The streptococcolytic enzyme zoocin A is a penicillin-binding protein

Heath, Lucie S.; Heath, Harry E.; LeBlanc, Paul A.; Smithberg, S. Rochelle; Dufour, Muriel; Simmonds, Robin S.; Sloan, Gary L.

doi:10.1016/j.femsle.2004.05.038

Cited by 9 publications

(12 citation statements)

References 20 publications

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“…The genes encoding for immunity factors are commonly adjacent to the bacteriocin peptidase gene (Fig. 5B) although they may not always be in the same orientation (Recsei et al, 1987;Heath et al, 1989Heath et al, , 2004Sugai et al, 1997b). Analysis of the T. denticola genome shows that immediately downstream of TDE1738, the gene TDE1739 encodes a protein with similarity to lysostaphin immunity factor (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The T. pallidum genome also contains a gene, Tp0806, that encodes a protein with homology to lysostaphin immunity factor. The ZoocinA immunity factor (Zif) acts as a penicillinbinding protein (Heath et al, 2004) capable of peptidoglycan reorganization, and downstream and in the same orientation as the T. pallidum M23 peptidase gene Tp0706 (homologous to TDE1738) is a gene, Tp0705 (Fig. 5C), annotated as a penicillin-binding protein, suggesting a role in protection from autolysis.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of a novel family of fibronectin‐binding proteins with M23 peptidase domains from Treponema denticola

Bamford

Francescutti

Cameron

et al. 2010

Molecular Oral Microbiology

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SUMMARY Interactions with fibronectin are important in the virulence strategies of a range of disease-related bacteria. The periodontitis-associated oral spirochaete Treponema denticola expresses at least two fibronectin-binding proteins, designated Msp (major surface protein) and OppA (oligopeptide-binding protein homologue). To identify other T. denticola outer membrane fibronectin-binding proteins, the amino acid sequence of the Treponema pallidum fibronectin-binding protein Tp0155 was used to survey the T. denticola genome. Seven T. denticola genes encoding orthologous proteins were identified. All but two were expressed in Escherichia coli and purified recombinant proteins bound fibronectin. Using antibodies to the N-terminal region of Tp0155, it was demonstrated that T. denticola TDE2318, with highest homology to Tp0155, was cell surface localized. Like Tp0155, the seven T. denticola proteins contained an M23 peptidase domain and four (TDE2318, TDE2753, TDE1738, TDE1297) contained one or two LysM domains. M23 peptidases can degrade peptidoglycan whereas LysM domains recognize carbohydrate polymers. In addition, TDE1738 may act as a bacteriocin based on homology with other bacterial lysins and the presence of an adjacent gene encoding a putative immunity factor. Collectively, these results suggest that T. denticola expresses fibronectin-binding proteins associated with the cell surface that may also have cell wall modifying or lytic functions.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Characterization of a novel family of fibronectin‐binding proteins with M23 peptidase domains from Treponema denticola

Bamford

Francescutti

Cameron

et al. 2010

Molecular Oral Microbiology

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“…Streptococcus oralis have direct cross-links in their peptidoglycan rather than the di-or tri-alanine usual for streptococci (Schleifer & Kandler, 1972). If zoocin A is a D-alanyl endopeptidase, as is believed (Heath et al, 2004), the presence of a direct crosslink in the peptidoglycan of these strains would explain the inability of zoocin A to cleave this substrate, despite its ability to bind to it.…”

Section: Binding To and Digestion Of Peptidoglycan By Zoocin Amentioning

confidence: 97%

“…Streptococcus equi ssp. zooepidemicus 4881.1KOE is a zif-zooA knockout mutant of the zoocin A producer strain (Heath et al, 2004).…”

Section: Bacterial Strains and Growth Conditionsmentioning

confidence: 99%

Targeting of streptococci by zoocin A

Åkesson

Dufour

Sloan

et al. 2007

FEMS Microbiology Letters

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Zoocin A is a domain-structured peptidoglycan hydrolase produced by Streptococcus equi ssp. zooepidemicus 4881. [(14)C]-zoocin A was used to measure the amount of zoocin A bound to the surface of cells and to purified peptidoglycan. The sensitivity of various streptococci to zoocin A correlated with the amount of zoocin A bound (R(2)=0.8609). Peptidoglycan purified from Streptococcus oralis and Streptococcus rattus were able to bind zoocin A but remained resistant to hydrolysis. All Streptococcus pyogenes strains were extremely sensitive to zoocin A with minimum inhibition concentrations of 31.5 ng mL(-1) or less, suggesting that zoocin A may have potential for use as an enzybiotic.

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“…Furthermore, incubation of zoocin A with penicillin decreased its enzymatic activity (Heath et al 2004 ). Zoocin A was shown to be capable of killing S. mutans in a triple -species plaque model (this species is involved in the pathogenesis of dental caries; Simmonds et al 1995 ).…”

Section: Other Bacteriocinsmentioning

confidence: 99%