Characteristics of extracellular protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus

Nitterauer, James D.

doi:10.1016/0378-1097(91)90388-q

Cited by 4 publications

(7 citation statements)

References 8 publications

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“…This resistance apparently is due to some change in a non-peptidoglycan component in the cell wall because peptidoglycan isolated from resistant cells is readily hydrolyzed by the enzyme [27]. Although the basis for resistance to hexosaminidase is unknown, it is not the same as that for endopeptidase because cells cured of pACK1 are able to produce hexosaminidase yet grow normally [13]. Nevertheless, cells from the early exponential phase of growth are susceptible to lysis by endopeptidase or hexosaminidase and produce pro-endopeptidase and prohexosaminidase; therefore, there must be a mechanism to allow time for the cells to develop resistance before harmful concentrations of endopeptidase and hexosaminidase accumulate.…”

Section: Discussionmentioning

confidence: 97%

“…simulans biovar staphylolyticus secretes pro-endopeptidase (M r 59 K), which is proteolytically processed to endopeptidase (M r 26 K) [5,14,15]. In our studies of extracellular protein production by this organism, we have detected only one proteolytic activity, which is due to sulphydryl protease [7][8][9][10]13]. Zhou et al [16] purified this enzyme and showed that it converted purified proendopeptidase to endopeptidase.…”

Section: Introductionmentioning

confidence: 97%

“…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%

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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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Section: Discussionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

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Extracellular proteolytic activation of bacteriolytic peptidoglycan hydrolases ofStaphylococcus simulansbiovarstaphylolyticus

Neumann

Heath

LeBlanc

et al. 1993

FEMS Microbiology Letters

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“…If lss is expressed in S. carnosus (see over), which lacks staphylolyticus ATCCI 362, the cysteine protease, which appears to be chromosomally encoded (Nitterauer et a/., 1991), was purified to homogeneityfrom the culture supernatant of s. simulans biovar staphylolyticus (ApACKl) in two chromatographic steps (not shown). This strain, which lacks the Iss-carrying plasmid pACK1, was chosen to avoid mixing of the cysteine protease and the lysostaphin.…”

Section: Processing Of Prolysostaphin By the Cysteine Proteasementioning

confidence: 99%

Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus

Thumm¹,

Götz²

1997

Molecular Microbiology

155

162

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SummaryLysostaphin is an extracellular glycylglycine endopeptidase produced by Staphylococcus simulans biovar staphyIolyticus ATCC1362 that lyses staphylococcal cells by hydrolysing the polyglycine interpeptide bridges of the peptidoglycan. Renewed analysis of the sequence of the lysostaphin gene (Iss), and the sequencing of the amino-terminus of purified prolysostaphin and of mature lysostaphin revealed that lysostaphin is organized as a preproprotein of 493 amino acids (aa), with a signal peptide consisting of 36aa, a propeptide of 21 1 aa from which 195 aa are organized in 15 tandem repeats of 13 aa length, and a mature protein of 246aa. Prolysostaphin is processed in the culture supernatant of S. simulans biovar StaphyIoIyficus by an extracellular cysteine protease. Although prolysostaphin was staphylolytically active, the mature lysostaphin was about 4.5-fold more active. The controlled expression in Staphylococcus carnosus of lss and lss with deletions in the prepropeptide region indicated that the tandem repeats of the propeptide are not necessary for protein export or activation of Lss, but keep Lss in a less active state. lntracellularly expressed pro-and mature lysostaphin exert staphylolytic activity in cell-free extracts, but do not affect growth of the corresponding clones. We characterized a lysostaphin immunity factor gene ( / i f ) which is located in the opposite direction to lss. The expression of /if in s. carnosus led to an increase in the serine/glycine ratio of the interpeptide bridges of peptidoglycan from 2 to 35%, suggesting that lysostaphin immunity depends on serine incorporation into the interpeptide bridge. If, in addition to /if, Iss is coexpressed the serinelglycine ratio is further increased to 58%, suggesting that Lss selects for optimal serine incorporation. Lif shows similarity to FemA and FemB

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“…To prove that epr sc was in fact responsible for the increased serine content in the peptidoglycan crossbridges, we attempted to cure pACK6 from strain DD 4747 by a number of different methods that previously had been successful in curing other plasmids from staphylococci [23]. None of these methods was successful.…”

Section: Resultsmentioning

confidence: 99%

Plasmid-specified FemABX-like immunity factor inStaphylococcus sciuriDD 4747

Heath

Gargis

Smithberg

et al. 2005

FEMS Microbiology Letters

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A plasmid from Staphylococcus sciuri DD 4747 had three open reading frames: a replication gene, an N-acetylmuramyl-l-alanine amidase-like gene, and a gene similar to the lysostaphin endopeptidase resistance gene (epr/lif). The epr-like gene was introduced into S. aureus RN4220; the recombinant strain was more resistant to lysostaphin endopeptidase and its cell wall peptidoglycan contained more serines and fewer glycines than the parental strain with the shuttle vector alone. Based on both its function and its similarity to femAB, this gene is a member of the femABX-like immunity gene family. Furthermore, this is the first example of a femABX-like immunity gene that is not linked to the gene for the bacteriolytic enzyme against which it specifies immunity.

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Characteristics of extracellular protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus

Cited by 4 publications

References 8 publications

Extracellular proteolytic activation of bacteriolytic peptidoglycan hydrolases ofStaphylococcus simulansbiovarstaphylolyticus

Extracellular proteolytic activation of bacteriolytic peptidoglycan hydrolases ofStaphylococcus simulansbiovarstaphylolyticus

Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus

Plasmid-specified FemABX-like immunity factor inStaphylococcus sciuriDD 4747

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