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Volumn 72, Issue 7, 2006, Pages 4845-4852

A protective immune response is generated in rainbow trout by an OmpH-like surface antigen (P18) of Flavobacterium psychrophilum

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGENS; BACTERIA; IMMUNOLOGY; ION EXCHANGE; NEGATIVE IONS; PROTEINS;

EID: 33746083229     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00279-06     Document Type: Article
Times cited : (42)

References (47)
  • 2
    • 0001326017 scopus 로고
    • Study of a bacteriophage infecting the myxobacterium Chondrococcus columnaris
    • Anacker, R. L., and E. J. Ordal. 1955. Study of a bacteriophage infecting the myxobacterium Chondrococcus columnaris. J. Bacteriol. 70:738-741.
    • (1955) J. Bacteriol. , vol.70 , pp. 738-741
    • Anacker, R.L.1    Ordal, E.J.2
  • 3
    • 0032822659 scopus 로고    scopus 로고
    • Use of primate model system to identify Chlamydia trachomatis protein antigens recognized uniquely in the context of infection
    • Bannantine, J. P., and D. D. Rockey. 1999. Use of primate model system to identify Chlamydia trachomatis protein antigens recognized uniquely in the context of infection. Microbiology 145:2077-2085.
    • (1999) Microbiology , vol.145 , pp. 2077-2085
    • Bannantine, J.P.1    Rockey, D.D.2
  • 5
    • 0030052649 scopus 로고    scopus 로고
    • Cutting a gordian knot: Emended classification and description of the genus Flavobacterium, emended description of the family Flavobacteriaceae, and proposal of Flavobacterium hydatis nom. nov. (basonym, Cytophaga aquatilis Strohl and Tait 1978)
    • Bernardet, J.-F., P. Segers, M. Vancanneyt, F. Berthe, K. Kersters, and P. Vandamme. 1996. Cutting a gordian knot: emended classification and description of the genus Flavobacterium, emended description of the family Flavobacteriaceae, and proposal of Flavobacterium hydatis nom. nov. (basonym, Cytophaga aquatilis Strohl and Tait 1978). Int. J. Syst. Bacteriol. 46:128-148.
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 128-148
    • Bernardet, J.-F.1    Segers, P.2    Vancanneyt, M.3    Berthe, F.4    Kersters, K.5    Vandamme, P.6
  • 6
    • 0035989637 scopus 로고    scopus 로고
    • Proposed minimal standards for describing new taxa of the family Flavobacteriaceae and emended description of the family
    • Bernardet, J.-F., Y. Nakagawa, and B. Holmes. 2002. Proposed minimal standards for describing new taxa of the family Flavobacteriaceae and emended description of the family. Int. J. Syst. Evol. Microbiol. 52:1049-1070.
    • (2002) Int. J. Syst. Evol. Microbiol. , vol.52 , pp. 1049-1070
    • Bernardet, J.-F.1    Nakagawa, Y.2    Holmes, B.3
  • 8
    • 16844381967 scopus 로고    scopus 로고
    • Flavobacterium johnsoniae GldJ is a lipoprotein that is required for gliding motility
    • Braun, T. F., and M. J. McBride. 2005. Flavobacterium johnsoniae GldJ is a lipoprotein that is required for gliding motility. J. Bacteriol. 187:2628-2637.
    • (2005) J. Bacteriol. , vol.187 , pp. 2628-2637
    • Braun, T.F.1    McBride, M.J.2
  • 9
    • 0034691928 scopus 로고    scopus 로고
    • Antimicrobial resistance patterns in Danish isolates of Flavobacterium psychrophilum
    • Bruun, M. S., A. S. Schimdt, L. Madsen, and I. Dalsgaard. 2000. Antimicrobial resistance patterns in Danish isolates of Flavobacterium psychrophilum. Aquaculture 189:201-212.
