SEROLOGICAL STUDIES ON THE FORMATION OF PROTEIN PARASPORAL INCLUSIONS IN <i>BACILLUS THURINGIENSIS </i>

Monro, R.E.

doi:10.1083/jcb.11.2.321

Cited by 22 publications

(4 citation statements)

References 11 publications

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“…In contrast, antiserum to soluble crystal protein was specific in the sense that it precipitated spore and crystal protein extracted with urea-mercaptoethanol or alkali but did not precipitate either of the vegetative cell extracts or the phosphate spore extract. This immunological pattern confirms a previous report that crystal antigen is not found in the vegetative cell (18). It also suggests that spore and crystal may share one or more similar antigens.…”

Section: Immunological Homology With Spore Proteinsupporting

confidence: 91%

“…The crystal first appears as a minute granule near the forespore, enlarges as the spore develops, and reaches its full size as the spore becomes mature (22). The crystal is synthesized from amino acids formed by protein turnover within the sporangium (17), a conclusion supported by the observation that crystal antigen is not found in the cell prior to sporulation (18). Furthermore, it has been asserted that crystal antigen is absent from the spore (18).…”

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confidence: 93%

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Immunological Homology Between Crystal and Spore Protein of Bacillus thuringiensis

1968

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Spore suspensions containing about 0.3% crystals and crystal suspensions containing about 0.1% spores were obtained from cultures of Bacillus thuringiensis by extraction with a two-phase system. Both preparations were tested for the presence of contaminating material from vegetative cells and were judged to be clean. Solutions of spore protein were obtained by extracting broken spores with phosphate buffer followed by extraction with either alkalior urea-mercaptoethanol. The alkali spore or urea spore extracts had the same isoelectric point as crystal protein solubilized with these reagents. An antiserum prepared against alkali crystal solution precipitated alkali or urea spore extracts and crystal solutions but not phosphate spore extracts or extracts of whole cells. Lines of identity between spore and crystal precipitates were observed by using the Ouchterlony doublediffusion technique. Absorption of the antiserum with an excess of urea spore extract caused a disappearance of the precipitin bands originating from the spore protein and the homologous bands from the crystal protein. The results suggest that the crystal and endospore contain one or more common proteins.

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Section: Immunological Homology With Spore Proteinsupporting

confidence: 91%

mentioning

confidence: 93%

Immunological Homology Between Crystal and Spore Protein of Bacillus thuringiensis

1968

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“…Immunological studies of B. thuringiensis subsp. kurstaki confirmed the microscopic studies (1,17,18). The one exception to date is Bacillus cereus subsp.…”

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confidence: 68%

Regulation of protoxin synthesis in Bacillus thuringiensis

Minnich¹,

Aronson²

1984

J Bacteriol

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A derivative of Bacillus thuringiensis subsp. kurstaki (HD-1) formed parasporal inclusions at 25°C, but not at 32°C. This strain differed from the parent only in the loss of a 110-megadalton (Md) plasmid, but plasmid and chromosomal copies of protoxin genes were present in both strains. On the basis of temperature shift experiments, the sensitive period appeared to be during midexponential growth, long before the time of protoxin synthesis at 3 to 4 h after the end of exponential growth. The conditional phenotype could be transferred by cell mating to naturally acrystalliferous Bacillus cereus. In all such cases, a 29-Md protoxin-encoding plasmid was transferred, but this plasmid alone was barely sufficient for protoxin synthesis. Protoxin production increased to detectable levels, but well below those of the parental donor strain, by simultaneous transfer of a 44-Md protoxin-enicoding plasmid. Transfer of a 5-Md plasmid with the two larger protoxin-coding plasmids resulted in a protoxin synthesis level approaching that of the donor strain. A role for some of the cryptic plasmids of kurstaki in parasporal body formation was implied. In contrast, a closely related B. thuringiensis strain, HD73, produced crystals at both 25 and 32°C even when the capacity was transferred on a 50-Md plasmid to B. cereus. The amount of protoxin produced in

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“…Young and Pitz-James [I] described the simultaneous development of the spore and crystal as seen in the light microscope and followed changes in a number of biochemical parameters during sporulation. Crystal antigens, which are absent from vegetative cells [2,3], appear during sporulation [2,4] some time before the development of heat resistance. Monro [5] provided evidence from radioactive labelling studies that the bulk, if not all, of the crystal protein is formed de novo during sporulation and concluded from immunological comparison [2] of crystal protein with soluble spore protein that the crystal and the spore did not share common components.…”

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confidence: 99%

Formation of the Parasporal Inclusion of Bacillus thuringiensis

Somerville

1971

European Journal of Biochemistry

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Under given experimental conditions, a reproducible sequence of biochemical events can be measured during sporulation in Bacillus thuringiensis. Electron microscope studies reveal that, during its formation, the crystalline inclusion of Bacillus thuringiensis is closely associated with the exosporium. This association persists through several serial sections and can also be demonstrated in a mutant strain which is biochemically blocked soon after crystal formation.Two asporogenic crystalliferous strains produce a toxin active on larvae of Plutella maculipennis whereas two sporogenic, acrystalliferous strains are not toxic.Data from immunological assays and from pulse-chase and label-chase experiments with [14C]leucine indicate that the crystal protein is synthesized at the time of appearance of crystal antigens. It is suggested that the crystal is synthesized and assembled on the exosporium.The production by Bacillus thuringiensis of a crystalline parasporal body concomitant with the formation of the endospore is the principal distinction between strains of B. thuringiensis and of Bacillus cereus. Much work on B. thuringiensis has centred on its entomodical capacity which has been attributed, in part, to the parasporal inclusion, although the molecular nature of the toxic agent and its mode of action are as yet unknown. Several workers have studied the formation of the crystal and its relationship to the spore. Young and Pitz-James [I] described the simultaneous development of the spore and crystal as seen in the light microscope and followed changes in a number of biochemical parameters during sporulation. Crystal antigens, which are absent from vegetative cells [2,3], appear during sporulation [2,4] some time before the development of heat resistance. Monro [5] provided evidence from radioactive labelling studies that the bulk, if not all, of the crystal protein is formed de novo during sporulation and concluded from immunological comparison [2] of crystal protein with soluble spore protein that the crystal and the spore did not share common components. Recent studies [3,6] have shown, however, that the crystal protein is immunologically and biochemically similar to a substantial protein fraction which can be removed from spores by extraction with reagents which dissolve the crystal protein. The precise extent and nature of this similarity remain to be established. Treatment of whole spores with urea-mercaptoethanol [7] removes some of this protein and produces spores which have altered germination requirements and different sensitivity to lysozyme, while retaining viability and heat resistance.It thus appears that the crystal protein may have some physiological function in the spore and that crystal formation may result from uncontrolled synthesis of spore protein.I n Bacillus subtilis it has been established that, under given conditions, there is a definite sequence of biochemical [8-101 events during sporulation. I n several spore-forming bacteria, including B. cereus [Ill and Bacillus subtilis [12,13], t...

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SEROLOGICAL STUDIES ON THE FORMATION OF PROTEIN PARASPORAL INCLUSIONS IN BACILLUS THURINGIENSIS

Cited by 22 publications

References 11 publications

Immunological Homology Between Crystal and Spore Protein of Bacillus thuringiensis

Immunological Homology Between Crystal and Spore Protein of Bacillus thuringiensis

Regulation of protoxin synthesis in Bacillus thuringiensis

Formation of the Parasporal Inclusion of Bacillus thuringiensis

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