Plasmid-encoded lysostaphin endopeptidase gene of Staphylococcus simulans biovar staphylolyticus

Heath, Lucie S.

doi:10.1016/0378-1097(87)90214-x

Cited by 21 publications

(39 citation statements)

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“…The genes for lysostaphin (end) in S. simulans bv. staphylolyticus and for ALE-1 (ale-1) in S. capitis EPK1 were found to be located on large plasmids (20,22,35). This was in contrast to a previous finding where the gene for lysostaphin was found to be located on the chromosome of S. simulans bv.…”

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confidence: 74%

“…staphylolyticus is resistant to lysis by lysostaphin (37), and this resistance is conferred by modifying the amino acid composition of interpeptide chains in cell wall peptidoglycan by increasing the serine content and decreasing the glycine content (11). The genetic elements for production and self-protection (immunity) of both lysostaphin and ALE-1 have been characterized (11,22,47,50). The gene involved in the modification of peptidoglycan (epr, for endopeptidase resistance) was shown to be located on a large plasmid, pACK1, together with the gene (end) which encodes the endopeptidase (22).…”

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“…The genetic elements for production and self-protection (immunity) of both lysostaphin and ALE-1 have been characterized (11,22,47,50). The gene involved in the modification of peptidoglycan (epr, for endopeptidase resistance) was shown to be located on a large plasmid, pACK1, together with the gene (end) which encodes the endopeptidase (22). Staphylococcus aureus cells transformed with a plasmid containing the 8.4-kb DNA fragment from pACK1 produced lysostaphin and were resistant to lysis by lysostaphin, which indicated that the DNA fragment contained both epr and end (11).…”

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Self-Protection against Cell Wall Hydrolysis in Streptococcus milleri NMSCC 061 and Analysis of the Millericin B Operon

Beukes

Hastings

2001

Appl Environ Microbiol

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Several bacterial species produce peptidoglycan hydrolases that lyse target cells (4,8,10,33,43). The physiological functions of these enzymes remain largely unknown. The suggestion that bacteria use them to gain a competitive advantage in environments where nutrients are limited has been made previously (49). They may also allow producer organisms to establish an ecological niche within a competitive environment (49).Millericin B, a peptidoglycan hydrolase produced by Streptococcus milleri NMSCC061, was purified and partially characterized as an endopeptidase that cleaves the interpeptide cross bridge and the stem peptide of susceptible peptidoglycan (6). This suggests that millericin B has activity similar to that of lysostaphin and ALE-1, both of which are glycylglycine endopeptidases that are produced by Staphylococcus simulans bv. staphylolyticus and Staphylococcus capitis EPK1, respectively (43, 47), as well as zoocin A, an endopeptidase produced by Streptococcus equi subsp. zooepidemicus 4881 (4).Molecular cloning of the ale-1 gene showed that the primary structure of the mature ALE-1 is very similar to that of the proenzyme form of lysostaphin. The genes for lysostaphin (end) in S. simulans bv. staphylolyticus and for ALE-1 (ale-1) in S. capitis EPK1 were found to be located on large plasmids (20,22,35). This was in contrast to a previous finding where the gene for lysostaphin was found to be located on the chromosome of S. simulans bv. staphylolyticus (24).S. simulans bv. staphylolyticus is resistant to lysis by lysostaphin (37), and this resistance is conferred by modifying the amino acid composition of interpeptide chains in cell wall peptidoglycan by increasing the serine content and decreasing the glycine content (11). The genetic elements for production and self-protection (immunity) of both lysostaphin and ALE-1 have been characterized (11,22,47,50). The gene involved in the modification of peptidoglycan (epr, for endopeptidase resistance) was shown to be located on a large plasmid, pACK1, together with the gene (end) which encodes the endopeptidase (22). Staphylococcus aureus cells transformed with a plasmid containing the 8.4-kb DNA fragment from pACK1 produced lysostaphin and were resistant to lysis by lysostaphin, which indicated that the DNA fragment contained both epr and end (11).The objective of this study was to determine whether the genes for millericin B and millericin B host immunity in S. milleri NMSCC 061 are similar in organization to the genes for lysostaphin and lysostaphin host immunity in S. simulans bv. staphylolyticus and the genes for ALE-1 and ALE-1 host immunity in S. capitis EPK1 (46,47,50). Here we describe the sequencing of the millericin B gene (milB) and the identification and sequencing of three additional genes in S. milleri NMSCC 061 that appear to be associated with millericin B host self-protection and its export. One of these genes (milF, for millericin B immunity factor), which is similar in sequence to genes that have been implicated in the synthesis of peptido...

