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Volumn 9, Issue , 2009, Pages

Differential proteomic analysis of Clostridium perfringens ATCC13124; Identification of dominant, surface and structure associated proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BUTYRYL COENZYME A DEHYDROGENASE; CHOLOYLGLYCINE HYDROLASE; CYSTATHIONINE BETA LYASE; ELECTRON TRANSFERRING FLAVOPROTEIN; ELONGATION FACTOR TU; ENVELOPE PROTEIN; FREUND ADJUVANT; GLUTAMATE SYNTHASE; GLYCOCHOLIC ACID; HYDROLYASE; MARKER; MEMBRANE PROTEIN; N ACETYLMURAMOYLALANINE AMIDASE; ORNITHINE CARBAMOYLTRANSFERASE; OXIDOREDUCTASE; PHOSPHOGLYCERATE KINASE; RIBOFLAVIN; RIBOFLAVIN BIOSYNTHESIS PROTEIN; RUBREDOXIN; SERINE PROTEINASE; STRUCTURAL PROTEIN; SUCROSE 6 PHOSPHATE DEHYDROGENASE; THREONINE DEHYDRATASE; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE; VACCINE; CYSTATHIONINE BETA-LYASE; LYASE; OUTER MEMBRANE PROTEIN; PROTEOME;

EID: 69449098311     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-9-162     Document Type: Article
Times cited : (33)

References (48)
  • 1
    • 50349128425 scopus 로고
    • Anaerobic infections of war wounds in the Middle East
    • Anaerobic infections of war wounds in the Middle East. JD MacLennan, Lancet 1943 ii 123 126
    • (1943) Lancet , vol.2 , pp. 123-126
    • MacLennan, J.D.1
  • 2
    • 0025824660 scopus 로고
    • Molecular genetics and pathogenesis of Clostridium perfringens
    • Molecular genetics and pathogenesis of Clostridium perfringens. IR Rood ST Cole, Microbiol Rev 1991 55 621 648
    • (1991) Microbiol Rev , vol.55 , pp. 621-648
    • Rood, I.R.1    Cole, S.T.2
  • 3
    • 33746298268 scopus 로고    scopus 로고
    • Clostridium perfringens wound infection
    • Newcastle, United Kingdom: Academic Press Sussman M
    • Clostridium perfringens wound infection. RW Titball JI Rood, Molecular Medical Microbiology Newcastle, United Kingdom: Academic Press, Sussman M, 2001 1875 1904
    • (2001) Molecular Medical Microbiology , pp. 1875-1904
    • Titball, R.W.1    Rood, J.I.2
  • 4
    • 69449095165 scopus 로고
    • An experimental evaluation of American commercial bivalent and pentavalent gas gangrene anti-toxins
    • An experimental evaluation of American commercial bivalent and pentavalent gas gangrene anti-toxins. IC Hall, Surg Gynecol Obstet 1945 81 487 499
    • (1945) Surg Gynecol Obstet , vol.81 , pp. 487-499
    • Hall, I.C.1
  • 5
    • 34547574258 scopus 로고    scopus 로고
    • Analysis of protection afforded by a Clostridium perfringens alpha-toxoid against heterologous clostridial phospholipases C
    • Analysis of protection afforded by a Clostridium perfringens alpha-toxoid against heterologous clostridial phospholipases C. BN Neeson GC Clark HS Atkins B Lingard RW Titball, Microb Pathog 2007 43 4 161 5
    • (2007) Microb Pathog , vol.43 , Issue.4 , pp. 161-5
    • Neeson, B.N.1    Clark, G.C.2    Atkins, H.S.3    Lingard, B.4    Titball, R.W.5
  • 6
    • 3943091070 scopus 로고    scopus 로고
    • Immunization with C-domain of -toxin prevents lethal infection, localizes tissue injury, and promotes host response to challenge with Clostridium perfringens
    • Immunization with C-domain of -toxin prevents lethal infection, localizes tissue injury, and promotes host response to challenge with Clostridium perfringens. DL Stevens RW Titball M Jepson CR Bayer SM Hayes-Scroer AE Bryant, J Infect Dis 2004 190 767 773
    • (2004) J Infect Dis , vol.190 , pp. 767-773
    • Stevens, D.L.1    Titball, R.W.2    Jepson, M.3    Bayer, C.R.4    Hayes-Scroer, S.M.5    Bryant, A.E.6
  • 8
    • 0036302998 scopus 로고    scopus 로고
    • Patterns of sequence conservation in the S-layer proteins and related sequences in Clostridium difficile
    • Patterns of sequence conservation in the S-layer proteins and related sequences in Clostridium difficile. E Calabi N Fairweather, J Bacteriol 2002 184 3886 3897
