메뉴 건너뛰기




Volumn 66, Issue 3, 1998, Pages 1252-1257

GroEL heat shock protein of Haemophilus ducreyi: Association with cell surface and capacity to bind to eukaryotic cells

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN;

EID: 0031888740     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.66.3.1252-1257.1998     Document Type: Article
Times cited : (93)

References (31)
  • 1
    • 0023601678 scopus 로고
    • Whole-cell ELISA for typing Neisseria meningitidis with monoclonal antibodies
    • Abdillahi, H., and J. T. Poolman. 1987. Whole-cell ELISA for typing Neisseria meningitidis with monoclonal antibodies. FEMS Micrnbiol. Lett. 48: 367-371.
    • (1987) FEMS Micrnbiol. Lett. , vol.48 , pp. 367-371
    • Abdillahi, H.1    Poolman, J.T.2
  • 3
    • 0031036567 scopus 로고    scopus 로고
    • Attachment of Haemophilus ducreyi to human foreskin fibroblasts involves LOS and fibronectin
    • Alfa, M. J., and P. Degagne. 1997. Attachment of Haemophilus ducreyi to human foreskin fibroblasts involves LOS and fibronectin. Microb. Pathog. 22:39-46.
    • (1997) Microb. Pathog. , vol.22 , pp. 39-46
    • Alfa, M.J.1    Degagne, P.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0027521181 scopus 로고
    • Antibodies directed against Haemophilus ducreyi heat shock proteins
    • Brown, T. J., J. Jardine, and C. A. Ison. 1993. Antibodies directed against Haemophilus ducreyi heat shock proteins. Microb, Pathog. 15:131-139.
    • (1993) Microb, Pathog. , vol.15 , pp. 131-139
    • Brown, T.J.1    Jardine, J.2    Ison, C.A.3
  • 7
    • 0025294798 scopus 로고
    • Induction of Salmonella stress proteins upon infection of macrophages
    • Buchmeier, N. A., and F. Heffron. 1990. Induction of Salmonella stress proteins upon infection of macrophages. Science 248:730-732.
    • (1990) Science , vol.248 , pp. 730-732
    • Buchmeier, N.A.1    Heffron, F.2
  • 8
    • 0025294377 scopus 로고
    • Characterization of the heat shock response and identification of heat shock protein antigens of Borrelia burgdorferi
    • Carreiro, M. M., D. C. Laux, and D. R. Nelson. 1990. Characterization of the heat shock response and identification of heat shock protein antigens of Borrelia burgdorferi. Infect. Immun. 58:2186-2191.
    • (1990) Infect. Immun. , vol.58 , pp. 2186-2191
    • Carreiro, M.M.1    Laux, D.C.2    Nelson, D.R.3
  • 9
    • 0026642506 scopus 로고
    • A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus
    • Ensgraber, M., and M. Loos. 1992. A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus. Infect. Immun. 60:3072-3078.
    • (1992) Infect. Immun. , vol.60 , pp. 3072-3078
    • Ensgraber, M.1    Loos, M.2
  • 10
    • 0026716505 scopus 로고
    • Urease-associated heat shock protein of Helkobacter pylori
    • Evans, D. J., Jr., D. G. Evans, L. Engstrand, and D. Y. Graham. 1992. Urease-associated heat shock protein of Helkobacter pylori. Infect. Immun. 60:2125-2127.
    • (1992) Infect. Immun. , vol.60 , pp. 2125-2127
    • Evans Jr., D.J.1    Evans, D.G.2    Engstrand, L.3    Graham, D.Y.4
  • 11
    • 0029086457 scopus 로고
    • Localisation and immunological properties of a 24-kDa surface protein of Haemophilus ducreyi
    • Frisk, A., E. L. Roggen, and T. Lagergård. 1995. Localisation and immunological properties of a 24-kDa surface protein of Haemophilus ducreyi. J. Med. Microbiol. 43:192-200.