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Self-Protection against Cell Wall Hydrolysis in Streptococcus milleri NMSCC 061 and Analysis of the Millericin B Operon

Beukes

Hastings

2001

Appl Environ Microbiol

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“…DNA was prepared from staphylococci that had been treated with acetone, lysozyme, and SDS as previously described (22). Hybridization analyses were performed essentially as described by Ausubel et al (6).…”

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confidence: 99%

Ribotype Delineation and Description of Staphylococcus sciuri Subspecies and Their Potential as Reservoirs of Methicillin Resistance and Staphylolytic Enzyme Genes

Kloos

Ballard

Webster

et al. 1997

International Journal of Systematic Bacteriology

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Three subspecies of Staphylococcus sciuri, S. sciuri subsp. sciuri Moos, Schleifer, and Smith 1976, 23& emend. Moos et al. 1996, S. sciuri subsp. curnaticus subsp. nov., and S. sciuri subsp. rodentium subsp. nov., are described on the basis of their ribotype patterns, DNA-DNA liquid hybridization data, and phenotypic characteristics. Normalized ribotyping subdivided the S. sciuri patterns into three blocks of patterns, each corresponding to a subspecies. Each subspecies formed a separate, well-defined DNA similarity group when DNA-DNA hybridizations were conducted under stringent (7OOC) reassociation conditions. S. sciuri subsp. sciuri could be distinguished from the other subspecies on the basis of its ability to produce acid from D-cellobiose, alkaline phosphatase activity, and inability to produce either clumping factor or protein A. S. sciuri subsp. curnaticus could be distinguished by its ability to produce acid aerobically from D-xylose and maltose, inability to produce acid from D-melezitose, and smaller colony size on P agar. S. sciuri subsp. rodentium could be distinguished by its positive reaction in the latex agglutination test for clumping factor and/or protein A and generally higher frequencies and levels of oxacillin and methicillin resistance. All 40 strains of S. sciuri tested (including representatives of all three subspecies) hybridized with the mecA gene probe. All strains of S. sciuri subsp. sciuri, 79% of the strains of S. sciuri subsp. carnuticus and 89% of the strains of S. sciuri subsp. rodentium exhibited extracellular, staphylolytic enzyme activity. This activity was associated with an enzyme(s) that immunoblotted with a lysostaphin-specific monoclonal antibody; however, only three strains hybridized with a lysostaphin (end) gene probe. The type strain of S. sciuri subsp. curnaticus is DD 791 (= ATCC 700058), and the type strain of S. sciuri subsp. rodentium is DD 4761 (= ATCC 700061).Staphylococcus sciuri is generally considered one of the most primitive Staphylococcus species; it is widely distributed in nature, is capable of growth on inorganic nitrogen salts as the sole source of nitrogen, and exhibits a wide range of biochemical activities (31-33). In the past 20 years since its original description (33), numerous laboratories have reported frequent isolation of this species from foods, farm animals, rodents, marsupials, marine mammals, and birds and occasional isolation from humans and their pets (1,2, 17,28,31,35,48,52,57,58).Most resident populations of S. sciuri are members of the normal cutaneous microflora of lower mammals. This species is rarely associated with infections. A preliminary investigation of a large collection of S. sciuri strains showed that a ribotyping method based on an analysis of genomic EcoRI fragments containing portions of the rRNA operons could be used to distinguish two major subgroups and additional strain variation within the species (10).In this study, we describe three subpopulations of S. sciuri which can be distinguished on the basis of their rib...

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“…Endopeptidase, hexosaminidase and extra- cellular sulphydryl protease activities are produced coordinately under a variety of conditions [5][6][7][8][9][10]. However, the corresponding genes are not in the same unit of transcription because the endopeptidase gene resides on a plasmid whereas the genes for hexosaminidase and protease are on the chromosome [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Extracellular proteolytic activation of bacteriolytic peptidoglycan hydrolases ofStaphylococcus simulansbiovarstaphylolyticus

Neumann

Heath

LeBlanc

et al. 1993

FEMS Microbiology Letters

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Staphylococcus simulans biovar staphylolyticus secreted two bacteriolytic peptidoglycan hydrolases as proproteins that were activated as they were processed by an extracellular sulphydryl protease. This processing resulted in the production of multiple molecular-mass forms of each enzyme. Cells from early exponential phase cultures were susceptible to lysis by the mature forms of each of the peptidoglycan hydrolases whereas stationary phase cells were resistant. Thus secretion of these bacteriolytic enzymes during early exponential growth as precursors that are activated later by the protease would provide time for the cells to become resistant.

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Plasmid-encoded lysostaphin endopeptidase gene of Staphylococcus simulans biovar staphylolyticus

Cited by 21 publications

References 4 publications

Self-Protection against Cell Wall Hydrolysis in Streptococcus milleri NMSCC 061 and Analysis of the Millericin B Operon

Self-Protection against Cell Wall Hydrolysis in Streptococcus milleri NMSCC 061 and Analysis of the Millericin B Operon

Ribotype Delineation and Description of Staphylococcus sciuri Subspecies and Their Potential as Reservoirs of Methicillin Resistance and Staphylolytic Enzyme Genes

Extracellular proteolytic activation of bacteriolytic peptidoglycan hydrolases ofStaphylococcus simulansbiovarstaphylolyticus

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