Isolation of a Common Cell Wall Antigen from the Proteolytic Strains of <i>Clostridium botulinum</i>

Takumi, Kenji; Kawata, Tomio

doi:10.1111/j.1348-0421.1974.tb00747.x

Cited by 9 publications

(6 citation statements)

References 26 publications

(24 reference statements)

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“…Later, using agglutination and the agglutination absorption test, Solomon et al [15] also demonstrated that C. botulinum type A shared somatic antigens with the proteolytic strains of types B and F, whereas type E shared somatic antigens with the nonproteolytic strains of types B and F. Recently, we have reported that a common antigenic material is present in the trypsin-treated cell wall extracts of proteolytic strains of C. botulinum [17] and suggested that they came from protein portions of the cell walls. This view was further supported by the present investigation.…”

Section: Discussionmentioning

confidence: 97%

“…Our recent studies [17] have shown that a protein-rich antigen sharing a common antigenic specificity among the proteolytic strains of Clostridium botulinum is readily solubilized from the isolated cell walls of C. botulinum type A by autolysis as well as by tryptic digestion. It is likely that the prime component responsible for the serological activity may be localized in protein moieties of the cell wall.…”

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confidence: 99%

“…The present investigation was aimed at purification of the cell wall protein antigen from the organism and elucidation of its immunochemical properties. Because the serological activity of this antigen was relatively labile and destroyed by acid or formamide [17], autolysis of the cell wall was chosen for extraction of the protein antigen.…”

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confidence: 99%

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

Takumi

Kawata

1975

Japanese Journal of Microbiology

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The cell wall protein antigen was solubilized from the isolated cell walls of Clostridium botulinum type A by autolysis and purified by diethylaminoethyl-cellulose column chromatography followed by gel filtration on Sephadex G-150. The two fractions showed a high degree of the serological activity and produced a main fused precipitin line in immunodiffusion tests against the homologous antiserum. The fact that antigenic fractions contained various kinds of amino acids but no detectable amounts of amino sugars or carbohydrates suggests that the antigens were principally composed of proteins. The protein antigen possessed multiple antigenic components in immunoelectrophoresis. As serological activity, the antigen was heat-stable and resistant to tryptic digestion but sensitive to the actions of pronase, nagarse or pepsin. The protein antigen appeared to be responsible for the common antigenicity among the proteolytic strains of C. botulinum.

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Section: Discussionmentioning

confidence: 97%

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confidence: 99%

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

Takumi

Kawata

1975

Japanese Journal of Microbiology

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“…Comparison between the Chemical Composition of SDS-Treated Cell Walls and Formamide-Extracted Cell Walls (Peptidoglycans) from C. botulinum Type E Our recent studies [22] have shown that the protein antigen sharing a common antigenicity among the proteolytic strains of C. botulinum is readily released from the cell walls by SDS-treatment as well as by tryptic digestion.…”

Section: And Discussionmentioning

confidence: 99%

“…Organisms and cultivation. The cultures of C. botulinum type A strains 190L and Akita-38, type B strains Okra and 17B, and type F strains Langeland and OSU were used as described previously [22]. C. botulinum type C strain Stockholm, type D strain 1873, and type E strains Saroma and VH were supplied from the Hokkaido Institute of Public Health, Sapporo.…”

Section: Methodsmentioning

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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Biological Membranes

Dillon

1981

Ultrastructure, Macromolecules, and Evolution

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Isolation of a Common Cell Wall Antigen from the Proteolytic Strains of Clostridium botulinum

Cited by 9 publications

References 26 publications

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

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

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

Biological Membranes

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