    • (1995) J. Med. Microbiol. , vol.43 , pp. 192-200
    • Frisk, A.1    Roggen, E.L.2    Lagergård, T.3
  • 12
    • 0023729074 scopus 로고
    • Immunochemical characterization of and isolation of the gene for a Borrelia hurgdorferi immunodominant 60-kilodalton antigen common to a wide range of bacteria
    • Hansen, K., J. M. Bangsborg, H. Fjordvang, N. Strandberg Pedersen, and P. Hindersson. 1988. Immunochemical characterization of and isolation of the gene for a Borrelia hurgdorferi immunodominant 60-kilodalton antigen common to a wide range of bacteria. Infect. Immun. 56:2047-2053.
    • (1988) Infect. Immun. , vol.56 , pp. 2047-2053
    • Hansen, K.1    Bangsborg, J.M.2    Fjordvang, H.3    Strandberg Pedersen, N.4    Hindersson, P.5
  • 13
    • 0025113835 scopus 로고
    • Legionella pneumophila htpAB heat shock operon: Nucleotide sequence and expression of the 60-kilodalton antigen in L. pneumophila-infected HeLa cells
    • Hoffman, P. S., L. Houston, and C. A. Butler. 1990. Legionella pneumophila htpAB heat shock operon: nucleotide sequence and expression of the 60-kilodalton antigen in L. pneumophila-infected HeLa cells. Infect. Immun. 58: 3380-3387.
    • (1990) Infect. Immun. , vol.58 , pp. 3380-3387
    • Hoffman, P.S.1    Houston, L.2    Butler, C.A.3
  • 14
    • 0029929131 scopus 로고    scopus 로고
    • Acidic pH changes receptor binding specificity of Helicobacter pylori: A binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization
    • Huesca, M., S. Borgia, P. Hoffman, and C. L. Lingwood. 1996. Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization. Infect. Immun. 64:2643-2648.
    • (1996) Infect. Immun. , vol.64 , pp. 2643-2648
    • Huesca, M.1    Borgia, S.2    Hoffman, P.3    Lingwood, C.L.4
  • 15
    • 14444267366 scopus 로고    scopus 로고
    • Unpublished data
    • Ison, C. A. Unpublished data.
    • Ison, C.A.1
  • 16
    • 0025249304 scopus 로고
    • Heat shock proteins and the immune response
    • Kaufmann, S. H. E. 1990. Heat shock proteins and the immune response. Immunol. Today 11:129-136.
    • (1990) Immunol. Today , vol.11 , pp. 129-136
    • Kaufmann, S.H.E.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0025977809 scopus 로고
    • Endotoxin shedding by enterobacteria: Free and cell-bound endotoxin differ in Limulus activity
    • Mattsby-Baltzer, I., K. Lindgren, B. Lindholm, and L. Edebo. 1991. Endotoxin shedding by enterobacteria: free and cell-bound endotoxin differ in Limulus activity. Infect. Immun. 59:689-695.
    • (1991) Infect. Immun. , vol.59 , pp. 689-695
    • Mattsby-Baltzer, I.1    Lindgren, K.2    Lindholm, B.3    Edebo, L.4
  • 19
    • 0026768043 scopus 로고
    • Molecular analysis of the Haemophilus ducreyi groE heat shock operon
    • Parsons, L. M., A. L. Waring, and M. Shayegani. 1992. Molecular analysis of the Haemophilus ducreyi groE heat shock operon. Infect. Immun. 60:4111-4118.
    • (1992) Infect. Immun. , vol.60 , pp. 4111-4118
    • Parsons, L.M.1    Waring, A.L.2    Shayegani, M.3
  • 20
    • 0030949252 scopus 로고    scopus 로고
    • Alterations in levels of DnaK and GroEL result in diminished survival and adherence of stressed Haemophilus ducreyi
    • Parsons, L. M., R. J. Limberger, and M. Shayegani. 1997. Alterations in levels of DnaK and GroEL result in diminished survival and adherence of stressed Haemophilus ducreyi. Infect. Immun. 65:2413-2419.
