A Search Within the Genera<i>Streptococcus, Enterococcus</i>and<i>Lactobacillus</i>for Organisms Inhibitory to Mutans Streptococci

James, S. M.; Tagg, John

doi:10.3109/08910608809141531

Cited by 10 publications

(9 citation statements)

References 33 publications

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“…Previously it was reported that S. rattus strain BHT inhibited a wide variety of MS indicators, but not strain BHT itself when tested by deferred antagonism on BACa medium [James and Tagg, 1988]. In the present study it was confirmed that strain BHT has strong anti-MS activity and it was established that this activity is stronger on TSYCa than on BACa.…”

Section: Discussionsupporting

confidence: 76%

“…However, despite the high overall incidence of BLIS production in these genera, only 6.5% of streptococci, enterococci and lactobacilli when tested on BACa appeared to produce anti-MS inhibitory activity [James and Tagg, 1988]. In the present study 9.9% of the 272 streptococci, enterococci and staphylococci displayed anti-MS activity on BACa medium.…”

Section: Discussionmentioning

confidence: 66%

“…zooepidemicus strain 4881 has inhibitory activity against S. mutans and S. sobrinus, but not S. rattus [James and Tagg, 1988]. The strain 4881 inhibitory agent (zoocin A) has subsequently been purified and its molecular weight estimated by SDS-PAGE as approximately 30,000 D. Two minutes' application of zoocin A in an artificial plaque test system brought about a specific decrease in the count of MS for up to 20 h [Simmonds et al, 1995].…”

Section: Discussionmentioning

confidence: 99%

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Diverse Activity Spectra of Bacteriocin–Like Inhibitory Substances Having Activity against Mutans Streptococci

Balakrishnan

Rs²,

Tagg³

2000

Caries Res

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Mutans streptococci (MS) are known to be causative agents of dental caries. It has been suggested that these cariogenic bacteria could be eliminated from dental plaque by application of bacteriocins or bacteriocin–like inhibitory substances (BLIS). In the present study 272 bacterial strains of the genera Streptococcus, Enterococcus and Staphylococcus were tested for their production of BLIS activity against MS by use of a deferred antagonism test on agar media supplemented with either whole blood or yeast extract. Although only 14.3% of the test strains displayed anti–MS activity, the inhibitory agents produced by these strains were characterised by considerable diversity in the range of their inhibitory action against both MS and other common oral streptococcal species. It is suggested that combinations of relatively specifically targeted anti–MS BLIS may have potential application to the prevention of dental caries.

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Section: Discussionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 66%

Section: Discussionmentioning

confidence: 99%

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Diverse Activity Spectra of Bacteriocin–Like Inhibitory Substances Having Activity against Mutans Streptococci

Balakrishnan

Rs²,

Tagg³

2000

Caries Res

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“…The Lancefield group C streptococcus Streptococcus zooepidemicus 4881 has been shown to produce inhibitory activity against strains of a variety of streptococcal species, including all Streptococcus pyogenes strains, all mutans streptococcal strains except Streptococcus rattus, and all S. zooepidemicus strains other than strain 4881 itself (11). The molecule responsible for this activity, zoocin A, was subsequently purified and characterized (25).…”

mentioning

confidence: 99%

Mode of action of a lysostaphin-like bacteriolytic agent produced by Streptococcus zooepidemicus 4881

Simmonds

Pearson

Kennedy

et al. 1996

Appl Environ Microbiol

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Electron microscopy of zoocin A-treated sensitive streptococcus cells revealed cytoplasmic disruption and ultimately complete rupture of the cell wall. Culture viability and optical density were shown to decrease rapidly and simultaneously in Streptococcus pyogenes FF22 but less quickly in the relatively more resistant Streptococcus mutans 10449. Zoocin A was shown to cleave hexaglycine in a colorimetric cell-free microtiter assay system, and it is concluded that the killing action of zoocin A, like that of lysostaphin, is most probably the result of direct cleavage of the peptidoglycan cross-links in the cell wall. The relationship between sensitivity to zoocin A and the peptidoglycan cross-linkage structure of Streptococcus zooepidemicus, Lactococcus spp., S. pyogenes, Streptococcus gordonii, Streptococcus oralis, S. mutans, and Streptococcus rattus has been evaluated.

