Lysostaphin: A New Bacteriolytic Agent for the Staphylococcus

Schindler, Charles A.; Schuhardt, V. T.

doi:10.1073/pnas.51.3.414

Cited by 429 publications

(305 citation statements)

References 17 publications

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“…Since the 1960s, one compound that has attracted attention as a potential anti-staphylococcal treatment is the endopeptidase lysostaphin [1,2]. This 27 kDa enzyme specifically cleaves crosslinking pentaglycine bridges that are found exclusively in the staphylococcal cell wall [3].…”

Section: Introductionmentioning

confidence: 99%

Bactericidal synergy of lysostaphin in combination with antimicrobial peptides

Desbois

Coote

2011

Eur J Clin Microbiol Infect Dis

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Drug-resistant staphylococci are a serious problem that urgently requires the discovery of new therapeutic agents. There has been resurgence in interest for using lysostaphin (a specific anti-staphylococcal enzyme) as a treatment for infections caused by these important pathogens. However, bacterial resistance to lysostaphin is a problem but the use of a combination treatment may surmount this issue. In this present study, using viable counts from suspension incubations, lysostaphin is shown to be synergistically bactericidal in combination with various conventional antimicrobial peptides, the antimicrobial protein bovine lactoferrin, a lantibiotic (nisin), and certain lipopeptides used clinically (colistin, daptomycin and polymyxin B). Combinations that act in synergy are of clinical importance as these reduce the doses of the compounds needed for effective treatments and, most importantly, decrease the chances of resistance being selected. The use of lysostaphin in combination with a peptide may represent a new avenue to tackling drug-resistant staphylococci.

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Section: Introductionmentioning

confidence: 99%

Bactericidal synergy of lysostaphin in combination with antimicrobial peptides

Desbois

Coote

2011

Eur J Clin Microbiol Infect Dis

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“…For example, the glycyl-glycine endopeptidase lysostaphin from Staphylococcus simulans hydrolyses the transpeptide bridges of certain staphylococcal cell walls (Schindler & Schuhardt, 1964;Zygmunt & Tavormina, 1972), whereas the bacteriocins zoocin A from Streptococcus zooepidemicus (Simmonds et al, 1996(Simmonds et al, , 1997 and stellalysin from Streptococcus constellatus (Heng et al, 2006b) are thought to act in a similar manner against various susceptible streptococci. In addition, the cyclic antimicrobial peptide uberolysin from various Streptococcus uberis strains kills susceptible cells by inducing their lysis (Wirawan et al, 2007).…”

Section: Sa-m57 Enterococcin V583 Corynicin Jk and Ypkk[val88-trp16mentioning

confidence: 99%

“…Several bacteriocins that have proven to be cell-wallhydrolysing (murolytic) enzymes, such as lysostaphin, zoocin A and stellalysin, have been reported from Grampositive bacteria (Schindler & Schuhardt, 1964;Simmonds et al, 1996;Heng et al, 2006b). Historically, staphylococcin 1580 from Staphylococcus epidermidis (Jetten & Vogels, 1972a, b;Jetten et al, 1972) was reported to be a bacteriocin with a subunit molecular mass of~20 kDa that formed multimeric structures of 300-400 kDa in conjunction with carbohydrate and lipid.…”

Section: Introductionmentioning

confidence: 99%

ef1097 and ypkK encode enterococcin V583 and corynicin JK, members of a new family of antimicrobial proteins (bacteriocins) with modular structure from Gram-positive bacteria

et al. 2007

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“…The N-terminal sequence of enterolysin A contains a domain which is found in members of the M37 family of metallopeptidases which have Zn 2+ in their catalytic sites (Recsei et al, 1987;Sugai et al, 1997). Members of this family include lysostaphin (Schindler & Schuhardt, 1964;Schleifer & Kandler, 1972;Schleifer & Fischer, 1982;Baba & Schneewind, 1996) and zoocin A (Simmonds et al, 1997) whose conserved N-terminal domain provides the enzymic functions of the proteins and contains a His-Xxx-His motif which may serve as the Zn 2+ ligand (Sugai et al, 1997).…”

Section: Dpc5280 Contains the Genetic Determinants For Cytolysin Prodmentioning

confidence: 99%

Production of enterolysin A by a raw milk enterococcal isolate exhibiting multiple virulence factors

et al. 2003

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Even though enterococci are a common cause of human infection they can readily be isolated from a range of food sources, including various meat and dairy products. An enterococcal strain, DPC5280, which exhibits a broad spectrum of inhibition against many Gram-positive bacteria was recently isolated from an Irish raw milk sample. Characterization of the inhibition revealed that the strain exhibits haemolytic activity characteristic of the two-component lantibiotic cytolysin and also produces a heat-labile antimicrobial protein of 34 kDa. The latter protein displayed cell wall hydrolytic activity, as evidenced by zymogram gels containing autoclaved lactococcal cells. N-terminal sequencing of the purified protein yielded the sequence ASNEWS which is 100 % identical to enterolysin A (accession no. AF249740), a protein which shares 28 and 29 % identity to the Gly-Gly endopeptidases, lysostaphin and zoocin A, respectively. Indeed, amplification of entL from DPC5280 and sequencing revealed that the protein is 100 % identical to enterolysin A. The DPC5280 strain also contained the determinants associated with multiple virulence factors, including gelatinase, aggregation substance and multiple antibiotic resistance. The linkage of this cell-wall-degrading enzyme to other virulence factors in enterococci may contribute to the competitiveness of pathogenic enterococci when found in complex microbial environments such as food and the gastrointestinal tract. INTRODUCTIONDespite the fact that foods containing enterococci have a long history of safe use, these organisms are not considered as GRAS (generally recognized as safe) organisms. They can readily be isolated from a range of food sources, including raw milk, and are often a constituent of some mixed starter strains used commercially. However, many strains can act as opportunistic pathogens, causing a variety of infections such as urinary tract infections, bacteremia and infective endocarditis (Murray, 1990;Jett et al., 1994), and are of major importance in community-acquired and in hospital-acquired (nosocomial) infections (Jett et al., 1994;Low et al., 1994;Jones et al., 1997;Simjee & Gill, 1997). A contributing factor to their pathogenesis is their evolving resistance to antibiotics. For example, resistance to the antibiotic vancomycin is now widespread among members of the genus, which leaves few options for disease management (Aguirre & Collins, 1993;Knudtson & Hartman, 1993;Facklam & Sahm, 1995;Klein et al., 1998). Considerable progress has recently been made in determining the traits responsible for pathogenesis of enterococci.For example, studies have shown that phenotypes such as production of cytolysin, which has both haemolytic activity (by lysing a broad spectrum of cells, including human, horse and rabbit erythrocytes) and bactericidal activity (against Gram-positive bacteria) play a role in the progression of enterococcal infection (Ike et al., 1984;Jett et al., 1992). Cytolysin enhances the virulence of Enterococcus faecalis in animal models, such as muri...

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Lysostaphin: A New Bacteriolytic Agent for the Staphylococcus

Cited by 429 publications

References 17 publications

Bactericidal synergy of lysostaphin in combination with antimicrobial peptides

Bactericidal synergy of lysostaphin in combination with antimicrobial peptides

ef1097 and ypkK encode enterococcin V583 and corynicin JK, members of a new family of antimicrobial proteins (bacteriocins) with modular structure from Gram-positive bacteria

Production of enterolysin A by a raw milk enterococcal isolate exhibiting multiple virulence factors

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