    • (2000) Aquaculture , vol.189 , pp. 201-212
    • Bruun, M.S.1    Schimdt, A.S.2    Madsen, L.3    Dalsgaard, I.4
  • 10
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • Bulieris, P. V., S. Behrens, O. Holst, and J. H. Kleinschmidt. 2003. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J. Biol. Chem. 278:9092-9099.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 11
    • 0035144167 scopus 로고    scopus 로고
    • Antigenic characterization of the fish pathogen Flavobacterium psychrophilum
    • Crump, E. M., M. B. Perry, S. C. Clouthier, and W. W. Kay. 2001. Antigenic characterization of the fish pathogen Flavobacterium psychrophilum. Appl. Environ. Microbiol. 67:750-759.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 750-759
    • Crump, E.M.1    Perry, M.B.2    Clouthier, S.C.3    Kay, W.W.4
  • 12
    • 24944490999 scopus 로고    scopus 로고
    • Identification and expression of a host-recognized antigen, FspA, from Flavobacterium psychrophilum
    • Crump, E. M., J. Burian, P. D. Allen, and W. W. Kay. 2005. Identification and expression of a host-recognized antigen, FspA, from Flavobacterium psychrophilum. Microbiology 151:3127-3135.
    • (2005) Microbiology , vol.151 , pp. 3127-3135
    • Crump, E.M.1    Burian, J.2    Allen, P.D.3    Kay, W.W.4
  • 13
    • 0033820548 scopus 로고    scopus 로고
    • Bacterial pathogens in rainbow trout, Oncorhynchus mykiss (Walbaum), reared at Danish freshwater farms
    • Dalsgaard, I., and L. Madsen. 2000. Bacterial pathogens in rainbow trout, Oncorhynchus mykiss (Walbaum), reared at Danish freshwater farms. J. Fish Dis. 23:199-209.
    • (2000) J. Fish Dis. , vol.23 , pp. 199-209
    • Dalsgaard, I.1    Madsen, L.2
  • 15
    • 0025263809 scopus 로고
    • Bacterial 'histone-like protein I' (HLP-I) is an outer membrane constituent?
    • Hirvas, L., J. Coleman, P. Koski, and M. Vaara. 1990. Bacterial 'histone-like protein I' (HLP-I) is an outer membrane constituent? FEBS Lett. 262:123-126.
    • (1990) FEBS Lett. , vol.262 , pp. 123-126
    • Hirvas, L.1    Coleman, J.2    Koski, P.3    Vaara, M.4
  • 16
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning protein segments
    • Hofmann, K., and W. Stoffel. 1993. TMbase-a database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler 374:166.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 17
    • 0030485797 scopus 로고    scopus 로고
    • Outbreaks of coldwater disease in wild ayu and pale chub
    • Iida, Y., and A. Mizokami. 1996. Outbreaks of coldwater disease in wild ayu and pale chub. Fish Pathol. 31:157-164.
    • (1996) Fish Pathol. , vol.31 , pp. 157-164
    • Iida, Y.1    Mizokami, A.2
  • 18
    • 3242760833 scopus 로고    scopus 로고
    • Relationship between gyrA mutations and quinolone resistance in Flavobacterium psychrophilum isolates
    • Izumi, S., and F. Aranishi. 2004. Relationship between gyrA mutations and quinolone resistance in Flavobacterium psychrophilum isolates. Appl. Environ. Microbiol. 70:3968-3972.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3968-3972
    • Izumi, S.1    Aranishi, F.2
  • 19
    • 0042194957 scopus 로고    scopus 로고
    • Efficacy of oral vaccine against bacterial coldwater disease in ayu Plecoglossus altivelis
    • Kondo, M., K. Kawai, M. Okabe, N. Nakano, and S. Oshima. 2003. Efficacy of oral vaccine against bacterial coldwater disease in ayu Plecoglossus altivelis. Dis. Aquat. Organ. 55:261-264.
    • (2003) Dis. Aquat. Organ. , vol.55 , pp. 261-264
    • Kondo, M.1    Kawai, K.2    Okabe, M.3    Nakano, N.4    Oshima, S.5
  • 20
    • 0025280947 scopus 로고
    • Complete sequence of the ompH gene encoding the 16-kDa cationic outer membrane protein of Salmonella typhimurium
    • Koski, P., L. Hirvas, and M. Vaara. 1990. Complete sequence of the ompH gene encoding the 16-kDa cationic outer membrane protein of Salmonella typhimurium. Gene 88:117-120.
