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Volumn 30, Issue 37, 2012, Pages 5500-5505

Cytotoxin CctA, a major virulence factor of Clostridium chauvoei conferring protective immunity against myonecrosis

Author keywords

Black leg; Leucocidin; Pore forming toxin; Protective immunity

Indexed keywords

BACTERIAL TOXIN; BACTERIAL VACCINE; CLOSTRIDIUM CHAUVOEI TOXIN A; CLOSTRIDIUM CHAUVOEI VACCINE; HYBRID PROTEIN; NUSA PROTEIN; UNCLASSIFIED DRUG;

EID: 84864309478     PISSN: 0264410X     EISSN: 18732518     Source Type: Journal    
DOI: 10.1016/j.vaccine.2012.06.050     Document Type: Article
Times cited : (42)

References (43)
  • 1
    • 84864296161 scopus 로고
    • The pathogenic anaerobia bacteria
    • Springfield, Illinois, USA, L.D. Smith, B.L. Williams, C.C. Thomas (Eds.)
    • The pathogenic anaerobia bacteria. Clostridium chauvoei 1984, 164-179. Springfield, Illinois, USA. 3rd ed. L.D. Smith, B.L. Williams, C.C. Thomas (Eds.).
    • (1984) Clostridium chauvoei , pp. 164-179
  • 3
    • 42449105324 scopus 로고    scopus 로고
    • Human fulminant gas gangrene caused by Clostridium chauvoei
    • Nagano N., Isomine S., Kato H., et al. Human fulminant gas gangrene caused by Clostridium chauvoei. J Clin Microbiol 2008, 46(4):1545-1547.
    • (2008) J Clin Microbiol , vol.46 , Issue.4 , pp. 1545-1547
    • Nagano, N.1    Isomine, S.2    Kato, H.3
  • 4
    • 84855869294 scopus 로고    scopus 로고
    • Lethal human neutropenic entercolitis caused by Clostridium chauvoei in the United States: tip of the iceberg?
    • Weatherhead J.E., Tweardy D.J. Lethal human neutropenic entercolitis caused by Clostridium chauvoei in the United States: tip of the iceberg?. J Infect 2012, 64(2):225-227.
    • (2012) J Infect , vol.64 , Issue.2 , pp. 225-227
    • Weatherhead, J.E.1    Tweardy, D.J.2
  • 6
    • 0029915545 scopus 로고    scopus 로고
    • Clostridial enteric diseases of domestic animals
    • Songer J.G. Clostridial enteric diseases of domestic animals. Clin Microbiol Rev 1996, 9:216-234.
    • (1996) Clin Microbiol Rev , vol.9 , pp. 216-234
    • Songer, J.G.1
  • 7
    • 85010818919 scopus 로고    scopus 로고
    • Pathogenesis and pathology of blackleg in ruminants: the role of toxins and neuraminidase. A short review
    • Useh N.M., Nok A.J., Esievo K.A. Pathogenesis and pathology of blackleg in ruminants: the role of toxins and neuraminidase. A short review. Vet Q 2003, 25(4):155-159.
    • (2003) Vet Q , vol.25 , Issue.4 , pp. 155-159
    • Useh, N.M.1    Nok, A.J.2    Esievo, K.A.3
  • 8
    • 84857381369 scopus 로고    scopus 로고
    • Evidence-based medicine concerning efficacy of vaccination against Clostridium chauvoei infection in cattle
    • Uzal F.A. Evidence-based medicine concerning efficacy of vaccination against Clostridium chauvoei infection in cattle. Vet Clin North Am Food Anim Pract 2012, 28(1):71-77.
    • (2012) Vet Clin North Am Food Anim Pract , vol.28 , Issue.1 , pp. 71-77
    • Uzal, F.A.1
  • 9
    • 0015336538 scopus 로고
    • Preparation of a Clostridium chauvoei antigen and determination of protective immunity by plate agglutination test
    • Claus K.D., Macheak M.E. Preparation of a Clostridium chauvoei antigen and determination of protective immunity by plate agglutination test. Am J Vet Res 1972, 33(5):1045-1052.
    • (1972) Am J Vet Res , vol.33 , Issue.5 , pp. 1045-1052
    • Claus, K.D.1    Macheak, M.E.2
  • 10
    • 0018575207 scopus 로고
    • Field studies in sheep with multicomponent clostridial vaccines
    • Kerry J.B., Craig G.R. Field studies in sheep with multicomponent clostridial vaccines. Vet Rec 1979, 105(24):551-554.
    • (1979) Vet Rec , vol.105 , Issue.24 , pp. 551-554
    • Kerry, J.B.1    Craig, G.R.2
  • 11
    • 0016177312 scopus 로고
    • The protective antigen of a highly immunogenic strain of Clostridium chauvoei including an evaluation of its flagella as a protective antigen
    • Chandler H.M., Gulasekharam J. The protective antigen of a highly immunogenic strain of Clostridium chauvoei including an evaluation of its flagella as a protective antigen. J Gen Microbiol 1974, 84(1):128-134.
