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Volumn 42, Issue 1, 2007, Pages 36-45

Effect of fish skin mucus on the soluble proteome of Vibrio salmonicida analysed by 2-D gel electrophoresis and tandem mass spectrometry

Author keywords

Proteomic analysis; Skin mucus; Vibrio salmonicida

Indexed keywords

CHAPERONIN; FLAGELLAR PROTEIN C; FLAGELLAR PROTEIN D; FLAGELLAR PROTEIN E; HEAT SHOCK PROTEIN; PEROXIDASE; PROTEIN; PROTEIN DNAK; PROTEOME; THIOL OXIDASE;

EID: 33845390354     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2006.10.003     Document Type: Article
Times cited : (47)

References (52)
  • 2
    • 58149204639 scopus 로고
    • Two serotype of Vibrio salmonicida isolated from diseased cod (Gadus morhua L.); virulence, immunological studies and vaccination experiments
    • Schrøder M.B., Espelid S., and Jørgensen T. Two serotype of Vibrio salmonicida isolated from diseased cod (Gadus morhua L.); virulence, immunological studies and vaccination experiments. Fish Shellfish Immunol 2 (1992) 211-221
    • (1992) Fish Shellfish Immunol , vol.2 , pp. 211-221
    • Schrøder, M.B.1    Espelid, S.2    Jørgensen, T.3
  • 4
    • 33845439809 scopus 로고
    • Vibrio salmonicida isolated from farmed Atlantic salmon in the Faroe Islands
    • Dalsgaard I., Jurgens O., and Mortensen A. Vibrio salmonicida isolated from farmed Atlantic salmon in the Faroe Islands. Bull Eur Assoc Fish Pathol 8 (1988) 53-54
    • (1988) Bull Eur Assoc Fish Pathol , vol.8 , pp. 53-54
    • Dalsgaard, I.1    Jurgens, O.2    Mortensen, A.3
  • 5
    • 0005095577 scopus 로고
    • Vibrio salmonicida (Hitra disease) in New Brunswick
    • O′Halloran J., and Henry R. Vibrio salmonicida (Hitra disease) in New Brunswick. Bull Aqua Assoc Ca 93 (1993) 96-98
    • (1993) Bull Aqua Assoc Ca , vol.93 , pp. 96-98
    • OHalloran, J.1    Henry, R.2
  • 6
    • 0025919589 scopus 로고
    • Seasonal variation in the presence of Vibrio salmonicida and total bacterial counts in Norwegian fish-farm water
    • Enger Ø., Husevåg B., and Goksøyr J. Seasonal variation in the presence of Vibrio salmonicida and total bacterial counts in Norwegian fish-farm water. Can J Microbiol 37 (1991) 618-623
    • (1991) Can J Microbiol , vol.37 , pp. 618-623
    • Enger, Ø.1    Husevåg, B.2    Goksøyr, J.3
  • 8
    • 85007874886 scopus 로고
    • Charateristics of a Vibrio sp. associated with the 'Hitra disease' of Atlantic salmon in Norwegian fish farms
    • Holm K.O., Strøm E., Stenvåg K., Raa J., and Jørgensen T. Charateristics of a Vibrio sp. associated with the 'Hitra disease' of Atlantic salmon in Norwegian fish farms. Fish Pathol 20 (1985) 125-129
    • (1985) Fish Pathol , vol.20 , pp. 125-129
    • Holm, K.O.1    Strøm, E.2    Stenvåg, K.3    Raa, J.4    Jørgensen, T.5
  • 9
    • 0015926145 scopus 로고
    • Lysozyme activity in plaice (Pleuronectes platessa L.)