    • (2002) J Bacteriol , vol.184 , pp. 3886-3897
    • Calabi, E.1    Fairweather, N.2
  • 11
    • 0035915688 scopus 로고    scopus 로고
    • Association between antibody response to toxin A and protection against recurrent Clostridium difficile diarrhea
    • Association between antibody response to toxin A and protection against recurrent Clostridium difficile diarrhea. L Kyne M Warny A Qamar CP Kelly, Lancet 2001 357 189 193
    • (2001) Lancet , vol.357 , pp. 189-193
    • Kyne, L.1    Warny, M.2    Qamar, A.3    Kelly, C.P.4
  • 14
    • 26944469989 scopus 로고    scopus 로고
    • Variability of Clostridium difficile surface proteins and specific serum antibody response in patients with Clostridium difficile-associated disease
    • Variability of Clostridium difficile surface proteins and specific serum antibody response in patients with Clostridium difficile-associated disease. S Péchiné C Janoir A Collignon, J Clin Microbiol 2005 43 5018 5025
    • (2005) J Clin Microbiol , vol.43 , pp. 5018-5025
    • Péchiné, S.1    Janoir, C.2    Collignon, A.3
  • 15
    • 0024464275 scopus 로고
    • Temperature regulation of virulence genes in pathogenic bacteria: A general strategy for human pathogens?
    • Temperature regulation of virulence genes in pathogenic bacteria: a general strategy for human pathogens? AT Maurelli, Microb Pathog 1989 7 1 10
    • (1989) Microb Pathog , vol.7 , pp. 1-10
    • Maurelli, A.T.1
  • 16
    • 0027522569 scopus 로고
    • Influence of pH on bacterial gene expression
    • Influence of pH on bacterial gene expression. ER Olsen, Mol Microbiol 1993 8 5 14
    • (1993) Mol Microbiol , vol.8 , pp. 5-14
    • Olsen, E.R.1
  • 17
    • 0026445985 scopus 로고
    • Interaction of the fish pathogen Aeromonas salmonicida with rainbow trout macrophages
    • Interaction of the fish pathogen Aeromonas salmonicida with rainbow trout macrophages. RA Garduno WW Kay, Infect Immun 1992 60 4612 4620
    • (1992) Infect Immun , vol.60 , pp. 4612-4620
    • Garduno, R.A.1    Kay, W.W.2
  • 18
    • 33646259670 scopus 로고
    • Notes upon certain anaerobes isolated from wounds
    • Notes upon certain anaerobes isolated from wounds. Robertson, J Pathol Bacteriol 1916 20 327
    • (1916) J Pathol Bacteriol , vol.20 , pp. 327
    • Robertson1
  • 19
  • 21
    • 0003497334 scopus 로고
    • U.S. Food Drug Administration AOAC, International, Gaithersburg, Md 8
    • Bacteriological analytical manual. U.S. Food and Drug Administration, AOAC, International, Gaithersburg, Md 8 1995
    • (1995) Bacteriological Analytical Manual
  • 23
    • 0032752644 scopus 로고    scopus 로고
    • A lithium chloride-extracted, broad-spectrum-adhesive 42-kilodalton protein of Staphylococcus epidermidis is ornithine carbamoyltransferase
    • A lithium chloride-extracted, broad-spectrum-adhesive 42-kilodalton protein of Staphylococcus epidermidis is ornithine carbamoyltransferase. M Hussain G Peters GS Chhatwal M Herrmann, Infect Immun 1999 67 6688 6690
    • (1999) Infect Immun , vol.67 , pp. 6688-6690
    • Hussain, M.1    Peters, G.2    Chhatwal, G.S.3    Herrmann, M.4
  • 25
    • 17644397901 scopus 로고    scopus 로고
    • Surface analyses and immune reactivities of major cell wall-associated proteins of group A Streptococcus
    • Surface analyses and immune reactivities of major cell wall-associated proteins of group A Streptococcus. JN Cole RD Ramirez BJ Currie SJ Cordwell SP Djordjevic MJ Walker, Infect Immun 2005 73 3137 3146
    • (2005) Infect Immun , vol.73 , pp. 3137-3146
    • Cole, J.N.1    Ramirez, R.D.2    Currie, B.J.3    Cordwell, S.J.4    Djordjevic, S.P.5    Walker, M.J.6
  • 26
    • 0025251769 scopus 로고
    • Arginine catabolism by strains of oral streptococci