    • (1974) J Gen Microbiol , vol.84 , Issue.1 , pp. 128-134
    • Chandler, H.M.1    Gulasekharam, J.2
  • 12
    • 0028945341 scopus 로고
    • Reversible expression of motility and flagella in Clostridium chauvoei and their relationship to virulence
    • Tamura Y., Kijima-Tanaka M., Aoki A., Ogikubo Y., Takahashi T. Reversible expression of motility and flagella in Clostridium chauvoei and their relationship to virulence. Microbiology 1995, 141(Pt 3):605-610.
    • (1995) Microbiology , vol.141 , Issue.PART 3 , pp. 605-610
    • Tamura, Y.1    Kijima-Tanaka, M.2    Aoki, A.3    Ogikubo, Y.4    Takahashi, T.5
  • 13
    • 0023395441 scopus 로고
    • Production, characterization, and protective effect of monoclonal antibodies to Clostridium chauvoei flagella
    • Tanaka M., Hirayama N., Tamura Y. Production, characterization, and protective effect of monoclonal antibodies to Clostridium chauvoei flagella. Infect Immun 1987, 55:1779-1783.
    • (1987) Infect Immun , vol.55 , pp. 1779-1783
    • Tanaka, M.1    Hirayama, N.2    Tamura, Y.3
  • 14
    • 33745987360 scopus 로고    scopus 로고
    • Characterization of a sialidase (neuraminidase) isolated from Clostridium chauvoei (Jakari strain)
    • Useh N.M., Ajanusi J.O., Esievo K.A., Nok A.J. Characterization of a sialidase (neuraminidase) isolated from Clostridium chauvoei (Jakari strain). Cell Biochem Funct 2006, 24(4):347-352.
    • (2006) Cell Biochem Funct , vol.24 , Issue.4 , pp. 347-352
    • Useh, N.M.1    Ajanusi, J.O.2    Esievo, K.A.3    Nok, A.J.4
  • 15
    • 2542628614 scopus 로고
    • Studies on the soluble antigen and hemolysin of Clostridium chavoei strain 64
    • Verpoort J.A., Joubert F.J., Jansen B.C. Studies on the soluble antigen and hemolysin of Clostridium chavoei strain 64. S Afr J Agric Sci 1966, 9:153-172.
    • (1966) S Afr J Agric Sci , vol.9 , pp. 153-172
    • Verpoort, J.A.1    Joubert, F.J.2    Jansen, B.C.3
  • 16
    • 33748426018 scopus 로고    scopus 로고
    • Purification and sensitivity of Clostridium chauvoei hemolysin to various erythrocytes
    • Hang'ombe B.M., Kohda T., Mukamoto M., Kozaki S. Purification and sensitivity of Clostridium chauvoei hemolysin to various erythrocytes. Comp Immunol Microbiol Infect Dis 2006, 29(4):263-268.
    • (2006) Comp Immunol Microbiol Infect Dis , vol.29 , Issue.4 , pp. 263-268
    • Hang'ombe, B.M.1    Kohda, T.2    Mukamoto, M.3    Kozaki, S.4
  • 17
    • 80051992799 scopus 로고    scopus 로고
    • Genetic and functional characterization of the NanA sialidase from Clostridium chauvoei
    • Vilei E.M., Johansson A., Schlatter Y., Redhead K., Frey J. Genetic and functional characterization of the NanA sialidase from Clostridium chauvoei. Vet Res 2011, 42(1):2.
    • (2011) Vet Res , vol.42 , Issue.1 , pp. 2
    • Vilei, E.M.1    Johansson, A.2    Schlatter, Y.3    Redhead, K.4    Frey, J.5
  • 18
    • 0024553747 scopus 로고
    • Rapid extraction of bacterial genomic DNA with guanidium thiocyanate
    • Pitcher D.G., Saunders N.A., Owen R.J. Rapid extraction of bacterial genomic DNA with guanidium thiocyanate. Lett Appl Microbiol 1989, 8:151-156.
    • (1989) Lett Appl Microbiol , vol.8 , pp. 151-156
    • Pitcher, D.G.1    Saunders, N.A.2    Owen, R.J.3
  • 19
    • 0004270170 scopus 로고    scopus 로고
    • John Wiley & Sons, Inc., New York, F.M. Ausubel, R. Brent, R.E. Kingston, F.M. Ausubel, R. Brent, R.E. Kingston (Eds.)
    • Current protocols in molecular biology 1999, John Wiley & Sons, Inc., New York. F.M. Ausubel, R. Brent, R.E. Kingston, F.M. Ausubel, R. Brent, R.E. Kingston (Eds.).
    • (1999) Current protocols in molecular biology
  • 20
    • 0035875343 scopus 로고    scopus 로고
    • GeneMarkS: a self-training method for prediction of gene starts in microbial genomes. implications for finding sequence motifs in regulatory regions
    • Besemer J., Lomsadze A., Borodovsky M. GeneMarkS: a self-training method for prediction of gene starts in microbial genomes. implications for finding sequence motifs in regulatory regions. Nucleic Acids Res 2001, 29(12):2607-2618.