    • Fletcher T.C., and White A. Lysozyme activity in plaice (Pleuronectes platessa L.). Experientia 29 (1973) 1283-1285
    • (1973) Experientia , vol.29 , pp. 1283-1285
    • Fletcher, T.C.1    White, A.2
  • 10
    • 0030957967 scopus 로고    scopus 로고
    • Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder
    • Cole A.M., Weis P., and Diamond G. Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J Biol Chem 272 (1997) 1208-12013
    • (1997) J Biol Chem , vol.272 , pp. 1208-12013
    • Cole, A.M.1    Weis, P.2    Diamond, G.3
  • 11
    • 49649145498 scopus 로고
    • Antibody production in the plaice Pleuronectes platessa after oral and parenteral immunisation with Vibrio anguillarum antigens
    • Fletcher T.C., and White A. Antibody production in the plaice Pleuronectes platessa after oral and parenteral immunisation with Vibrio anguillarum antigens. Aquaculture 1 (1973) 417-428
    • (1973) Aquaculture , vol.1 , pp. 417-428
    • Fletcher, T.C.1    White, A.2
  • 12
    • 0033382041 scopus 로고    scopus 로고
    • In situ adherence of Vibrio spp. to cryosections of Atlantic salmon, Salmo salar L., tissue
    • Knudsen G., Sørum H., Press C.M.L., and Olafsen J.A. In situ adherence of Vibrio spp. to cryosections of Atlantic salmon, Salmo salar L., tissue. J Fish Dis 22 (1999) 409-418
    • (1999) J Fish Dis , vol.22 , pp. 409-418
    • Knudsen, G.1    Sørum, H.2    Press, C.M.L.3    Olafsen, J.A.4
  • 14
    • 3242790338 scopus 로고    scopus 로고
    • Regulation of Vibrio anguillarum empA metalloprotease expression and its role in virulence
    • Denkin S.M., and Nelson D.R. Regulation of Vibrio anguillarum empA metalloprotease expression and its role in virulence. Appl Environ Microbiol 70 (2004) 4193-4204
    • (2004) Appl Environ Microbiol , vol.70 , pp. 4193-4204
    • Denkin, S.M.1    Nelson, D.R.2
  • 15
    • 0032802152 scopus 로고    scopus 로고
    • Induction of arotease activity in Vibrio anguillarum by gastrointestinal mucus
    • Denkin S.M., and Nelson D.R. Induction of arotease activity in Vibrio anguillarum by gastrointestinal mucus. Appl Environ Microbiol 65 (1999) 3555-3560
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3555-3560
    • Denkin, S.M.1    Nelson, D.R.2
  • 16
    • 0030741128 scopus 로고    scopus 로고
    • Roles of motility in bacterial-host interactions
    • Otteman K.M., and Miller J.F. Roles of motility in bacterial-host interactions. Mol Microbiol 24 (1997) 1106-1117
    • (1997) Mol Microbiol , vol.24 , pp. 1106-1117
    • Otteman, K.M.1    Miller, J.F.2
  • 17
    • 0038013943 scopus 로고    scopus 로고
    • From motility to virulence: sensing and responding to environmental signals in Vibrio cholerae
    • Krukonis E.S., and DiRita V.J. From motility to virulence: sensing and responding to environmental signals in Vibrio cholerae. Curr Opin Microbiol 6 (2003) 186-190
    • (2003) Curr Opin Microbiol , vol.6 , pp. 186-190
    • Krukonis, E.S.1    DiRita, V.J.2
  • 19
    • 0032807472 scopus 로고    scopus 로고
    • The chemotactic response of Vibrio angillarum to fish intestinal mucus is mediated by a combination of multiple mucus components
    • O'Toole R., Lundeberg S., Fredriksson S.A., Jansson A., Jansson B., Nilsson B., et al. The chemotactic response of Vibrio angillarum to fish intestinal mucus is mediated by a combination of multiple mucus components. J Bacteriol 181 (1999) 4308-4317
    • (1999) J Bacteriol , vol.181 , pp. 4308-4317
    • O'Toole, R.1    Lundeberg, S.2    Fredriksson, S.A.3    Jansson, A.4    Jansson, B.5    Nilsson, B.6
  • 21
    • 22844435410 scopus 로고    scopus 로고
