Purification and Immunochemical Properties of a Wall Protein Antigen from <i>Clostridium difficile</i> ATCC 11011

Takumi, Kenji; Takeoka, Aya; Kawata, Tomio

doi:10.1111/j.1348-0421.1987.tb03145.x

Cited by 11 publications

(21 citation statements)

References 34 publications

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“…These proteins all contain three cell wall binding domains, the role of which is to anchor proteins to the cell surface, and are similar to the S-layer protein, SlpA, of C. difficile (Calabi et al 2001). The amino acid compositions of CBO0378 and CBO380 are comparable to that determined for an antigenic cell wall protein of proteolytic C. botulinum type A strain 190L (Takumi et al 1983), suggesting that these genes may encode the S-layer proteins for Hall A.…”

Section: Components Of the Cell Surfacementioning

confidence: 59%

Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes

Sebaihia¹,

Peck²,

Minton³

et al. 2007

Genome Res.

235

215

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Clostridium botulinum is a heterogeneous Gram-positive species that comprises four genetically and physiologically distinct groups of bacteria that share the ability to produce botulinum neurotoxin, the most poisonous toxin known to man, and the causative agent of botulism, a severe disease of humans and animals. We report here the complete genome sequence of a representative of Group I (proteolytic) C. botulinum (strain Hall A, ATCC 3502). The genome consists of a chromosome (3,886,916 bp) and a plasmid (16,344 bp), which carry 3650 and 19 predicted genes, respectively. Consistent with the proteolytic phenotype of this strain, the genome harbors a large number of genes encoding secreted proteases and enzymes involved in uptake and metabolism of amino acids. The genome also reveals a hitherto unknown ability of C. botulinum to degrade chitin. There is a significant lack of recently acquired DNA, indicating a stable genomic content, in strong contrast to the fluid genome of Clostridium difficile, which can form longer-term relationships with its host. Overall, the genome indicates that C. botulinum is adapted to a saprophytic lifestyle both in soil and aquatic environments. This pathogen relies on its toxin to rapidly kill a wide range of prey species, and to gain access to nutrient sources, it releases a large number of extracellular enzymes to soften and destroy rotting or decayed tissues.

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Section: Components Of the Cell Surfacementioning

confidence: 59%

Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes

Sebaihia¹,

Peck²,

Minton³

et al. 2007

Genome Res.

235

215

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“…Usually, the subunit proteins isolated from gram-positive bacteria require neither specific cations nor supporting layers for their reassembly, while those from gram-negative bacteria require both cations and supporting layers of Clostridium difficile (13). We also found that these strains carrying regular arrays possessed two major cell wall proteins (13), and one of the major proteins with a molecular weight of 32 kDa of strain ATCC 11011 of the organism was purified and characterized (27). This paper describes properties of the two major cell wall proteins with molecular weights of 38 kDa and 42 kDa, and reassembly of a tetragonal array of C. difficile GAI 4131.…”

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confidence: 92%

Characterization and Reassembly of a Regular Array in the Cell Wall of Clostridium difficile GAI 4131

Masuda

Itoh

Kawata

1989

Microbiology and Immunology

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The cell wall of Clostridium difficile GAI 4131 was revealed by electron microscopy to have an outer layer composed of a nearly square array and contained the two major proteins with molecular weights of 38 kDa and 42 kDa. The properties and reassembly of the two major proteins into the regular array were investigated. When the isolated cell walls were treated with hydrophobic bond-disrupting agents or a chelating agent specific for Ca2+, the two major proteins were effectively removed and the regularly arranged outer layer disappeared. The amino acid composition of the two major proteins differed from each other. The two major proteins also gave different peptide maps from each other upon proteolysis with Staphylococcus aureus V8 protease. The major proteins solubilized from the isolated cell walls with 8 M urea or 4 M guanidine hydrochloride could be reassembled into open-ended cylinders possessing the native regular pattern by dialysis against neutral buffer containing 5 mm CaCl2. The reassembled cylinders purified by centrifugation on a Percoll density gradient were composed of almost equal amounts of the 38 kDa and 42 kDa proteins ond freed from the other proteins. These results suggest that the regular array in the outer cell wall layer is constructed from the two major cell wall proteins and requires Ca2+ for its assembly.

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“…Molecular weights of S layer proteins range from 40 to 200 kDa (14). Although data on characterization and functional significance of S layer of several bacterial species have been accumulated (4,11,12), there is scant information on S layer and S layer proteins of pathogenic clostridial strains (6,17,18). Previously Takagi et al (15), electron-microscopically demonstrated that C. tetani strain Riku-3 had a regularly arranged surface lattice on the cell wall.…”

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confidence: 99%

“…All bacterial strains were grown in GAM broth (Nissui Pharmaceutical Co., Ltd., Tokyo) at 37 C for 15 hr. Cell walls were prepared from cells harvested at the early stationary growth phase of C. tetani strain AO 174 according to the methods described previously (17). S layer protein was purified from the cell wall preparation as follows : the cell wall (17).…”

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confidence: 99%

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S Layer Protein of Clostridium tetani: Purification and Properties

Takumi

Susami

Takeoka

et al. 1991

Microbiology and Immunology

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S layer protein of Clostridium tetani strain AO 174, a nontoxigenic derivative of strain Harvard A 47, was prepared from the cell walls by 4 M urea extraction and purified by DEAE-Sepharose CL-6B chromatography followed by a combination of anion-exchange chromatography and reverse-phase chromatography using an HPLC system. The molecular weight of the S layer protein was estimated to be 140 kilodaltons (kDa) by SDS-PAGE.The amino acid composition of the 140 kDa protein was very similar to those of S layer proteins from the other bacterial species: it was rich in acidic amino acid and lacked cysteine. Also, the protein was unique in its extremely low content of proline (0.02 to 0.03 mol% ). Multiple isoelectric forms ranging from pH 4.0 to 4.5 were observed in the purified preparation. immunodiffusion analysis showed that the 140 kDa protein was a common antigen to the three strains of C. tetani tested.

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Purification and Immunochemical Properties of a Wall Protein Antigen from Clostridium difficile ATCC 11011

Cited by 11 publications

References 34 publications

Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes

Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes

Characterization and Reassembly of a Regular Array in the Cell Wall of Clostridium difficile GAI 4131

S Layer Protein of Clostridium tetani: Purification and Properties

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