    • (2001) Nucleic Acids Res , vol.29 , Issue.12 , pp. 2607-2618
    • Besemer, J.1    Lomsadze, A.2    Borodovsky, M.3
  • 21
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen J.D., Nielsen H., von Heijne G., Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 2004, 340(4):783-795.
    • (2004) J Mol Biol , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 22
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy J.L., Laird M.R., Chen F., et al. PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 2005, 21:617-623.
    • (2005) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3
  • 23
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994, 22(22):4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 24
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 25(24):4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 25
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: an application to display phylogenetic trees on personal computers
    • Page R.D. TreeView: an application to display phylogenetic trees on personal computers. Comput Appl Biosci 1996, 12(4):357-358.
    • (1996) Comput Appl Biosci , vol.12 , Issue.4 , pp. 357-358
    • Page, R.D.1
  • 26
    • 0030722136 scopus 로고    scopus 로고
    • Beta2 toxin, a novel toxin produced by Clostridium perfringens
    • Gibert M., Jolivet-Reynaud C., Popoff M.R., Jolivet-Renaud C. Beta2 toxin, a novel toxin produced by Clostridium perfringens. Gene 1997, 203(1):65-73.
    • (1997) Gene , vol.203 , Issue.1 , pp. 65-73
    • Gibert, M.1    Jolivet-Reynaud, C.2    Popoff, M.R.3    Jolivet-Renaud, C.4
  • 27
    • 0032841470 scopus 로고    scopus 로고
    • Characterization of apxIVA, a new RTX determinant of Actinobacillus pleuropneumoniae
    • Schaller A., Kuhn R., Kuhnert P., et al. Characterization of apxIVA, a new RTX determinant of Actinobacillus pleuropneumoniae. Microbiology 1999, 145:2105-2116.
    • (1999) Microbiology , vol.145 , pp. 2105-2116
    • Schaller, A.1    Kuhn, R.2    Kuhnert, P.3
  • 28
    • 25144494029 scopus 로고    scopus 로고
    • A metabolic enzyme as a primary virulence factor of Mycoplasma mycoides subsp. mycoides small colony
    • Pilo P., Vilei E.M., Peterhans E., et al. A metabolic enzyme as a primary virulence factor of Mycoplasma mycoides subsp. mycoides small colony. J Bacteriol 2005, 187(19):6824-6831.
    • (2005) J Bacteriol , vol.187 , Issue.19 , pp. 6824-6831
    • Pilo, P.1    Vilei, E.M.2    Peterhans, E.3
  • 29
    • 0023744105 scopus 로고
    • Purification and partial characterization of a hemolysin produced by Actinobacillus pleuropneumoniae type strain 4074
    • Frey J., Nicolet J. Purification and partial characterization of a hemolysin produced by Actinobacillus pleuropneumoniae type strain 4074. FEMS Microbiol Lett 1988, 55:41-46.
    • (1988) FEMS Microbiol Lett , vol.55 , pp. 41-46
    • Frey, J.1    Nicolet, J.2
  • 30
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul S.F., Madden T.L., Schäffer A.A., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25(17):3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schäffer, A.A.3
  • 31
    • 3242876302 scopus 로고    scopus 로고
    • Proteome analyst: custom predictions with explanations in a web-based tool for high-throughput proteome annotations
    • Web Server issue
    • Szafron D., Lu P., Greiner R., et al. Proteome analyst: custom predictions with explanations in a web-based tool for high-throughput proteome annotations. Nucleic Acids Res 2004, 32(Web Server issue):W365-W371.
    • (2004) Nucleic Acids Res , vol.32
    • Szafron, D.1    Lu, P.2    Greiner, R.3
  • 32
    • 79953870583 scopus 로고    scopus 로고
    • Clostridium botulinum group III: a group with dual identity shaped by plasmids, phages and mobile elements
    • Skarin H., Hafstrom T., Westerberg J., Segerman B. Clostridium botulinum group III: a group with dual identity shaped by plasmids, phages and mobile elements. BMC Genomics 2011, 12:185.
