Characterization of the exosporium of Bacillus cereus

Charlton, S.; Moir, Anne; Baillie, Les

doi:10.1046/j.1365-2672.1999.00878.x

Cited by 112 publications

(94 citation statements)

References 22 publications

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“…However, the regulation of production of InhA, subtilisin or other exoenzymes may be much more important for the survival of B. thuringiensis or B. subtilis in natural environments than in laboratory conditions. A homologous InhA protein has recently been found in an active form on the exosporium of B. cereus (Charlton et al, 1999). This suggests that the presence of InhA on the spore surface may have functional significance.…”

Section: Discussionmentioning

confidence: 93%

Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation The GenBank/EMBL/DDBJ accession number for the sequence reported in this paper is AF287346.

2001

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The immune inhibitor A (InhA) metalloprotease from Bacillus thuringiensis specifically cleaves antibacterial proteins produced by the insect host, suggesting that it may contribute to the overall virulence of B. thuringiensis. The transcriptional regulation of the inhA gene in both B. thuringiensis and Bacillus subtilis was investigated. Using a transcriptional inhA'-lacZ fusion, it was shown that inhA expression is activated at the onset of sporulation.However, the transcriptional start site of inhA is similar to σ A -dependent promoters, and deletion of the sporulation-specific sigma factors σ F or σ E had no effect on inhA expression in B. subtilis. The DNA region upstream from inhA contains two genes encoding polypeptides similar to the SinI and SinR regulators of B. subtilis. SinR is a DNA-binding protein regulating gene expression and SinI inhibits SinR activity. Overexpression of the sin genes affects the expression of the inhA'-lacZ transcriptional fusion in B. thuringiensis : early induction of inhA expression was observed when sinI was overexpressed, whereas inhA expression was reduced in a strain overexpressing sinR, suggesting that inhA transcription is repressed, directly or indirectly, by SinR. inhA transcription was greatly reduced in B. thuringiensis and B. subtilis spo0A mutants. Analysis of the inhA'-lacZ expression in abrB and abrB-spo0A mutants of B. subtilis indicates that the Spo0A-dependent regulation of inhA expression depends on AbrB, which is known to regulate expression of transition state and sporulation genes in B. subtilis.

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Section: Discussionmentioning

confidence: 93%

Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation The GenBank/EMBL/DDBJ accession number for the sequence reported in this paper is AF287346.

2001

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“…3). GroEL has already been reported as an exosporium-adsorbed protein in B. cereus, removable by salt washing (Charlton et al, 1999;Todd et al, 2003). The Zn-dependent metalloprotease immune inhibitor A (InhA), a major component of unwashed exosporium preparations of B. cereus, was not detectable in B. anthracis exosporium.…”

Section: Identification Of Proteins In Unwashed Exosporiummentioning

confidence: 99%

“…Much of the work published on the fine structure and composition of the exosporium to date has focused upon B. cereus (Gerhardt & Ribi, 1964;Matz et al, 1970;Beaman et al, 1971;Charlton et al, 1999). This layer is chemically complex, consisting of protein, amino and neutral polysaccharides, lipids and ash (Matz et al, 1970).…”

Section: Introductionmentioning

confidence: 99%

“…B. cereus exosporium antigens first appear at the engulfment stage (stage III) of sporulation (DesRosier & Lara, 1984). Bacillus thuringiensis (Garcia-Patrone & Tandecarz, 1995), B. cereus (Charlton et al, 1999) and B. anthracis (Sylvestre et al, 2002) spores contain specific glycoproteins in their surface layers. The B. anthracis collagen-like spore surface glycoprotein (BclA) reported by Sylvestre et al (2002) is a structural component of the filaments of the hairy nap and is highly immunogenic.…”

Section: Introductionmentioning

confidence: 99%

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Identification of proteins in the exosporium of Bacillus anthracis

et al. 2004

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Spores of Bacillus anthracis, the causative agent of anthrax, possess an exosporium. As the outer surface layer of these mature spores, the exosporium represents the primary contact surface between the spore and environment/host and is a site of spore antigens. The exosporium was isolated from the endospores of the B. anthracis wild-type Ames strain, from a derivative of the Ames strain cured of plasmid pXO2 " , and from a previously isolated pXO1" doubly cured strain, B. anthracis UM23Cl2. The protein profiles of SDS-PAGE-separated exosporium extracts were similar for all three. This suggests that avirulent variants lacking either or both plasmids are realistic models for studying the exosporium from spores of B. anthracis. A number of loosely adsorbed proteins were identified from amino acid sequences determined by either nanospray-MS/MS or N-terminal sequencing. Salt and detergent washing of the exosporium fragments removed these and revealed proteins that are likely to represent structural/integral exosporium proteins. Seven proteins were identified in washed exosporium: alanine racemase, inosine hydrolase, ExsF, CotY, ExsY, CotB and a novel protein, named ExsK. CotY, ExsY and CotB are homologues of Bacillus subtilis outer spore coat proteins, but ExsF and ExsK are specific to B. anthracis and other members of the Bacillus cereus group.

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“…Transmission electron microscopy (TEM) revealed the exosporium to be a thin, layered structure (Gerhardt and Ribi, 1964;Liu et al, 2004). The exosporium influences spore hydrophobicity and organism pathogenicity (Charlton et al, 1999). Enzymes associated with the exosporium surface may limit premature germination (Todd et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Atomic force microscopy of Bacillus spore surface morphology

Zolock¹,

Li²,

Bleckmann³

et al. 2006

Micron

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Bacillus spore surface morphology was imaged with atomic force microscopy (AFM) to determine if characteristic surface features could be used to distinguish between four closely related species; Bacillus anthracis Sterne strain, Bacillus thuringiensis var. kurstaki, Bacillus cereus strain 569, and Bacillus globigii var. niger. AFM surface height images showed an irregular topography across the curved upper surface of the spores. Phase images showed a superficial grain structure with different levels of phase contrast and significant differences in average surface morphologies among the four species. Although spores of the same species showed similarities, there was significant variability within each species. Overall, AFM revealed that spore surface morphology is rich with information, which can be used to distinguish a sample of about 20 spores from a similar number of spores of closely related species. Statistical analysis of spore morphology from a combination of amplitude and phase images for a small sample allows differentiation between, B. anthracis and its close relatives. q

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Characterization of the exosporium of Bacillus cereus

Cited by 112 publications

References 22 publications

Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation The GenBank/EMBL/DDBJ accession number for the sequence reported in this paper is AF287346.

Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation The GenBank/EMBL/DDBJ accession number for the sequence reported in this paper is AF287346.

Identification of proteins in the exosporium of Bacillus anthracis

Atomic force microscopy of Bacillus spore surface morphology

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