Paracrystalline Sheets Reaggregated from Solubilized Exosporium of
            <i>Bacillus cereus</i>

Beaman, T C; Pankratz, H. Stuart; Gerhardt, Philipp

doi:10.1128/jb.107.1.320-324.1971

Cited by 40 publications

(22 citation statements)

References 24 publications

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“…The exosporium of B. cereus group spores appears to be assembled concurrent with but independent of the cortex and coat (Ohye and Murrell, 1973). Previous investigations of the content and structure of the exosporium suggest that its assembly is uniform (Gerhardt and Ribi, 1964;Beaman et al, 1971;Ohye and Murrell, 1973;Steichen et al, 2005). The experiments described in this paper, which were designed to Immobilized spores were allowed to germinate and outgrow as described in Fig.…”

Section: Discussionmentioning

confidence: 99%

Non‐uniform assembly of the Bacillus anthracis exosporium and a bottle cap model for spore germination and outgrowth

Steichen

Kearney

Turnbough³

2007

Molecular Microbiology

119

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SummarySpores of Bacillus anthracis are enclosed by an exosporium composed of a basal layer and an external hair-like nap. The nap is formed by a collagen-like glycoprotein called BclA, while the basal layer contains many different proteins, one of which is a sporespecific alanine racemase (Alr). In this study, we employed fluorescence microscopy and a fluorescently labelled anti-Alr monoclonal antibody (mAb) to examine the distribution of Alr within the exosporium. Binding of the mAb occurred over approximately three-quarters of the exosporium but not in a cap-like region at one end of the spore, indicating the absence or inaccessibility of Alr in this region. We also determined that the cap-like region, or cap, corresponds to the first part of the exosporium assembled within the mother cell during sporulation and the only part of the exosporium assembled in a DexsY mutant strain of B. anthracis. Our results provide the first direct evidence that exosporium assembly is a non-uniform process and suggest that exosporium formation is discontinuous. Finally, we demonstrated that during spore germination and outgrowth, the outgrowing cell always escapes from its exosporium shell by popping through the cap, suggesting that the cap is designed to facilitate the emergence of the outgrowing cell.

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Section: Discussionmentioning

confidence: 99%

Non‐uniform assembly of the Bacillus anthracis exosporium and a bottle cap model for spore germination and outgrowth

Steichen

Kearney

Turnbough³

2007

Molecular Microbiology

119

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“…Spores of all the B. cereus group species possess an outermost layer, called the exosporium, which is not present on other species, including B. clausii, B. safensis and B. subtilis, among others (Driks, 2002;Traag et al, 2010). The exosporium is comprised of a paracrystalline basal layer which is covered by a hair-like nap layer (Gerhardt and Ribi, 1964;Hachisuka et al, 1966;Gerhardt, 1967;Beaman et al, 1971;Sylvestre et al, 2002;Lai et al, 2003;Steichen et al, 2003;Todd et al, 2003;Giorno et al, 2007;). The exosporium, as the outermost layer of the spores of these species, likely plays important roles in interactions with surfaces in the soil.…”

Section: Introductionmentioning

confidence: 99%

Assembly of the BclB glycoprotein into the exosporium and evidence for its role in the formation of the exosporium ‘cap’ structure in Bacillus anthracis

Thompson

Hoelscher

Driks

et al. 2012

Molecular Microbiology

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Summary The outermost layer of the Bacillus anthracis spore consists of an exosporium comprised of an outer hair-like nap layer and an internal basal layer. A major component of the hair-like nap is the glycosylated collagen-like protein BclA. A second collagen-like protein, BclB, is also present in the exosporium. BclB possesses an N-terminal sequence that targets it to the exosporium and is similar in sequence to a cognate targeting region in BclA. BclB lacks, however, sequence similarity to the region of BclA thought to mediate attachment to the basal layer via covalent interactions with the basal layer protein BxpB. Here we demonstrate that BxpB is critical for correct localization of BclB during spore formation and that the N-terminal domains of the BclA and BclB proteins compete for BxpB-controlled assembly sites. We found that BclB is located principally in a region of the exosporium that excludes a short arc on one side of the exosporium (the so-called bottle-cap region). We also found that in bclB mutant spores, the distribution of exosporium proteins CotY and BxpB is altered, suggesting that BclB has roles in exosporium assembly. In bclB mutant spores, the distance between the exosporium and the coat, the interspace, is reduced.

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“…Electron microscopy has revealed that the exosporium is composed of a paracrystalline basal layer and a hair-like outer layer (Gerhardt and Ribi 1964). The paracrystalline layer has a hexagonal, perforate lattice structure (Beaman et al 1971). In addition to protein components, the native exosporium fraction contained lipid and carbohydrate (Matz et al 1970;Beaman et al 1971).…”

Section: Introductionmentioning

confidence: 99%

“…The paracrystalline layer has a hexagonal, perforate lattice structure (Beaman et al 1971). In addition to protein components, the native exosporium fraction contained lipid and carbohydrate (Matz et al 1970;Beaman et al 1971). Approximately eight protein components were reported to be present in the exosporium, but these were not characterized further (Beaman et al 1971).…”

Section: Introductionmentioning

confidence: 99%

“…In addition to protein components, the native exosporium fraction contained lipid and carbohydrate (Matz et al 1970;Beaman et al 1971). Approximately eight protein components were reported to be present in the exosporium, but these were not characterized further (Beaman et al 1971). More recently, an exosporium-specific glycoprotein has been shown to be synthesized by B. thuringiensis (Garcia-Patrone and Tandecarz 1995).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the exosporium of Bacillus cereus

Charlton

Moir

Baillie³

1999

J Appl Microbiol

112

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Exosporium components from endospores of Bacillus cereus ATCC 10876 were purified and separated by gel electrophoresis. Several of the proteins for which N‐terminal sequences were recovered were found to have homologues in protein databases which have been demonstrated to have enzymic activity in other organisms. Amongst these is a zinc metalloprotease, immune inhibitor A, already described in B. thuringiensis. This has been shown to be present in an active 73 kDa form on the exosporium of B. cereus. Other proteins associated with the exosporium include the molecular chaperone GroEL and a homologue of RocA (1‐pyrroline‐5‐carboxylate dehydrogenase (EC 1.5.1.12)) of B. subtilis. Although these are unlikely to represent integral structural proteins of the exosporium, the observation that they are selectively present in the spore surface layer suggests that this layer may have functional significance.

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Paracrystalline Sheets Reaggregated from Solubilized Exosporium of Bacillus cereus

Cited by 40 publications

References 24 publications

Non‐uniform assembly of the Bacillus anthracis exosporium and a bottle cap model for spore germination and outgrowth

Non‐uniform assembly of the Bacillus anthracis exosporium and a bottle cap model for spore germination and outgrowth

Assembly of the BclB glycoprotein into the exosporium and evidence for its role in the formation of the exosporium ‘cap’ structure in Bacillus anthracis

Characterization of the exosporium of Bacillus cereus

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