    • Innate immunity of fish (overview)
    • Magnadottir B. Innate immunity of fish (overview). Fish Shellfish Immunol 20 (2006) 137-151
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 137-151
    • Magnadottir, B.1
  • 22
    • 0010573067 scopus 로고
    • Lysozyme from rainbow trout, Salmo gairdneri Richardson, as an antibacterial agent against fish pathogens
    • Grinde B. Lysozyme from rainbow trout, Salmo gairdneri Richardson, as an antibacterial agent against fish pathogens. J Fish Dis 12 (1989) 95-104
    • (1989) J Fish Dis , vol.12 , pp. 95-104
    • Grinde, B.1
  • 24
    • 0028874411 scopus 로고
    • Growth of Escherichia coli K88 in piglet ileal mucus: protein expression as an indicator of type of metabolism
    • Blomberg L., Gustafsson L., Cohen P.S., Conway P.L., and Blomberg A. Growth of Escherichia coli K88 in piglet ileal mucus: protein expression as an indicator of type of metabolism. J Bacteriol 177 (1995) 6695-6703
    • (1995) J Bacteriol , vol.177 , pp. 6695-6703
    • Blomberg, L.1    Gustafsson, L.2    Cohen, P.S.3    Conway, P.L.4    Blomberg, A.5
  • 25
    • 0026642506 scopus 로고
    • A 66-Kd heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus
    • Ensgraber M., and Loos M. A 66-Kd heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus. Infect Immun 60 (1992) 3072-3078
    • (1992) Infect Immun , vol.60 , pp. 3072-3078
    • Ensgraber, M.1    Loos, M.2
  • 26
    • 0027285297 scopus 로고
    • Pathogenicity of Heliobacter pylori: a perspective
    • Lee A., Fox J., and Hazell S. Pathogenicity of Heliobacter pylori: a perspective. Infect Immun 61 (1993) 1601-1610
    • (1993) Infect Immun , vol.61 , pp. 1601-1610
    • Lee, A.1    Fox, J.2    Hazell, S.3
  • 27
    • 0030728057 scopus 로고    scopus 로고
    • Mucobacterium tuberculosis chaperonin 10 stimulates bone resorption: a contributory factor in Pott's disease
    • Meghji S., White P.A., Nair S.P., Reddi K., Heron K., Henderson B., et al. Mucobacterium tuberculosis chaperonin 10 stimulates bone resorption: a contributory factor in Pott's disease. J Exp Med 186 (1997) 1241-1246
    • (1997) J Exp Med , vol.186 , pp. 1241-1246
    • Meghji, S.1    White, P.A.2    Nair, S.P.3    Reddi, K.4    Heron, K.5    Henderson, B.6
  • 28
    • 0026021812 scopus 로고
    • The role of a stress-response protein in Salmonella typhimurium virulence
    • Johnson K., Charles I., Dougan G., Pickard D., O'Gaora P., Costa G., et al. The role of a stress-response protein in Salmonella typhimurium virulence. Mol Microb 5 (1991) 401-407
    • (1991) Mol Microb , vol.5 , pp. 401-407
    • Johnson, K.1    Charles, I.2    Dougan, G.3    Pickard, D.4    O'Gaora, P.5    Costa, G.6
  • 29
    • 0025029317 scopus 로고
    • Synthesis of species-specific stress proteins by virulent strains of Listeria monocytogenes
    • Sokolovic Z., Fuchs A., and Goebel W. Synthesis of species-specific stress proteins by virulent strains of Listeria monocytogenes. Infect Immun 58 (1990) 3582-3587
    • (1990) Infect Immun , vol.58 , pp. 3582-3587
    • Sokolovic, Z.1    Fuchs, A.2    Goebel, W.3
  • 30
    • 0025294377 scopus 로고
    • Characterization of the heat shock response and identification of heat shock protein antigens of Borrelia burgdorferi
    • Carreiro M.M., Laux D.C., and Nelson D.R. Characterization of the heat shock response and identification of heat shock protein antigens of Borrelia burgdorferi. Infect Immun 58 (1990) 2186-2191
    • (1990) Infect Immun , vol.58 , pp. 2186-2191
    • Carreiro, M.M.1    Laux, D.C.2    Nelson, D.R.3
  • 31
    • 0028028165 scopus 로고