    • (1990) Gene , vol.88 , pp. 117-120
    • Koski, P.1    Hirvas, L.2    Vaara, M.3
  • 21
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 22
    • 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
  • 23
    • 0036927142 scopus 로고    scopus 로고
    • Characterization of serum and mucosal antibody responses and relative per cent survival in rainbow trout, Oncorhynchus mykiss (Walbaum), following immunization and challenge with Flavobacterium psychrophilum
    • LaFrentz, B. R., S. E. LaPatra, G. R. Jones, J. L. Congleton, B. Sun, and K. D. Cain. 2002. Characterization of serum and mucosal antibody responses and relative per cent survival in rainbow trout, Oncorhynchus mykiss (Walbaum), following immunization and challenge with Flavobacterium psychrophilum. J. Fish Dis. 25:703-713.
    • (2002) J. Fish Dis. , vol.25 , pp. 703-713
    • LaFrentz, B.R.1    LaPatra, S.E.2    Jones, G.R.3    Congleton, J.L.4    Sun, B.5    Cain, K.D.6
  • 24
    • 0042572310 scopus 로고    scopus 로고
    • Passive immunization of rainbow trout, Oncorhynchus mykiss (Walbaum), against Flavobacterium psychrophilum, the causative agent of bacterial coldwater disease and rainbow trout fry syndrome
    • LaFrentz, B. R., S. E. LaPatra, G. R. Jones, and K. D. Cain. 2003. Passive immunization of rainbow trout, Oncorhynchus mykiss (Walbaum), against Flavobacterium psychrophilum, the causative agent of bacterial coldwater disease and rainbow trout fry syndrome. J. Fish Dis. 26:371-384.
    • (2003) J. Fish Dis. , vol.26 , pp. 371-384
    • LaFrentz, B.R.1    LaPatra, S.E.2    Jones, G.R.3    Cain, K.D.4
  • 25
    • 3242771514 scopus 로고    scopus 로고
    • Protective immunity in rainbow trout Oncorhynchus mykiss following immunization with distinct molecular mass fractions isolated from Flavobacterium psychrophilum
    • LaFrentz, B. R., S. E. LaPatra, G. R. Jones, and K. D. Cain. 2004. Protective immunity in rainbow trout Oncorhynchus mykiss following immunization with distinct molecular mass fractions isolated from Flavobacterium psychrophilum. Dis. Aquat. Organ. 59:17-26.
    • (2004) Dis. Aquat. Organ. , vol.59 , pp. 17-26
    • LaFrentz, B.R.1    LaPatra, S.E.2    Jones, G.R.3    Cain, K.D.4
  • 26
    • 0000450352 scopus 로고
    • First isolation of Cytophaga psychrophila from a systemic disease in eel and cyprinids
    • Lehman, J., D. Mock, F. J. Stürenberg, and J.-F. Bernardet. 1991. First isolation of Cytophaga psychrophila from a systemic disease in eel and cyprinids. Dis. Aquat. Organ. 10:217-220.
    • (1991) Dis. Aquat. Organ. , vol.10 , pp. 217-220
    • Lehman, J.1    Mock, D.2    Stürenberg, F.J.3    Bernardet, J.-F.4
  • 28
    • 0034856934 scopus 로고    scopus 로고
    • The structure of the lipopolysaccharide O-antigen produced by Flavobacterium psychrophilum (259-93)
    • MacLean, L. L., E. Vinogradov, E. M. Crump, M. B. Perry, and W. W. Kay. 2001. The structure of the lipopolysaccharide O-antigen produced by Flavobacterium psychrophilum (259-93). Eur. J. Biochem. 268:2710-2716.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2710-2716
    • MacLean, L.L.1    Vinogradov, E.2    Crump, E.M.3    Perry, M.B.4    Kay, W.W.5
  • 29
    • 0002470618 scopus 로고    scopus 로고
    • Characterization of Flavobacterium psychrophilum: A comparison of proteolytic activity and virulence of strains isolated from rainbow trout (Oncorhynchus mykiss)
    • A. C. Barnes, G. A. Davidson, M. P. Hiney, and D. McIntosh (ed.). Fisheries Research Services, Aberdeen, United Kingdom
    • Madsen, L., and I. Dalsgaard. 1998. Characterization of Flavobacterium psychrophilum: a comparison of proteolytic activity and virulence of strains isolated from rainbow trout (Oncorhynchus mykiss), p. 45-52. In A. C. Barnes, G. A. Davidson, M. P. Hiney, and D. McIntosh (ed.), Methodology in fish diseases research. Fisheries Research Services, Aberdeen, United Kingdom.