    • (1997) Infect. Immun. , vol.65 , pp. 2413-2419
    • Parsons, L.M.1    Limberger, R.J.2    Shayegani, M.3
  • 21
    • 0030021824 scopus 로고    scopus 로고
    • Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis
    • Phadnis, S. H., M. H. Parlow, M. Levy, D. Ilver, C. M. Caulkins, J. B. Connors, and B. E. Dunn. 1996. Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis. Infect. Immun. 64:905-912.
    • (1996) Infect. Immun. , vol.64 , pp. 905-912
    • Phadnis, S.H.1    Parlow, M.H.2    Levy, M.3    Ilver, D.4    Caulkins, C.M.5    Connors, J.B.6    Dunn, B.E.7
  • 22
    • 0026521346 scopus 로고
    • Haemophilus ducreyi, a cytotoxin-producing bacterium
    • Purvén, M., and T. Lagergård. 1992. Haemophilus ducreyi, a cytotoxin-producing bacterium. Infect. Immun. 60:1156-1162.
    • (1992) Infect. Immun. , vol.60 , pp. 1156-1162
    • Purvén, M.1    Lagergård, T.2
  • 23
    • 0028116493 scopus 로고
    • Subcellular localization and chaperone activities of Borrelia burgdorferi Hsp60 and Hsp70
    • Scorpio, A., P. Johnson, A. Laquerre, and D. R. Nelson. 1994. Subcellular localization and chaperone activities of Borrelia burgdorferi Hsp60 and Hsp70. J. Bacteriol. 176:6449-6456.
    • (1994) J. Bacteriol. , vol.176 , pp. 6449-6456
    • Scorpio, A.1    Johnson, P.2    Laquerre, A.3    Nelson, D.R.4
  • 24
    • 0023840143 scopus 로고
    • The Mycobacterium tuberculosis 65-kilodalton antigen is a heat shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein
    • Shinnick, T. M., M. H. Vodkin, and J. C. Williams. 1988. The Mycobacterium tuberculosis 65-kilodalton antigen is a heat shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein. Infect. Immun. 56:446-451.
    • (1988) Infect. Immun. , vol.56 , pp. 446-451
    • Shinnick, T.M.1    Vodkin, M.H.2    Williams, J.C.3
  • 25
    • 14444270172 scopus 로고    scopus 로고
    • Characterization of the interaction between Haemophilus ducreyi and epithelial cell proteoglycans
    • abstr. P374, ISSTDR, Seville, Spain
    • Taylor, S. N., J. E. Figueroa, and K. H. Johnston. 1997. Characterization of the interaction between Haemophilus ducreyi and epithelial cell proteoglycans, abstr. P374, p. 124. In Program and abstracts of the 12th Meeting of the ISSTDR. ISSTDR, Seville, Spain.
    • (1997) Program and Abstracts of the 12th Meeting of the ISSTDR , pp. 124
    • Taylor, S.N.1    Figueroa, J.E.2    Johnston, K.H.3
  • 27
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 28
    • 0028008787 scopus 로고
    • M protein mediates Streptococcal adhesion to HEp-2 cells
    • Wang, J.-R., and M. W. Stinson. 1994. M protein mediates Streptococcal adhesion to HEp-2 cells. Infect. Immun. 62:442-448.
    • (1994) Infect. Immun. , vol.62 , pp. 442-448
    • Wang, J.-R.1    Stinson, M.W.2
  • 29
    • 0029742511 scopus 로고    scopus 로고
    • Flow cytometric analysis of the heat shock protein 60 expressed on the cell surface of Helkobacter pylori
    • Yamaguchi, H., T. Osaki, H. Taguchi, T. Hanana, T. Yamamoto, and S. Kamiya. 1996. Flow cytometric analysis of the heat shock protein 60 expressed on the cell surface of Helkobacter pylori. J. Med. Microbiol. 45: 270-277.
    • (1996) J. Med. Microbiol. , vol.45 , pp. 270-277
    • Yamaguchi, H.1    Osaki, T.2    Taguchi, H.3    Hanana, T.4    Yamamoto, T.5    Kamiya, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.