    • Heat shock response and heat shock protein antigens of Vibrio cholerae
    • Sahu G.K., Chowdhury R., and Das J. Heat shock response and heat shock protein antigens of Vibrio cholerae. Infect Immun 62 (1994) 5624-5631
    • (1994) Infect Immun , vol.62 , pp. 5624-5631
    • Sahu, G.K.1    Chowdhury, R.2    Das, J.3
  • 32
    • 0023839992 scopus 로고
    • A heat shock operon in Coxiella burnetti produces a major antigen homologous to a protein in both mycobacteria and Escherichia coli
    • Vodkin M.H., and Williams J.C. A heat shock operon in Coxiella burnetti produces a major antigen homologous to a protein in both mycobacteria and Escherichia coli. J Bacteriol 170 (1988) 1227-1234
    • (1988) J Bacteriol , vol.170 , pp. 1227-1234
    • Vodkin, M.H.1    Williams, J.C.2
  • 33
    • 0024418447 scopus 로고
    • Stress proteins, infection, and immune surveillance
    • Young R.A., and Elliot T.J. Stress proteins, infection, and immune surveillance. Cell 59 (1989) 5-8
    • (1989) Cell , vol.59 , pp. 5-8
    • Young, R.A.1    Elliot, T.J.2
  • 34
    • 0033015775 scopus 로고    scopus 로고
    • Role of DnaK in in vitro and in vivo expression of virulence factors of Vibrio cholerae
    • Chakrabarti S., Sengupta N., and Rukhsana C. Role of DnaK in in vitro and in vivo expression of virulence factors of Vibrio cholerae. Infect Immun 67 (1999) 1025-1033
    • (1999) Infect Immun , vol.67 , pp. 1025-1033
    • Chakrabarti, S.1    Sengupta, N.2    Rukhsana, C.3
  • 35
    • 0031951605 scopus 로고    scopus 로고
    • Differential regulation of multiple flagellins in Vibrio cholerae
    • Klose K.E., and Mekalanos J.J. Differential regulation of multiple flagellins in Vibrio cholerae. J Bacteriol 180 (1998) 303-316
    • (1998) J Bacteriol , vol.180 , pp. 303-316
    • Klose, K.E.1    Mekalanos, J.J.2
  • 36
    • 0028957972 scopus 로고
    • Genetic and molecular characterization of the polar flagellum of Vibrio parahaemolyticus
    • McCarter L.L. Genetic and molecular characterization of the polar flagellum of Vibrio parahaemolyticus. J Bacteriol 177 (1995) 1595-1609
    • (1995) J Bacteriol , vol.177 , pp. 1595-1609
    • McCarter, L.L.1
  • 37
    • 0029835581 scopus 로고    scopus 로고
    • Identification and characterization of additional flagellin genes from Vibrio anguillarum
    • McGee K., Horstedt P., and Milton D. Identification and characterization of additional flagellin genes from Vibrio anguillarum. J Bacteriol 178 (1996) 5188-5198
    • (1996) J Bacteriol , vol.178 , pp. 5188-5198
    • McGee, K.1    Horstedt, P.2    Milton, D.3
  • 38
    • 3042611950 scopus 로고    scopus 로고
    • Vibrio fischeri flagellin A is essential for normal motility and for symbiotic competence during initial squid light organ colonization
    • Millikan D.S., and Ruby E.G. Vibrio fischeri flagellin A is essential for normal motility and for symbiotic competence during initial squid light organ colonization. J Bacteriol 186 (2004) 4315-4325
    • (2004) J Bacteriol , vol.186 , pp. 4315-4325
    • Millikan, D.S.1    Ruby, E.G.2
  • 39
    • 0020639220 scopus 로고
    • The role of the flagellum in the adherence of Vibrio cholera
    • Attridge S.R., and Rowley D. The role of the flagellum in the adherence of Vibrio cholera. J Infect Dis 147 (1983) 864-872
    • (1983) J Infect Dis , vol.147 , pp. 864-872
    • Attridge, S.R.1    Rowley, D.2
  • 40
    • 0023901517 scopus 로고
    • Flagella, motility and invasive virulence of Pseudomonas aeruginosa
    • Drake D., and Montie T.C. Flagella, motility and invasive virulence of Pseudomonas aeruginosa. J Gen Microbiol 134 (1988) 43-52