    • (1998) Methodology in Fish Diseases Research , pp. 45-52
    • Madsen, L.1    Dalsgaard, I.2
  • 30
    • 4444288546 scopus 로고    scopus 로고
    • Identification of P18, a surface protein produced by the fish pathogen Flavobacterium psychrophilum
    • Massias, B., F. Dumetz, M.-C. Urdaci, and M. Le Hénaff. 2004. Identification of P18, a surface protein produced by the fish pathogen Flavobacterium psychrophilum. J. Appl. Microbiol. 97:574-580.
    • (2004) J. Appl. Microbiol. , vol.97 , pp. 574-580
    • Massias, B.1    Dumetz, F.2    Urdaci, M.-C.3    Le Hénaff, M.4
  • 31
    • 0038696158 scopus 로고    scopus 로고
    • Purification and characterization of a membrane glycoprotein from the fish pathogen Flavobacterium psychrophilum
    • Merle, C., D. Faure, M.-C. Urdaci, and M. Le Hénaff. 2003. Purification and characterization of a membrane glycoprotein from the fish pathogen Flavobacterium psychrophilum. J. Appl. Microbiol. 94:1120-1127.
    • (2003) J. Appl. Microbiol. , vol.94 , pp. 1120-1127
    • Merle, C.1    Faure, D.2    Urdaci, M.-C.3    Le Hénaff, M.4
  • 32
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA
    • Missiakas, D., J. M. Betton, and S. Raina. 1996. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA. FkpA and Skp/OmpH. Mol. Microbiol. 21:871-884.
    • (1996) FkpA and Skp/OmpH. Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 33
    • 0141816847 scopus 로고    scopus 로고
    • Involvement of a sialic acid-binding lectin with hemagglutination and hydrophobicity of Flavobacterium psychrophilum
    • Moller, J. D., J. L. Larsen, L. Madsen, and I. Dalsgaard. 2003. Involvement of a sialic acid-binding lectin with hemagglutination and hydrophobicity of Flavobacterium psychrophilum. Appl. Environ. Microbiol. 69:5275-5280.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5275-5280
    • Moller, J.D.1    Larsen, J.L.2    Madsen, L.3    Dalsgaard, I.4
  • 34
    • 20644457107 scopus 로고    scopus 로고
    • Characterisation of surface blebbing and membrane vesicles produced by Flavobacterium psychrophilum
    • Moller, J. D., A. C. Barnes, I. Dalsgaard, and A. E. Ellis. 2005. Characterisation of surface blebbing and membrane vesicles produced by Flavobacterium psychrophilum. Dis. Aquat. Organ. 64:201-209.
    • (2005) Dis. Aquat. Organ. , vol.64 , pp. 201-209
    • Moller, J.D.1    Barnes, A.C.2    Dalsgaard, I.3    Ellis, A.E.4
  • 36
    • 0030614959 scopus 로고    scopus 로고
    • Identification of procaryotic and eucaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of procaryotic and eucaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 37
    • 0025272240 scopus 로고
    • Rapid and sensitive sequence comparison with FASTP and FASTA
    • Pearson, W. R. 1990. Rapid and sensitive sequence comparison with FASTP and FASTA. Methods Enzymol. 183:63-98.
    • (1990) Methods Enzymol. , vol.183 , pp. 63-98
    • Pearson, W.R.1
  • 38
    • 0036166182 scopus 로고    scopus 로고
    • The outer membrane fraction of Flavobacterium psychrophilum induces protective immunity in rainbow trout and ayu
    • Rahman, H., A. Kuroda, J. M. Dijkstra, I. Kiryu, T. Nakanishi, and M. Ototake. 2002. The outer membrane fraction of Flavobacterium psychrophilum induces protective immunity in rainbow trout and ayu. Fish Shellfish Immunol. 12:169-179.
