메뉴 건너뛰기




Volumn 16, Issue 12, 1997, Pages 3426-3434

Aerolysin and pertussis toxin share a common receptor-binding domain

Author keywords

Aerolysin; C type lectins; Carbohydrate binding; Pertussis toxin; Toxins

Indexed keywords

AEROLYSIN; BACTERIAL TOXIN; CARBOHYDRATE BINDING PROTEIN; CELL RECEPTOR; LECTIN; MUTANT PROTEIN; PERTUSSIS TOXIN; UNCLASSIFIED DRUG;

EID: 0030957151     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.12.3426     Document Type: Article
Times cited : (50)

References (45)
  • 2
    • 0023884187 scopus 로고
    • Use of glycosyltransferases to restore pertussis toxin receptor activity to asialogalactofetuin
    • Armstrong, G.D., Howard, L.A. and Peppler, M.S. (1988) Use of glycosyltransferases to restore pertussis toxin receptor activity to asialogalactofetuin. J. Biol. Chem., 263, 8677-8684.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8677-8684
    • Armstrong, G.D.1    Howard, L.A.2    Peppler, M.S.3
  • 3
    • 0029916915 scopus 로고    scopus 로고
    • The PROSITE database, its status in 1995
    • Bairoch, A., Bucher, P. and Hofmann, K. (1996) The PROSITE database, its status in 1995. Nucleic Acid Res., 24, 189-196.
    • (1996) Nucleic Acid Res. , vol.24 , pp. 189-196
    • Bairoch, A.1    Bucher, P.2    Hofmann, K.3
  • 4
    • 0028878878 scopus 로고
    • Activation and mechanism of Clostridium septicum alpha toxin
    • Ballard, J., Crabtree, J., Roe, B.A. and Tweten, R.K. (1995) Activation and mechanism of Clostridium septicum alpha toxin. Infect. Immun., 63, 340-344.
    • (1995) Infect. Immun. , vol.63 , pp. 340-344
    • Ballard, J.1    Crabtree, J.2    Roe, B.A.3    Tweten, R.K.4
  • 5
    • 0027412196 scopus 로고
    • ALSCRIPT - A tool to format multiple sequence alignments
    • Barton, G.J. (1993) ALSCRIPT - a tool to format multiple sequence alignments. Protein Eng., 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 7
    • 0023877979 scopus 로고
    • Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein
    • Brennan, M.J., David, J.L., Kenimer, J.G. and Manclark, C.R. (1988) Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein. J. Biol. Chem., 263, 4895-4899.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4895-4899
    • Brennan, M.J.1    David, J.L.2    Kenimer, J.G.3    Manclark, C.R.4
  • 8
    • 0030591452 scopus 로고    scopus 로고
    • The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of the link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily
    • Brissett, N.C. and Perkins, S.J. (1996) The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of the link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily. FEBS Lett., 388, 211-216.
    • (1996) FEBS Lett. , vol.388 , pp. 211-216
    • Brissett, N.C.1    Perkins, S.J.2
  • 9
    • 0025004421 scopus 로고
    • Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida
    • Buckley, J.T. (1990) Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida. Biochem. Cell Biol., 68, 221-224.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 221-224
    • Buckley, J.T.1
  • 10
    • 0023710284 scopus 로고
    • Carbohydrate-recognition domains in animal lectins
    • Drickamer, K. (1988) Carbohydrate-recognition domains in animal lectins. J. Biol. Chem., 263, 9557-9560.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 12
    • 0028367338 scopus 로고
    • Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 Å resolution
    • Fraser, M.E., Chernaia, M.M., Kozlov, Y.V. and James, M.N.G. (1994) Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 Å resolution. Nature Struct. Biol., 1, 59-64.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 59-64
    • Fraser, M.E.1    Chernaia, M.M.2    Kozlov, Y.V.3    James, M.N.G.4
  • 13
    • 0001983754 scopus 로고
    • Seven toxic peptides that cross cell membranes
    • Jeljaszewica, J. and Wadstrom, T. (eds), Academic Press, New York
    • Gill, D.M. (1978) Seven toxic peptides that cross cell membranes. In Jeljaszewica, J. and Wadstrom, T. (eds), Bacterial Toxins and Cell Membranes. Academic Press, New York, pp. 291-332.
    • (1978) Bacterial Toxins and Cell Membranes , pp. 291-332
    • Gill, D.M.1
  • 14
    • 0027957760 scopus 로고
    • Insight into E-selectin ligand interaction from the crystal structure and mutagenesis of the lee EGF domains