    • (1988) J Gen Microbiol , vol.134 , pp. 43-52
    • Drake, D.1    Montie, T.C.2
  • 41
    • 29644433083 scopus 로고    scopus 로고
    • A bacterial flagellin, Vibrio vulnificus FlaB, has a strong mucosal adjuvant activity to induce protective immunity
    • Lee S.E., Kim S.Y., Jeong B.C., Kim Y.R., Bae S.J., Ahn O.S., et al. A bacterial flagellin, Vibrio vulnificus FlaB, has a strong mucosal adjuvant activity to induce protective immunity. Infect Immun 74 (2006) 694-702
    • (2006) Infect Immun , vol.74 , pp. 694-702
    • Lee, S.E.1    Kim, S.Y.2    Jeong, B.C.3    Kim, Y.R.4    Bae, S.J.5    Ahn, O.S.6
  • 42
    • 0029913592 scopus 로고    scopus 로고
    • Flagellin A is essential for the virulence of Vibrio anguillarum
    • Milton D., O'Toole R., Horstedt P., and Wolf-Watz H. Flagellin A is essential for the virulence of Vibrio anguillarum. J Bacteriol 178 (1996) 1310-1319
    • (1996) J Bacteriol , vol.178 , pp. 1310-1319
    • Milton, D.1    O'Toole, R.2    Horstedt, P.3    Wolf-Watz, H.4
  • 43
    • 0022634633 scopus 로고
    • Campylobacter pyloridis and gastritis: association with inter-cellular spaces and adaptation to an environment of mucus as important factors in colonization of the gastric epithelium
    • Hazell S.L., Lee A., Brady L., and Hennessy W. Campylobacter pyloridis and gastritis: association with inter-cellular spaces and adaptation to an environment of mucus as important factors in colonization of the gastric epithelium. J Infect Dis 153 (1986) 658-663
    • (1986) J Infect Dis , vol.153 , pp. 658-663
    • Hazell, S.L.1    Lee, A.2    Brady, L.3    Hennessy, W.4
  • 45
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Eschetichia coli
    • Seaver L.C., and Implay J.A. Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Eschetichia coli. J Bacteriol 183 (2001) 7173-7181
    • (2001) J Bacteriol , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Implay, J.A.2
  • 46
    • 1642483650 scopus 로고    scopus 로고
    • Vibrio cholerae thiol peroxidase-glutaredoxin fusion is a 2-Cys TSA/AhpC subfamily acting as a lipid hydroperoxide reductase
    • Cha M.-K., Hong S.-K., Lee D.-S., and Kim I.-H. Vibrio cholerae thiol peroxidase-glutaredoxin fusion is a 2-Cys TSA/AhpC subfamily acting as a lipid hydroperoxide reductase. J Biol Chem 279 (2004) 11035-11041
    • (2004) J Biol Chem , vol.279 , pp. 11035-11041
    • Cha, M.-K.1    Hong, S.-K.2    Lee, D.-S.3    Kim, I.-H.4
  • 47
    • 0033991496 scopus 로고    scopus 로고
    • Redox sensing by prokaryotic transcription factors
    • Zheng M., and Storz G. Redox sensing by prokaryotic transcription factors. Biochem Pharmacol 59 (2000) 1-6
    • (2000) Biochem Pharmacol , vol.59 , pp. 1-6
    • Zheng, M.1    Storz, G.2
  • 49
    • 0028590012 scopus 로고
    • Characterization of the 5′ region of the Atlantic salmon (Salmo salar) transferrin-encoding gene
    • Kvingedal A.M. Characterization of the 5′ region of the Atlantic salmon (Salmo salar) transferrin-encoding gene. Gene 150 (1994) 335-339
    • (1994) Gene , vol.150 , pp. 335-339
    • Kvingedal, A.M.1
  • 50
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt Biochem 72 (1976) 248-254
    • (1976) Analyt Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 51
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell P.H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250 (1975) 4007-4021
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 52
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Lammeli U.K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Lammeli, U.K.1


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