Temperate Bacteriophages of Bacillus subtilis

Zahler, Stanley A.

doi:10.1007/978-1-4684-5424-6_13

Cited by 13 publications

(9 citation statements)

References 134 publications

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“…B. cereus is genotypically closely related to B. thuringiensis, and it has been suggested that they be grouped into a single species (4). In contrast to the well-studied phages infecting B. subtilis (29,40), no information is available on the molecular biology and relationships of viruses for the B. cereus-B. thuringiensis group.…”

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confidence: 99%

Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli

et al. 1997

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The ply genes encoding the endolysin proteins from Bacillus cereus phages Bastille, TP21, and 12826 were identified, cloned, and sequenced. The endolysins could be overproduced in Escherichia coli (up to 20% of total cellular protein), and the recombinant proteins were purified by a two-step chromatographical procedure. All three enzymes induced rapid and specific lysis of viable cells of several Bacillus species, with highest activity on B. cereus and B. thuringiensis. Ply12 and Ply21 were experimentally shown to be N-acetylmuramoyl-L-alanine amidases (EC 3.5.1.28). No apparent holin genes were found adjacent to the ply genes. However, Ply21 may be endowed with a signal peptide which could play a role in timing of cell lysis by the cytoplasmic phage endolysin. The individual lytic enzymes (PlyBa, 41.1 kDa; Ply21, 29.5 kDa, Ply12, 27.7 kDa) show remarkable heterogeneity, i.e., their amino acid sequences reveal only little homology. The N-terminal part of Ply21 was found to be almost identical to the catalytic domains of a Bacillus sp. cell wall hydrolase (CwlSP) and an autolysin of B. subtilis (CwlA). The C terminus of PlyBa contains a 77-amino-acid sequence repeat which is also homologous to the binding domain of CwlSP. Ply12 shows homology to the major autolysins from B. subtilis and E. coli. Comparison with database sequences indicated a modular organization of the phage lysis proteins where the enzymatic activity is located in the N-terminal region and the C-termini are responsible for specific recognition and binding of Bacillus peptidoglycan. We speculate that the close relationship of the phage enzymes and cell wall autolysins is based upon horizontal gene transfer among different Bacillus phages and their hosts.Numerous bacteriophages for the genus Bacillus have been isolated, and at present, they are grouped into 33 phage species. With one exception, all of them belong to the tailed phages (1). Lytic activity is not necessarily restricted to a single species, especially with respect to the phages used for typing strains of Bacillus cereus and Bacillus thuringiensis (2, 35). B. cereus is genotypically closely related to B. thuringiensis, and it has been suggested that they be grouped into a single species (4). In contrast to the well-studied phages infecting B. subtilis (29,40), no information is available on the molecular biology and relationships of viruses for the B. cereus-B. thuringiensis group.At the end of their multiplication cycle, most bacteriophages are released from the cells through the action of endogenous cell wall hydrolases, termed endolysins or phage lysins (for a review, see reference 38). Several genes encoding lysins from phages infecting both gram-negative and gram-positive hosts have been cloned and sequenced. In some cases, the catalytic mechanisms have been determined, which place the phage lysins into three distinct groups: amidases, muramidases (glycosidases and transglycosylases), and endopeptidases (38). Recently, a fourth type of enzyme was described (L-alanoyl-Dglutamate pe...

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Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli

et al. 1997

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“…The location of the thyPIG 3 gene in that region as well as the attPIG 3 (I. Santos, unpubl, results) reveals a genomic organization for IG 3 phage quite similar to some other phages of group III as SPI3, 3 T and 9 11 [24].…”

Section: Discussionmentioning

confidence: 89%

“…SPI3 is resident in B. subtilis, R and H 2 in B. amyloliquefaciens H [24]. These phages are, however, clearly related to each other.…”

Section: Discussionmentioning

confidence: 92%

Cloning of the thymidylate synthetase gene (thyPIG 3) from theBacillus subtilis temperate phage IG 3

Santos

Lencastre

1992

Archives of Virology

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The thyPIG 3 gene from Bacillus subtilis bacteriophage IG 3 was cloned in the plasmid pHV 33. Two recombinant plasmids, pISL 61 and pISL 62 carrying that gene are effective in transforming to thymine prototrophy both Escherichia coli (by complementation) and B. subtilis (by complementation and recombination). The comparison of cloned fragment containing the thyPIG 3 gene and the thyP 3 gene from phage phi 3 T, by restriction analysis and DNA hybridization, suggests a strong homology between the two. The thyPIG 3 gene was mapped in this study in the central region of the IG 3 genome.

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“…We produced lysates of phage H2 by mitomycin-C-induced lysis of B. arnyloliquefaciens strain CU8004 (= strain H), and produced a B. subtilis lysogen of H2 that we call CU7004 (Zahler et al, 1987). Although H2 lysates produced faint clearing of overlays of strain CU1050 (our usual plating bacterium for phage SPQ; Rosenthal et al, 1979) or strain CU1065, we could not detect individual plaques.…”

Section: Production Of Strain Cu3431mentioning

confidence: 91%

“…We have studied temperate bacteriophage production in several strains of Bacillus amyloliquefaciens, a bacterium often used in industrial fermentations (Zahler et al, 1987), and have selected a phage released by strain H for detailed examination; this phage was named phage H2.…”

Section: Introductionmentioning

confidence: 99%

H2, a Temperate Bacteriophage Isolated from Bacillus amyloliquefaciens Strain H

Zahler

Korman²,

Thomas³

et al. 1987

Microbiology

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Bacillus amyloliquefaciens strain H is lysogenic for a large temperate phage we call H2. H2 has a polyhedral head 85 nm in diameter and a tail of about 17 x 434 nm. H2 lysogenizes Bacillus subtilis between the tyrA and metB genes, and gives specialized transduction of metB and, at lower frequencies, of ilvD and ilvA. The phage carries a thymidylate synthase gene and converts thymine auxotrophs of B. subtilis to prototrophy. The H2 genome is a linear DNA molecule about 129 kb in length. DNA extracted from phage particles grown in B. subtilis is not cut by the restriction endonucleases HaeIII, Fnu4HI, Bsp1286I, and BamHI; the latter enzyme is produced by B. amyloliquefaciens strain H. The prophage in lysogenic B. subtilis cells can be cut by these enzymes. We have isolated H2 mutants that carry the transposon Tn917, or a mutation resulting in clear-plaque morphology, or both.

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Temperate Bacteriophages of Bacillus subtilis

Cited by 13 publications

References 134 publications

Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli

Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli

Cloning of the thymidylate synthetase gene (thyPIG 3) from theBacillus subtilis temperate phage IG 3

H2, a Temperate Bacteriophage Isolated from Bacillus amyloliquefaciens Strain H

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