    • Arginine catabolism by strains of oral streptococci. E Floderus LE Linder ML Sund, APMIS 1990 98 1045 1052
    • (1990) APMIS , vol.98 , pp. 1045-1052
    • Floderus, E.1    Linder, L.E.2    Sund, M.L.3
  • 27
    • 0036955884 scopus 로고    scopus 로고
    • Identification and characterization of two temperature-induced surface-associated proteins of Streptococcus suis with high homologies to members of the arginine deiminase system of Streptococcus pyogenes
    • Identification and characterization of two temperature-induced surface-associated proteins of Streptococcus suis with high homologies to members of the arginine deiminase system of Streptococcus pyogenes. N Winterhoff R Goethe P Gruening M Rohde H Kalisz HE Smith P Valentin-Weigand, J Bacteriol 2002 184 6768 6776
    • (2002) J Bacteriol , vol.184 , pp. 6768-6776
    • Winterhoff, N.1    Goethe, R.2    Gruening, P.3    Rohde, M.4    Kalisz, H.5    Smith, H.E.6    Valentin-Weigand, P.7
  • 28
    • 58249109483 scopus 로고    scopus 로고
    • Immunization against Clostridium perfringens cells elicits protection against Clostridium tetani in mouse model: Identification of cross-reactive proteins using proteomic methodologies
    • Immunization against Clostridium perfringens cells elicits protection against Clostridium tetani in mouse model: identification of cross-reactive proteins using proteomic methodologies. SI Alam S Bansod L Singh, BMC Microbiol 2008 8 194
    • (2008) BMC Microbiol , vol.8 , pp. 194
    • Alam, S.I.1    Bansod, S.2    Singh, L.3
  • 30
    • 33846135746 scopus 로고    scopus 로고
    • Clostridium perfringens antigens recognized by broiler chickens immune to necrotic entritis
    • Clostridium perfringens antigens recognized by broiler chickens immune to necrotic entritis. RR Kulkarni VR Parreira S Sharif JF Prescott, Clin Vac Immunol 2006 13 1358 1362
    • (2006) Clin Vac Immunol , vol.13 , pp. 1358-1362
    • Kulkarni, R.R.1    Parreira, V.R.2    Sharif, S.3    Prescott, J.F.4
  • 31
    • 0037296905 scopus 로고    scopus 로고
    • Multiple peptide forms observed in two-dimensional gels of Methylococcus capsulatus (Bath) are generated during the separation process
    • Multiple peptide forms observed in two-dimensional gels of Methylococcus capsulatus (Bath) are generated during the separation process. FS Bersen OA Karlsen JC Murrell HB Jensen, Electrophoresis 2003 24 757 761
    • (2003) Electrophoresis , vol.24 , pp. 757-761
    • Bersen, F.S.1    Karlsen, O.A.2    Murrell, J.C.3    Jensen, H.B.4
  • 32
    • 0033920377 scopus 로고    scopus 로고
    • Deamidation as a widespread phenomenon in two-dimensional polyacrylamide gel electrophoresis of human blood plasma proteins
    • Deamidation as a widespread phenomenon in two-dimensional polyacrylamide gel electrophoresis of human blood plasma proteins. H Sarioglu F Lottspeich T Walk G Jung C Eckerskorn, Electrophoresis 2000 21 2209 2218
    • (2000) Electrophoresis , vol.21 , pp. 2209-2218
    • Sarioglu, H.1    Lottspeich, F.2    Walk, T.3    Jung, G.4    Eckerskorn, C.5
  • 34
    • 0028803091 scopus 로고
    • Immune response to Schistosoma mansoni phosphoglycerate kinase during natural and experimental infection: Identification of a schistosome-specific B-cell epitope
    • Immune response to Schistosoma mansoni phosphoglycerate kinase during natural and experimental infection: identification of a schistosome-specific B-cell epitope. KW Lee A Thakur AM Karim PT LoVerde, Infect Immun 1995 63 4307 4311
    • (1995) Infect Immun , vol.63 , pp. 4307-4311
    • Lee, K.W.1    Thakur, A.2    Karim, A.M.3    Loverde, P.T.4
  • 36
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • The Hsp70 and Hsp60 chaperone machines. B Bukau AL Horwich, Cell 1998 92 351 366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 38
    • 0032486286 scopus 로고    scopus 로고
    • Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. V Pancholi VA Fischetti, J Biol Chem 1998 273 14503 14515
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 40
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins. D Granato GE Bergonzelli RD Pridmore L Marvin M Rouvet IE Corthesy-Theulaz, Infect Immun 2004 72 2160 2169
    • (2004) Infect Immun , vol.72 , pp. 2160-2169
    • Granato, D.1    Bergonzelli, G.E.2    Pridmore, R.D.3    Marvin, L.4    Rouvet, M.5    Corthesy-Theulaz, I.E.6
  • 41
    • 25444445823 scopus 로고    scopus 로고
    • Identification of immunogenic and serum binding proteins of Staphylococcus epidermidis
    • Identification of immunogenic and serum binding proteins of Staphylococcus epidermidis. BR Sellman AP Howell C Kelly-Boyd SM Baker, Infect Immun 2005 73 6591 6600
    • (2005) Infect Immun , vol.73 , pp. 6591-6600
    • Sellman, B.R.1    Howell, A.P.2    Kelly-Boyd, C.3    Baker, S.M.4
  • 42
    • 0036249166 scopus 로고    scopus 로고
    • Identification of vaccine candidate antigens of Staphylococcus aureus by serological proteome analysis
    • DOI 10.1002/1615-9861(200205)2:5<580::AID-PROT580>3.0.CO;2-G
    • Identification of vaccine candidate antigens of Staphylococcus aureus by serological proteome analysis. O Vytvytska E Nagy M Blüggel HE Meyer R Kurzbauer LA Huber CS Klade, Proteomics 2002 2 580 590 (Pubitemid 34507348)
    • (2002) Proteomics , vol.2 , Issue.5 , pp. 580-590
    • Vytvytska, O.1    Nagy, E.2    Bluggel, M.3    Meyer, H.E.4    Kurzbauer, R.5    Huber, L.A.6    Klade, C.S.7
  • 43
    • 0036434714 scopus 로고    scopus 로고
    • Elongation factor Tu and E1 b subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae
    • Elongation factor Tu and E1 b subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae. SF Dallo TR Kannan MW Blaylock JB Baseman, Mol Microbiol 2002 46 1041 1051
    • (2002) Mol Microbiol , vol.46 , pp. 1041-1051
    • Dallo, S.F.1    Kannan, T.R.2    Blaylock, M.W.3    Baseman, J.B.4
  • 45
    • 0023142181 scopus 로고
    • Comparison of clindamycin and rifampicin, tetracylin, metronidazoles and penicillin for efficacy in prevention of experimental gas gangrene due to Clostridium perfringens
    • Comparison of clindamycin and rifampicin, tetracylin, metronidazoles and penicillin for efficacy in prevention of experimental gas gangrene due to Clostridium perfringens. DL Stevens KA Maier BM Laine JE Mitten, J Infect Dis 1987 155 220 228
    • (1987) J Infect Dis , vol.155 , pp. 220-228
    • Stevens, D.L.1    Maier, K.A.2    Laine, B.M.3    Mitten, J.E.4
  • 46
    • 31344438726 scopus 로고    scopus 로고
    • The cytosolic, cell surface and extracellular proteomes of the biotechnologically important soil bacterium Corynebacterium efficiens YS-314 in comparison to those of Corynebacterium glutamicum ATCC 13032
    • The cytosolic, cell surface and extracellular proteomes of the biotechnologically important soil bacterium Corynebacterium efficiens YS-314 in comparison to those of Corynebacterium glutamicum ATCC 13032. N Hansmeier TC Chao A Puhler A Tauch J Kalinowski, Proteomics 2006 6 233 250
    • (2006) Proteomics , vol.6 , pp. 233-250
    • Hansmeier, N.1    Chao, T.C.2    Puhler, A.3    Tauch, A.4    Kalinowski, J.5
  • 47
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. MM Bradford, Anal Bichem 1976 72 248 254
    • (1976) Anal Bichem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 48
    • 0021306856 scopus 로고
    • Systems for polyacrylamide gel electrophoresis
    • New York: Academic Press Jaeoby WB 6717283
    • Systems for polyacrylamide gel electrophoresis. PJ Blackshear, Methods in enzymology New York: Academic Press, Jaeoby WB, 1984 104 237 255 6717283
    • (1984) Methods in Enzymology , vol.104 , pp. 237-255
    • Blackshear, P.J.1


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