Bacteriocins from human and rodent streptococci

Kelstrup, J.; Gibbons, R. J.

doi:10.1016/0003-9969(69)90227-1

Cited by 93 publications

(44 citation statements)

References 18 publications

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“…Some of the observed inhibitory patterns may have been attributable to the combined action of two or more distinct inhibitory substances. Studies of the production of bacteriocine-like substances by a-haemolytic streptococci (Kelstrup and Gibbons, 1969;Rogers, 1976) have also indicated that the observed spectra of inhibitory activity may represent the combined action of two or more distinct inhibitors.…”

Section: Discussionmentioning

confidence: 99%

"Fingerprinting" -haemolytic streptococci by their production of and sensitivity to bacteriocine-like inhibitors

Tagg¹,

Bannister²

1979

Journal of Medical Microbiology

152

163

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Section: Discussionmentioning

confidence: 99%

"Fingerprinting" -haemolytic streptococci by their production of and sensitivity to bacteriocine-like inhibitors

Tagg¹,

Bannister²

1979

Journal of Medical Microbiology

152

163

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“…Mutacin was thermostable (as indicated by analysis for residual activity after incubation in a boiling water bath for up to 30 min). It was stable after 24 h of incubation in different buffers (with a pH range of 4 to 10) at room temperature. Mutacin residual activity after incubation at pH 11 for 24 h dropped to about 50% activity.…”

Section: Resultsmentioning

confidence: 98%

“…These antimicrobial substances may be important for sustained colonization of indigenous bacteria in a densely populated milieu typified by plaque accumulation on the surfaces of teeth (17,24). In addition, these inhibitory substances may serve to exclude nonindigenous, potential pathogens from colonizing a susceptible host (37).…”

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confidence: 99%

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Isolation and biochemical characterization of a novel lantibiotic mutacin from Streptococcus mutans

1994

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Certain members of the indigenous biota of humans produce antimicrobial substances called bacteriocins, which inhibit other bacteria, including members of their own species. One of these substances, mutacin, is made by Streptococcus mutans, a member of the oral biota. Mutacin inhibits other mutans streptococci as well as many gram-positive exogenous pathogens. Here, we report for the first time the purification and partial biochemical characterization of a lanthionine-containing mutacin peptide from S. mutans T8. The biologically active peptide was-isolated from the broth cultures by ultrafiltration and differential precipitation. The final mutacin preparation was homogeneous as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and N-terminal amino acid sequencing. A molecular mass of the peptide was estimated by electrospray ionization mass spectroscopy to be 3,244.64 + 1.15 Da. Its amino acid composition indicates the presence of lanthionine and likely ,B-methyllanthionine in a total of about 25 amino acids. Because a,,B-unsaturated amino acids, the precursors of lanthionine residues, are often found in lantibiotics, we carried out the addition reaction of the mutacin with N-(methyl)mercaptoacetamide. The subsequent electrospray ionization mass spectroscopy analysis indicated the presence of two reaction products with Mrs of 3,350.45 and 3,456.0. These are interpreted as the mutacin molecule with the addition of one and two molecules of reagent to the unsaturated amino acids, respectively. Sequencing of the peptide revealed an N-terminal amino acid sequence of Asn-Arg-Trp-Trp-Gln-Gly-Val-Val.

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“…Kelstrup and Gibbons [15] initially suggested that streptococcal bacteriocins could be differentiated on the basis of their inhibitory spectra, the morphology of their inhibition zones, and their sensitivity to chloroform and various enzymes. Subsequently, Kelstrup and Funder-Nielsen [16] divided the bacteriocins of S. mutans into two groups according to differences in their heat sensitivity and molecular masses.…”

Section: Introductionmentioning

confidence: 99%

Different bacteriocin activities of Streptococcus mutans reflect distinct phylogenetic lineages

Balakrishnan

Simmonds

Kilian

et al. 2002

Journal of Medical Microbiology

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Bacteriocins produced by mutans streptococci are known as mutacins. In this study 16 broadly active mutacin-producing Streptococcus mutans strains from New Zealand, North America and Europe were classified into four groups (A-D) on the basis of differences in their activity in deferred antagonism tests against either the homologous producer strain (to test for presence of self-immunity) or indicator strains Staphylococcus aureus 46 and Enterococcus faecium TE1. Two of the strains included in the study (UA140 and UA96) were representatives of the group I and II mutacin producer strains previously described by Caufield and co-workers. One of the New Zealand isolates of group A (S. mutans strain N) appeared to produce inhibitory activity similar to that of the group I prototype strain UA140. Four other New Zealand isolates of group B (S. mutans strains M19, M34, B34 and D14) had mutacin II-like activity. The group B mutacin producers differed from the group A mutacin producers in their additional activity against Staph. aureus 46. Seven S. mutans strains (M46, B46, B57, M12, M28, B28 and 13M) were distinguished from the group A and group B mutacin producers in that they inhibited E. faecium TE1. These were called group C mutacin producers. Strains H7 and H23 resembled the group C strains in their action on both indicator strains TE1 and 46. However, these two strains failed to exhibit immunity to their own inhibitory products in the deferred antagonism test and were separately classified as group D mutacin producers. Phylogenetic analysis of the strains by several genotypic and phenotypic characteristics revealed that the mutacin groups were associated with distinct evolutionary lineages of S. mutans.

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Bacteriocins from human and rodent streptococci

Cited by 93 publications

References 18 publications

"Fingerprinting" -haemolytic streptococci by their production of and sensitivity to bacteriocine-like inhibitors

"Fingerprinting" -haemolytic streptococci by their production of and sensitivity to bacteriocine-like inhibitors

Isolation and biochemical characterization of a novel lantibiotic mutacin from Streptococcus mutans

Different bacteriocin activities of Streptococcus mutans reflect distinct phylogenetic lineages

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