    • Graves, B.J. et al. (1994) Insight into E-selectin ligand interaction from the crystal structure and mutagenesis of the lee EGF domains. Nature, 367, 532-538.
    • (1994) Nature , vol.367 , pp. 532-538
    • Graves, B.J.1
  • 15
    • 0025233528 scopus 로고
    • Site-directed mutagenesis of the hole-forming toxin aerolysin: Studies on the role of histidines in receptor binding and oligomerization of the monomer
    • Green, M.J. and Buckley, J.T. (1990) Site-directed mutagenesis of the hole-forming toxin aerolysin: studies on the role of histidines in receptor binding and oligomerization of the monomer. Biochemistry, 29, 2177-2180.
    • (1990) Biochemistry , vol.29 , pp. 2177-2180
    • Green, M.J.1    Buckley, J.T.2
  • 16
    • 0028044180 scopus 로고
    • Partial purification of the rat erythrocyte receptor for the channel-forming toxin aerolysin and reconstitution into planar lipid bilayers
    • Gruber, H.J., Wilmsen, H.-U., Cowell, S., Schindler, H. and Buckley, J.T. (1994) Partial purification of the rat erythrocyte receptor for the channel-forming toxin aerolysin and reconstitution into planar lipid bilayers. Mol. Microbiol., 14, 1093-1011.
    • (1994) Mol. Microbiol. , vol.14 , pp. 1093-11011
    • Gruber, H.J.1    Wilmsen, H.-U.2    Cowell, S.3    Schindler, H.4    Buckley, J.T.5
  • 17
    • 0028970780 scopus 로고
    • Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation
    • Hardie, K.R., Schulze, A., Parker, M.W. and Buckley, J.T. (1995) Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation. Mol. Microbiol., 17, 1035-1044.
    • (1995) Mol. Microbiol. , vol.17 , pp. 1035-1044
    • Hardie, K.R.1    Schulze, A.2    Parker, M.W.3    Buckley, J.T.4
  • 18
    • 0027389529 scopus 로고
    • Binding of pertussis toxin to lipid vesicles containing glycolipids
    • Hausman, S.Z. and Burns, D.L. (1993) Binding of pertussis toxin to lipid vesicles containing glycolipids. Infect. Immun., 61, 335-337.
    • (1993) Infect. Immun. , vol.61 , pp. 335-337
    • Hausman, S.Z.1    Burns, D.L.2
  • 19
    • 0029016503 scopus 로고
    • Utilization of sialic acid-binding synthetic peptide sequences derived from pertussis toxin as novel anti-inflammatory agents
    • Heerze, L.D., Smith, R.H., Wang, N. and Armstrong, G.D. (1995) Utilization of sialic acid-binding synthetic peptide sequences derived from pertussis toxin as novel anti-inflammatory agents. Glycobiology, 5, 427-433.
    • (1995) Glycobiology , vol.5 , pp. 427-433
    • Heerze, L.D.1    Smith, R.H.2    Wang, N.3    Armstrong, G.D.4
  • 20
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 21
    • 0020071103 scopus 로고
    • Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein
    • Howard, S.P. and Buckley, J.T. (1982) Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein. Biochemistry, 21, 1662-1667.
    • (1982) Biochemistry , vol.21 , pp. 1662-1667
    • Howard, S.P.1    Buckley, J.T.2
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones, T.A., Zhou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 23
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, J.P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, J.P.1
  • 24
    • 0030572693 scopus 로고    scopus 로고
    • Solution structure of the Link module: A hyaluronan-binding domain involved in extracellular matrix stability and cell migration
    • Kohda, D., Morton, C.J., Parkar, A.A., Hatanaka, H., Inagaki, F.M., Campbell, I.D. and Day, A.J. (1996) Solution structure of the Link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration. Cell, 86, 767-775.
    • (1996) Cell , vol.86 , pp. 767-775
    • Kohda, D.1    Morton, C.J.2    Parkar, A.A.3    Hatanaka, H.4    Inagaki, F.M.5    Campbell, I.D.6    Day, A.J.7
  • 25
    • 0027246026 scopus 로고
    • Characterization of pertussis toxin analogs containing mutations in B-oligomer subunits
    • Loosmore, S., Zealey, G., Cockle, S., Boux, H., Chong, P., Yacoob, R. and Klein, M. (1993) Characterization of pertussis toxin analogs containing mutations in B-oligomer subunits. Infect. Immun., 61, 2316-2324.
    • (1993) Infect. Immun. , vol.61 , pp. 2316-2324
    • Loosmore, S.1    Zealey, G.2    Cockle, S.3    Boux, H.4    Chong, P.5    Yacoob, R.6    Klein, M.7
  • 27
    • 0022572101 scopus 로고
    • Hydrophobic photolabelling of pertussis toxin subunits interacting with lipids
