Immunochemical Characterization of Cell Wall Protein Antigen Purified from the Cell Wall Autolysate of <i>Clostridium botulinum</i> Type A

Takumi, Kenji; Kawata, Tomio

doi:10.1111/j.1348-0421.1975.tb00840.x

Cited by 2 publications

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“…The antigen was found to be a common antigen among the proteolytic strains of the organism by immunodiffusion. The wall protein antigen obtained from autolysate of the cell wall by subsequent ionexchange chromatography and gel filtration still contained several antigens (26). In addition, toxin production of strain 190L appeared to be closely related to formation of the wall protein antigen, because nontoxigenic variants induced by treatment with detergents were associated with deficiency of the outer layer of the cell wall (28).…”

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Purification and characterization of a wall protein antigen from Clostridium botulinum type A

Takumi¹,

Takeoka²,

Kawata³

1983

Infect Immun

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A wall surface protein, designated antigen S, was extracted from Clostridium botulinum type A strain 190L with 0.1% Brij 58-2 M LiCl and purified sequentially by acetone pecipitation, ion-exchange chromatography, hydroxyapatite chromatography, chromatofocusing, and gel filtration. Crossed immunoelectrophoresis of the purified antigen S preparation against homologous multispecific antiserum to whole cells revealed only a single precipitin line. Antigen S had an apparent molecular weight of about 195,000, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The antigen was composed predominantly of acidic amino acid residues, and the isoelectric point was estimated to be at pH 4.75. Tryptic digestion of antigen S destroyed antigenic activity and produced one major polypeptide fragment with a molecular weight of about 44,000. Indirect immunoferritin labeling showed that antigen S was located on the outer layer of the cell wall.

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confidence: 99%

Purification and characterization of a wall protein antigen from Clostridium botulinum type A

Takumi¹,

Takeoka²,

Kawata³

1983

Infect Immun

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“…Escherichia coli strain B, Staphylococcus aureus strain 3528 and Micrococcus lysodeikticus strain 12698 by the hot formamide method of Perkins [14] kindly provided by Dr. K. Hisatsune (Department of Microbiology, School of Pharmaceutical Sciences, Josai University, Sakado, Saitama) were also used as antigens. The quantitative precipitin test and immunodiffusion test were carried out as described previously [23]. RESULTS…”

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confidence: 99%

Quantitative Chemical Analyses and Antigenic Properties of Peptidoglycans from Clostridium botulinum and Other Clostridia

Takumi

Kawata

1976

Japanese Journal of Microbiology

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The cell wall peptidoglycans were isolated from Clostridium botulinum and some other species of the genus Clostridium by hot formamide extraction and their quantitative chemical composition and antigenic properties were determined.The peptidoglycan of C. botulinum type E was found to be a diaminopimelic acid (DAP)-containing type composed of glucosamine, muramic acid, glutamic acid, alanine and DAP in the molar ratio of 0.76 :0.78 :1.00:1.88 :0.81. All other types of C. botulinum and Clostridium sporogenes also belonged to the same peptidoglycan type. The peptidoglycans of Clostridium bfermentans and Clostridium histolyticum contained DAP but they differed from those of C. botulinum in the molar ratio of alanine to glutamic acid. The peptidoglycan of Clostridium perfringens was composed of glutamic acid, alanine, DAP and glycine in the molar ratio of 1.00 :1.64 :0.94 :0.90. On the other hand, the peptidoglycan of Clostridium septicum was found to contain lysine instead of DAP and the molar ratio was 1.00:1.41 :0.96 for glutamic acid, alanine and lysine. In spite of the difference in amino acid composition of peptidoglycans among the clostridia, the quantitative precipitin test demonstrated that antiserum against C. botulinum type E peptidoglycan cross-reacted with the peptidoglycans from other clostridia as well as various types of C. botulinum.It is well known that the cell walls of grampositive bacteria are composed mainly of peptidoglycan, polysaccharides, teichoic acid or teichuronic acid. The peptidoglycan, which is the only cell wall heteropolymer common to almost all bacteria, is composed of repeating units of N-acetylglucosamine and N-acetylmuramic acid in which the Dlactate moiety of each muramic acid residue is substituted by a short peptide chain consisting of alternating L-and D-amino acid moieties, and the peptide chain is further connected to another adjacent peptide by various modes of cross-linkages [4,16,25].The chemical constituents of the cell walls of various species of the genus Clostridium were qualitatively determined by Cummins and colleague [2, 3] and these results were used for classification of this genus [19]. Although there are a few studies on the quantitative chemical analyses of peptidoglycans of some clostridia [12,13,15]

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Immunochemical Characterization of Cell Wall Protein Antigen Purified from the Cell Wall Autolysate of Clostridium botulinum Type A

Cited by 2 publications

References 20 publications

Purification and characterization of a wall protein antigen from Clostridium botulinum type A

Purification and characterization of a wall protein antigen from Clostridium botulinum type A

Quantitative Chemical Analyses and Antigenic Properties of Peptidoglycans from Clostridium botulinum and Other Clostridia

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