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“…Zoocin A has been shown to inhibit the growth of all Streptococcus pyogenes strains and all S. zooepidemicus strains other than 4881 itself (14). Both enzymes, lysostaphin and zoocin A, possess a catalytic domain in the N-terminal portion and a substrate recognition domain in the C-terminal region.…”

mentioning

confidence: 99%

Purification and Partial Characterization of a Murein Hydrolase, Millericin B, Produced by Streptococcus milleri NMSCC 061

Beukes

Bierbaum

Sahl

et al. 2000

Appl Environ Microbiol

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Streptococcus milleri NMSCC 061 was screened for antimicrobial substances and shown to produce a bacteriolytic cell wall hydrolase, termed millericin B. The enzyme was purified to homogeneity by a four-step purification procedure that consisted of ammonium sulfate precipitation followed by gel filtration, ultrafiltration, and ion-exchange chromatography. The yield following ion-exchange chromatography was 6.4%, with a greater-than-2,000-fold increase in specific activity. The molecular weight of the enzyme was 28,924 as determined by electrospray mass spectrometry. The amino acid sequences of both the N terminus of the enzyme (NH 2 SENDFSLAMVSN) and an internal fragment which was generated by cyanogen bromide cleavage (NH 2 SIQTNAPWGL) were determined by automated Edman degradation. Millericin B displayed a broad spectrum of activity against gram-positive bacteria but was not active against Bacillus subtilis W23 or Escherichia coli ATCC 486 or against the producer strain itself. N-Dinitrophenyl derivatization and hydrazine hydrolysis of free amino and free carboxyl groups liberated from peptidoglycan digested with millericin B followed by thin-layer chromatography showed millericin B to be an endopeptidase with multiple activities. It cleaves the stem peptide at the N terminus of glutamic acid as well as the N terminus of the last residue in the interpeptide cross-link of susceptible strains.Most eubacteria are mechanically stabilized by the shapedetermining peptidoglycan, which consists of polysaccharide chains that are connected by short peptides. Expansion of the bacterial cell wall during growth and splitting of the septum prior to cell separation require enzymes that cleave some of the existing covalent bonds within the peptidoglycan sacculus. These enzymes are collectively known as peptidoglycan hydrolases (24). Some have been characterized as N-acetylmuramidases, N-acetylglucosaminidases, N-acetylmuramyl-L-alanine amidases, endopeptidases, and transglycosidases (10). Most peptidoglycan hydrolases have been characterized as bacteriolytic enzymes by in vitro studies (29). Lysostaphin, which is active against Staphylococcus aureus, is one such enzyme. It has been suggested that lysostaphin may function catabolically to release nutrients from other staphylococci in the environment, with the producer cell being protected by a specific immunity protein (12,18). The lytic effect of lysostaphin results from a direct attack on the integrity of the staphylococcal cell wall, specifically bringing about cleavage of the pentaglycine crosslink between the stem peptides of individual peptidoglycan subunits (4).Zoocin A, a bacteriolytic cell wall hydrolase produced by Streptococcus zooepidemicus 4881, like lysostaphin, cleaves bonds within the peptide moiety of peptidoglycan (26). Zoocin A has been shown to inhibit the growth of all Streptococcus pyogenes strains and all S. zooepidemicus strains other than 4881 itself (14). Both enzymes, lysostaphin and zoocin A, possess a catalytic domain in the N-terminal portion and a...

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A Search Within the GeneraStreptococcus, EnterococcusandLactobacillusfor Organisms Inhibitory to Mutans Streptococci

Cited by 10 publications

References 33 publications

Diverse Activity Spectra of Bacteriocin–Like Inhibitory Substances Having Activity against Mutans Streptococci

Diverse Activity Spectra of Bacteriocin–Like Inhibitory Substances Having Activity against Mutans Streptococci

Mode of action of a lysostaphin-like bacteriolytic agent produced by Streptococcus zooepidemicus 4881

Purification and Partial Characterization of a Murein Hydrolase, Millericin B, Produced by Streptococcus milleri NMSCC 061

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