    • (2002) Fish Shellfish Immunol. , vol.12 , pp. 169-179
    • Rahman, H.1    Kuroda, A.2    Dijkstra, J.M.3    Kiryu, I.4    Nakanishi, T.5    Ototake, M.6
  • 40
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schäfer, U., K. Beck, and M. Muller. 1999. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 274:24567-24574.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schäfer, U.1    Beck, K.2    Muller, M.3
  • 41
    • 1842787813 scopus 로고    scopus 로고
    • The periplasmic E. coli chaperone Skp is a trimer in solution: Biophysical and preliminary crystallographic characterization
    • Schlapschy, M., M. K. Dommel, K. Hadian, M. Fogarasi, I. P. Korndorfer, and A. Skerra. 2004. The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization. Biol. Chem. 385:137-143.
    • (2004) Biol. Chem. , vol.385 , pp. 137-143
    • Schlapschy, M.1    Dommel, M.K.2    Hadian, K.3    Fogarasi, M.4    Korndorfer, I.P.5    Skerra, A.6
  • 42
    • 0033760554 scopus 로고    scopus 로고
    • Occurrence of antimicrobial resistance in fish-pathogenic and environmental bacteria associated with four Danish rainbow trout farms
    • Schmidt, A. S., M. S. Bruun, I. Dalsgaard, K. Pedersen, and J. L. Larsen. 2000. Occurrence of antimicrobial resistance in fish-pathogenic and environmental bacteria associated with four Danish rainbow trout farms. Appl. Environ. Microbiol. 66:4908-4915.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4908-4915
    • Schmidt, A.S.1    Bruun, M.S.2    Dalsgaard, I.3    Pedersen, K.4    Larsen, J.L.5
  • 43
    • 0035375081 scopus 로고    scopus 로고
    • Purification and characterization of a psychrophilic, calcium-induced, growth-phase-dependent metalloprotease from the fish pathogen Flavobacterium psychrophilum
    • Secades, P., B. Alvarez, and J. A. Guijarro. 2001. Purification and characterization of a psychrophilic, calcium-induced, growth-phase-dependent metalloprotease from the fish pathogen Flavobacterium psychrophilum. Appl. Environ. Microbiol. 67:2436-2444.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2436-2444
    • Secades, P.1    Alvarez, B.2    Guijarro, J.A.3
  • 44
    • 0642347021 scopus 로고    scopus 로고
    • Purification and properties of a new psychrophilic metalloprotease (Fpp2) in the fish pathogen Flavobacterium psychrophilum
    • Secades, P., B. Alvarez, and J. A. Guyarro. 2003. Purification and properties of a new psychrophilic metalloprotease (Fpp2) in the fish pathogen Flavobacterium psychrophilum. FEMS Microbiol. Lett. 226:273-279.
    • (2003) FEMS Microbiol. Lett. , vol.226 , pp. 273-279
    • Secades, P.1    Alvarez, B.2    Guyarro, J.A.3
  • 45
    • 0021266294 scopus 로고
    • Yet another improved staining method for the detection of proteins in polyacrylamide gels
    • Tunón, P., and K.-E. Johansson. 1984. Yet another improved staining method for the detection of proteins in polyacrylamide gels. J. Biochem. Biophys. Methods 9:171-179.
    • (1984) J. Biochem. Biophys. Methods , vol.9 , pp. 171-179
    • Tunón, P.1    Johansson, K.-E.2
  • 46
    • 27244446613 scopus 로고    scopus 로고
    • Type I signal peptidase: An overview
    • Tuteja, R. 2005. Type I signal peptidase: an overview. Arch. Biochem. Biophys. 441:107-111.
    • (2005) Arch. Biochem. Biophys. , vol.441 , pp. 107-111
    • Tuteja, R.1
  • 47
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • Walton, T. A., and M. C. Sousa. 2004. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol. Cell 15:367-374.
    • (2004) Mol. Cell , vol.15 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2


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