    • Momecucco, C., Tomasi, M., Schiavo, G. and Rappuoli, R. (1986) Hydrophobic photolabelling of pertussis toxin subunits interacting with lipids. FEBS Lett., 194, 301-304.
    • (1986) FEBS Lett. , vol.194 , pp. 301-304
    • Momecucco, C.1    Tomasi, M.2    Schiavo, G.3    Rappuoli, R.4
  • 28
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G. Brenner, S.E., Hubbard, T. and Chothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol., 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 30
    • 0027976196 scopus 로고
    • Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
    • Parker, M.W., Buckley, J.T., Postma, J.P.M., Tucker, A.D., Leonard, K., Pattus, F. and Tsernoglou, D. (1994) Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature, 367, 292-295.
    • (1994) Nature , vol.367 , pp. 292-295
    • Parker, M.W.1    Buckley, J.T.2    Postma, J.P.M.3    Tucker, A.D.4    Leonard, K.5    Pattus, F.6    Tsernoglou, D.7
  • 31
    • 0030043134 scopus 로고    scopus 로고
    • Aerolysin - The ins and outs of a model channel-forming toxin
    • Parker, M.W., van der Goot, F.G. and Buckley, J.T. (1996) Aerolysin - the ins and outs of a model channel-forming toxin. Mol. Microbiol., 19, 205-212.
    • (1996) Mol. Microbiol. , vol.19 , pp. 205-212
    • Parker, M.W.1    Van Der Goot, F.G.2    Buckley, J.T.3
  • 32
    • 0021182482 scopus 로고
    • The concept of pertussis as a toxin-mediated disease
    • Pittman, M. (1984) The concept of pertussis as a toxin-mediated disease. Pediatr. Infect. Dis., 3, 467-486.
    • (1984) Pediatr. Infect. Dis. , vol.3 , pp. 467-486
    • Pittman, M.1
  • 33
    • 0027448859 scopus 로고
    • Antiinflammatory effects in experimental meningitis of prokaryotic peptides that mimic selectins
    • Rozdzinski, E., Jones, T., Burnette, W.N., Burroughs, M. and Tuomanen, E. (1993) Antiinflammatory effects in experimental meningitis of prokaryotic peptides that mimic selectins. J. Infect. Dis., 168, 1422-1428.
    • (1993) J. Infect. Dis. , vol.168 , pp. 1422-1428
    • Rozdzinski, E.1    Jones, T.2    Burnette, W.N.3    Burroughs, M.4    Tuomanen, E.5
  • 34
    • 0029820557 scopus 로고    scopus 로고
    • Structure of the catalytic fragment of poly (ADP-ribose) polymerase from chicken
    • Ruf, A., de Murcia, J.M., de Murcia, G.M. and Schulz, G.E. (1996) Structure of the catalytic fragment of poly (ADP-ribose) polymerase from chicken. Proc. Natl Acad. Sci. USA, 93, 7481-7485.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7481-7485
    • Ruf, A.1    De Murcia, J.M.2    De Murcia, G.M.3    Schulz, G.E.4
  • 37
    • 0026543155 scopus 로고
    • Crystal structure of the cell-binding B oligomer of verotoxin-1 from E.coli
    • Stein, P.E., Boodhoo, A., Tyrrell, G.J., Brunton, J.L. and Read, R.J. (1992) Crystal structure of the cell-binding B oligomer of verotoxin-1 from E.coli. Nature, 355, 748-750.
    • (1992) Nature , vol.355 , pp. 748-750
    • Stein, P.E.1    Boodhoo, A.2    Tyrrell, G.J.3    Brunton, J.L.4    Read, R.J.5
  • 40
    • 0027499943 scopus 로고
    • Localisation of a receptor-binding domain on the S3 subunit of pertussis toxin by peptide mapping
    • Tallet, A., Seabrook, R.N., Irons, L.I., Robinson, A., van Heyningen, S. and Atkinson, T. (1993) Localisation of a receptor-binding domain on the S3 subunit of pertussis toxin by peptide mapping. Eur. J. Biochem., 211, 743-748.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 743-748
    • Tallet, A.1    Seabrook, R.N.2    Irons, L.I.3    Robinson, A.4    Van Heyningen, S.5    Atkinson, T.6
  • 41
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas, N.K. (1991) Atomic features of protein-carbohydrate interactions. Curr. Opin. Struct. Biol., 1, 732-740.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 732-740
    • Vyas, N.K.1
  • 42
    • 0026342025 scopus 로고
    • Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing
    • Weis, W.I., Kahn, R., Fourme, R., Drickamer, K. and Hendrickson, W.A. (1991) Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science, 254, 1608-1615.
    • (1991) Science , vol.254 , pp. 1608-1615
    • Weis, W.I.1    Kahn, R.2    Fourme, R.3    Drickamer, K.4    Hendrickson, W.A.5
  • 43
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis, W.I., Drickamer, K. and Hendrickson, W.A. (1992) Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature, 360, 127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.