    • (2011) BMC Genomics , vol.12 , pp. 185
    • Skarin, H.1    Hafstrom, T.2    Westerberg, J.3    Segerman, B.4
  • 33
    • 40349113428 scopus 로고    scopus 로고
    • NetB, a new toxin that is associated with avian necrotic enteritis caused by Clostridium perfringens
    • Keyburn A.L., Boyce J.D., Vaz P., et al. NetB, a new toxin that is associated with avian necrotic enteritis caused by Clostridium perfringens. PLoS Pathog 2008, 4(2):e26.
    • (2008) PLoS Pathog , vol.4 , Issue.2
    • Keyburn, A.L.1    Boyce, J.D.2    Vaz, P.3
  • 34
    • 0027214133 scopus 로고
    • Molecular genetic analysis of beta-toxin of Clostridium perfringens reveals sequence homology with alpha-toxin, gamma-toxin, and leukocidin of Staphylococcus aureus
    • Hunter S.E., Brown J.E., Oyston P.C., Sakurai J., Titball R.W. Molecular genetic analysis of beta-toxin of Clostridium perfringens reveals sequence homology with alpha-toxin, gamma-toxin, and leukocidin of Staphylococcus aureus. Infect Immun 1993, 61:3958-3965.
    • (1993) Infect Immun , vol.61 , pp. 3958-3965
    • Hunter, S.E.1    Brown, J.E.2    Oyston, P.C.3    Sakurai, J.4    Titball, R.W.5
  • 35
    • 0038752612 scopus 로고    scopus 로고
    • Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis
    • Ivanova N., Sorokin A., Anderson I., et al. Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis. Nature 2003, 423(6935):87-91.
    • (2003) Nature , vol.423 , Issue.6935 , pp. 87-91
    • Ivanova, N.1    Sorokin, A.2    Anderson, I.3
  • 36
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., Gouaux J.E. Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 1996, 274(5294):1859-1866.
    • (1996) Science , vol.274 , Issue.5294 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 37
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • Hammarström M., Hellgren N., van den Berg S., Berglund H., Härd T. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci 2002, 11(2):313-321.
    • (2002) Protein Sci , vol.11 , Issue.2 , pp. 313-321
    • Hammarström, M.1    Hellgren, N.2    van den Berg, S.3    Berglund, H.4    Härd, T.5
  • 38
    • 0032963482 scopus 로고    scopus 로고
    • Clostridium perfringens beta-toxin is sensitive to thiol-group modification but does not require a thiol group for lethal activity
    • Nagahama M., Kihara A., Miyawaki T., et al. Clostridium perfringens beta-toxin is sensitive to thiol-group modification but does not require a thiol group for lethal activity. Biochim Biophys Acta 1999, 1454(1):97-105.
    • (1999) Biochim Biophys Acta , vol.1454 , Issue.1 , pp. 97-105
    • Nagahama, M.1    Kihara, A.2    Miyawaki, T.3
  • 39
    • 0031887515 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Clostridium perfringens beta-toxin: expression of wild-type and mutant toxins in Bacillus subtilis
    • Steinthorsdottir V., Fridriksdottir V., Gunnarsson E., Andresson O.S. Site-directed mutagenesis of Clostridium perfringens beta-toxin: expression of wild-type and mutant toxins in Bacillus subtilis. FEMS Microbiol Lett 1998, 158(1):17-23.
    • (1998) FEMS Microbiol Lett , vol.158 , Issue.1 , pp. 17-23
    • Steinthorsdottir, V.1    Fridriksdottir, V.2    Gunnarsson, E.3    Andresson, O.S.4
  • 40
    • 0029125825 scopus 로고
    • Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification
    • Walker B., Bayley H. Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification. J Biol Chem 1995, 270(39):23065-23071.
    • (1995) J Biol Chem , vol.270 , Issue.39 , pp. 23065-23071
    • Walker, B.1    Bayley, H.2
  • 41
    • 0028978519 scopus 로고
    • Restoration of pore-forming activity in staphylococcal alpha-hemolysin by targeted covalent modification
    • Walker B., Bayley H. Restoration of pore-forming activity in staphylococcal alpha-hemolysin by targeted covalent modification. Protein Eng 1995, 8:491-495.
    • (1995) Protein Eng , vol.8 , pp. 491-495
    • Walker, B.1    Bayley, H.2
  • 42
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


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