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

Simmonds, Robin S.; Pearson, Leonard; Kennedy, Richard; Tagg, John

doi:10.1128/aem.62.12.4536-4541.1996

Cited by 70 publications

(45 citation statements)

References 31 publications

(29 reference statements)

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“…zooepidemicus 4881 [1], S. equi subsp. zooepidemicus 8b [8] and S. gordonii DL1 at 37³C in 5% CO P in air. E. coli DH5KFP was routinely cultured in 2UYT medium, Luria-Bertani (LB) medium or on LB agar (LBA) plates [9].…”

Section: Bacterial Strains and Plasmidsmentioning

confidence: 97%

Zoocin A immunity factor: a femA-like gene found in a group C streptococcus

Beatson

1998

FEMS Microbiology Letters

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A 6.8-kb fragment of Streptococcus equi subsp. zooepidemicus 4881 DNA containing the zoocin A gene (zooA) was cloned in Escherichia coli and sequenced. We have identified a gene we call zoocin A immunity factor (zif), which protects the producer cell from the otherwise lethal action of its own product. Transformation of Streptococcus gordonii DL1 with zooA and zif changed its phenotypic character from a non-zoocin A producing-zoocin A sensitive cell to a zoocin A producing-zoocin A resistant cell. zif has sequence homology to femA (factor essential for methicillin resistance) and lif (lysostaphin immunity factor). No differences were observed in amino acid or amino sugar compositions of peptidoglycan purified from zoocin A sensitive vs. zoocin A immune cells. z

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Section: Bacterial Strains and Plasmidsmentioning

confidence: 97%

Zoocin A immunity factor: a femA-like gene found in a group C streptococcus

Beatson

1998

FEMS Microbiology Letters

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“…A 6.8 kb EcoRI fragment containing the gene encoding zoocin A (zooA) was cloned into Escherichia coli and the sequence of zooA determined [2]. The N-terminal region of zoocin A had a high degree of homology to the N-terminal region of lysostaphin, an endopeptidase produced by Staphylococcus simulans biovar staphylolyticus that speci¢cally targets the cell walls of some staphylococcal species, and to a number of other enzymes with pepti-dase activity [3]. Thus, the N-terminal region of zoocin A was predicted to contain the catalytic domain (CAT).…”

Section: Introductionmentioning

confidence: 99%

Functional characterization of domains found within a lytic enzyme produced by Streptococcus equi subsp. zooepidemicus

Lai¹

2002

FEMS Microbiology Letters

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Zoocin A is a lysostaphin-like streptococcolytic enzyme produced by Streptococcus equi subsp. zooepidemicus 4881 that specifically targets the cell walls of some closely related species. On the basis of sequence homology it was suggested that zoocin A was a domainstructured enzyme with the N-terminal domain responsible for catalysis (CAT) and the C-terminal domain for target recognition (SBD). Polypeptides corresponding to zoocin A (rZooA) and each of the putative domains (rCAT and rSBD) were prepared by use of recombinant technology. The biological activities of each was compared by use of a dye-release assay and a cell-binding assay. Cell wall hydrolysis was shown to be a function of CAT and target recognition a function of the SBD. Expression of the zoocin A immunity factor gene produced cell walls resistant to hydrolysis by either rZooA or its component domains, and with reduced capacity to bind rZooA and rSBD.

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“…Of the remaining three classes, only class III gathers large-size molecules such as zoocin A from Streptococcus equi ssp. zooepidemicus, millericin B from Streptococcus milleri, streptococcin A-M57 from Streptococcus pyogenes and dysgalacticin from Streptococcus dysgalactiae (Simmonds et al 1996;Beukes et al 2000;Heng et al 2004Heng et al , 2006. However, these bacteriocins are heat-labile substances from various species of Streptococcus whereas lactosporin is produced by the Bacillus spp.…”

Section: Discussionmentioning

confidence: 99%

Characterization of lactosporin, a novel antimicrobial protein produced byBacillus coagulansATCC 7050

Riazi

Wirawan

Badmaev

et al. 2009

Journal of Applied Microbiology

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Aims: To characterize the antimicrobial protein produced by Bacillus coagulans used in the probiotic dietary supplement (Lactospore® Probiotic, Sabinsa Corp., Piscataway, NJ, USA). Methods and Results: Bacillus coagulans ATCC 7050 was grown at 37°C for 18 h. The cell free supernatant was concentrated 10‐fold (lactosporin preparation, LP). The antimicrobial activity of LP was confirmed against Micrococcus luteus ATCC 10420 in a well diffusion assay. The proteinaceous nature of LP was determined following exposure to different enzymes. The activity of LP was pH‐dependent but stable to heat. The isoelectric point of LP was determined to be 3·5–4·0. PCR analyses showed no similarity between lactosporin and known antimicrobial proteins produced by the Bacillus spp. Conclusions: Lactosporin is a novel antimicrobial protein. Initial characterization indicates that it may fall outside of the conventional classification of class I and II bacteriocins. Loss of activity after exposure to a number of proteolytic enzymes and lipase suggest that lactosporin may posses a lipid moiety which contributes to its inhibitory activity. Significance and Impact of the Study: The unique characteristics of lactosporin, including its antimicrobial activity against pathogenic micro‐organisms, indicate that it may have potential for application in foods and personal care products.

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

Cited by 70 publications

References 31 publications

Zoocin A immunity factor: a femA-like gene found in a group C streptococcus

Zoocin A immunity factor: a femA-like gene found in a group C streptococcus

Functional characterization of domains found within a lytic enzyme produced by Streptococcus equi subsp. zooepidemicus

Characterization of lactosporin, a novel antimicrobial protein produced byBacillus coagulansATCC 7050

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