenkins, H.T.4    Baines, E.R.5    Gurusiddappa, S.6    Hook, M.7    Potts, J.R.8
  • 22
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electronopaque stain in electron microscopy
    • Reynolds, E. S. 1963. The use of lead citrate at high pH as an electronopaque stain in electron microscopy. J. Cell Biol. 17:208-212.
    • (1963) J. Cell Biol , vol.17 , pp. 208-212
    • Reynolds, E.S.1
  • 23
    • 0031025739 scopus 로고    scopus 로고
    • Identification, purification, and characterization of the type 4 fimbriae of Pasteurella multocida
    • Ruffolo, C. G., J. M. Tennent, W. P. Michalski, and B. Adler. 1997. Identification, purification, and characterization of the type 4 fimbriae of Pasteurella multocida. Infect. Immun. 65:339-343.
    • (1997) Infect. Immun , vol.65 , pp. 339-343
    • Ruffolo, C.G.1    Tennent, J.M.2    Michalski, W.P.3    Adler, B.4
  • 24
    • 0031022602 scopus 로고    scopus 로고
    • SAM as a protein interaction domain involved in developmental regulation
    • Schultz, J., C. P. Ponting, K. Hoffman, and P. Bork. 1997. SAM as a protein interaction domain involved in developmental regulation. Prot. Sci. 6:249-253.
    • (1997) Prot. Sci , vol.6 , pp. 249-253
    • Schultz, J.1    Ponting, C.P.2    Hoffman, K.3    Bork, P.4
  • 25
    • 2442442058 scopus 로고    scopus 로고
    • The molecular basis of fibronectin-mediated bacterial adherence to host cells
    • Schwarz-Linek, U., M. Hook, and J. R. Potts. 2004. The molecular basis of fibronectin-mediated bacterial adherence to host cells. Mol. Microbiol. 52:631-641.
    • (2004) Mol. Microbiol , vol.52 , pp. 631-641
    • Schwarz-Linek, U.1    Hook, M.2    Potts, J.R.3
  • 26
    • 33748209542 scopus 로고    scopus 로고
    • Fibronectin-binding proteins of Gram-positive cocci
    • Schwarz-Linek, U., M. Hook, and J. R. Potts. 2006. Fibronectin-binding proteins of Gram-positive cocci. Microb. Infect. 8:2291-2298.
    • (2006) Microb. Infect , vol.8 , pp. 2291-2298
    • Schwarz-Linek, U.1    Hook, M.2    Potts, J.R.3
  • 27
    • 0034661711 scopus 로고    scopus 로고
    • Common fold in helix-hairpin-helix proteins
    • Shao, X., and N. V. Grishin. 2000. Common fold in helix-hairpin-helix proteins. Nucleic Acids Res. 28:2643-2650.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2643-2650
    • Shao, X.1    Grishin, N.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.