Influences of cationic bactericidal agents on membrane ATPase of bacillus subtilis

Rosenthal, S; Buchanan, Audria M.

doi:10.1016/0005-2736(74)90054-6

Cited by 16 publications

(6 citation statements)

References 28 publications

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“…In addition to its interaction with SDS, AS-48 also bond strongly to cardiolipin. Interaction with anionic phospholipids may be an essential step in the biological activity of cationic peptides with an amphiphilic structure (20).…”

Section: Methodsmentioning

confidence: 99%

Purification and amino acid composition of peptide antibiotic AS-48 produced by Streptococcus (Enterococcus) faecalis subsp. liquefaciens S-48

Gálvez

Giménez‐Gallego

Maqueda

et al. 1989

Antimicrob Agents Chemother

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Peptide antibiotic AS-48 was purified to homogeneity by ion-exchange chromatography, gel filtration chromatography, and reversed-phase liquid chromatography. The purified fraction was active against gram-positive and gram-negative bacteria. AS-48 is a basic protein with an isoelectric point of ca. 10.5 and a molecular mass of 7.4 kilodaltons. Its inhibitory activity was markedly affected by sodium dodecyl sulfate and cardiolipin but not by neuraminidase, pectinase, I8-glucosidase, or 0-glucuronidase. Differential scanning calorimetry data suggested that AS-48 molecules lack a compact structure.Since bacteriocin production by group D streptococci was first reported (11), extensive studies have been performed on this subject, many of them describing the production and characterization of different types of classic bacteriocins (2,6,12,16).However, production of peptide antibiotics by members of this group is very unusual, with the exception of nisin (8). This substance and the small bacteriocin C3603 (9) deserve further attention, since they both could be included in a group of strongly basic peptides that display marked antimicrobial activity. It has been suggested that the large number of similar substances from different origins described so far (3,24,27), most of them showing structural and functional similarities, reflects the conservation in the course of evolution of a general mechanism of antibiosis by basic peptides (22).In a previous paper (5), we described the partial purification and characterization of a new antibiotic peptide (AS-48) produced by Streptococcus (Enterococcus) faecalis subsp.liquefaciens S-48. This substance showed potential for inhibition of gram-positive unrelated bacteria and also gramnegative bacteria. In this paper, new data are presented concerning the complete purification and amino acid composition of this substance. Similarities to other basic peptides are also discussed. MATERIALS AND METHODSMicroorganisms. S. faecalis subsp. liquefaciens S-48 (isolated from a human wound exudate) was used as the producer strain. S. faecalis subsp. liquefaciens S-47 and Escherichia coli U-9, both from our laboratory collection, were used as susceptible strains.Growth media, antibiotic production, and assay of activity. Brain heart infusion (BHI broth; BBL Microbiology Systems, Cockeysville, Md.) was used as the growth medium. Buffered CM-G (5) was used for antibiotic production.The procedures for antibiotic assay and determination of arbitrary units were as previously described (5). The plating medium for the antibiotic assay consisted of Mueller-Hinton agar (BBL). Soft-agar overlay tubes consisted of 0.75% agar * Corresponding author.(Difco Laboratories, Detroit, Mich.). All media were buffered with 0.15 M sodium phosphate, pH 7.2.For antibiotic production, batches of buffered CM-G were inoculated with overnight growth of the producer strain (4% [vol/vol]) and incubated at 37°C for 8 h. The cells were then removed by centrifugation, and the supernatants were purified.Purification of AS-48. Th...

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Section: Methodsmentioning

confidence: 99%

Purification and amino acid composition of peptide antibiotic AS-48 produced by Streptococcus (Enterococcus) faecalis subsp. liquefaciens S-48

Gálvez

Giménez‐Gallego

Maqueda

et al. 1989

Antimicrob Agents Chemother

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“…The mode of action of the damaging component(s) on spermatozoa is not sufficiently clear. Cationic proteins bind to sperm membranes (Shannon and Curson, 1983) and may exert their damaging activity in a manner similar to that described for bacterial membranes (Farley et al, 1989;Rosenthal and Buchanan, 1974). Reduced activity in some cationic fractions is probably due to not meeting the ultimate criteria as described by Farley et al (1989): saturation binding to negatively charged surface sites followed by hydrophobic interaction with the outer membrane, which may serve to stabilise the binding.…”

Section: "Tmentioning

confidence: 97%

Anionic and cationic components from protein aggregates in bovine seminal plasma and their effects of sperm motility

al-Somai

Vishwanath

Molan

et al. 1994

Molecular Reproduction Devel

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Bovine seminal plasma proteins are in an aggregated form of high molecular weight in their native state. By immobilisation on a cation exchanger with exposure to disaggregating conditions (i.e., acetonitrile and low pH), the high-molecular-weight aggregates could be dissociated to slowly release the low-molecular-weight components. The anionic component released from the cation exchanger during disaggregation was collected by adsorption on a hydrophobic interaction column. The cationic component remaining on the cation exchanger was eluted with NaOH. Both components were found on gel permeation chromatography to be < 5 kDa. SDS-PAGE of the various fractions showed that components of low molecular weight were still in an aggregated form. These components resulting from the disaggregation process have detrimental effects on sperm motility and the effects were more substantial compared with that of whole seminal plasma. All the cationic components were significantly detrimental to sperm motility, especially the fractions of low molecular weight. The anionic fractions reduced sperm motility when in an aggregated state. The isolated anionic peptide was not detrimental in its free form. In all fractions the peptides tended to re-aggregate to a higher molecular weight under neutral conditions, however, the isolated anionic peptide (molecular weight < 1,500) failed to do so.

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“…However, changes in PL composition may have other more subtle effects. CTAB stimulates the membrane-bound ATPase activity of Bacillus subtilis, the stimulation being reversed by PE or phosphatidylserine (Rosenthal & Buchanan 1974). It is noteworthy that one of the PL reduced to very low concentrations by P-depletion in Esch.…”

Section: Discussionmentioning

confidence: 97%

Effect of R‐plasmid RP1 and Nutrient Depletion on the Resistance of Escherichia coli to Cetrimide, Chlorhexidine and Phenol

Klemperer

Ismail

Brown

1980

Journal of Applied Bacteriology

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The minimum inhibitory concentation of cetrimide and chlorhexidine for Escherichia coli is altered when R-plasmid RPI is inserted into it. Using disinfectant-agar plates as a test system, the sensitivity of Esch. coli to these disinfectants and to phenol was found to vary, not only with the presence of RPI, but also with the nutritional status of the inoculum. The different inocula also varied in their ability to bind H i and there was some correlation between this property and chlorhexidine sensitivity.

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Influences of cationic bactericidal agents on membrane ATPase of bacillus subtilis

Cited by 16 publications

References 28 publications

Purification and amino acid composition of peptide antibiotic AS-48 produced by Streptococcus (Enterococcus) faecalis subsp. liquefaciens S-48

Purification and amino acid composition of peptide antibiotic AS-48 produced by Streptococcus (Enterococcus) faecalis subsp. liquefaciens S-48

Anionic and cationic components from protein aggregates in bovine seminal plasma and their effects of sperm motility

Effect of R‐plasmid RP1 and Nutrient Depletion on the Resistance of Escherichia coli to Cetrimide, Chlorhexidine and Phenol

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