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PubMed1961

Staphylococcal penicillinase. I. Inhibition and stimulation of activity.

Saz, Arthur K. (National Institute of Allergy and Infectious Diseases, Bethesda, Md.), Dolores L. Lowery, and Leah J. Jackson. Staphylococcal penicillinase. I. Inhibition and stimulation of activity. J. Bacteriol. 82:298-304. 1961.-The penicillinase extracted from a penicillin-resistant strain of Staphylococcus aureus was shown to be inhibited up to 70% by various dipeptides and particularly by d-valyl-d-valine. It is of interest that the nucleus of penicillin contains d-valine. Various dipeptides formed by condensing amino acids and metal-binding compounds such as benzidine and biphenyl have been shown to inhibit penicillinase activity in considerably lower concentration than the dipeptides composed of amino acids alone. Contrariwise, it has been found that various alcohols, and particularly n-propanol, markedly stimulate the activity of the penicillinase both in whole cells and in cell-free extracts. The alcohols fall into a symmetrical series in respect to stimulatory activity with methyl < ethyl < n-propanol > n-butanol > amyl > isoamyl > octyl. Evidence is also presented showing that staphylococcal penicillinase is associated with the particulate fraction of the cell and it is postulated that the alcohols stimulate as a result of bringing insoluble enzyme and substrate into closer apposition. Bacillus subtilis strain 749 penicillinase, which is essentially soluble, is not stimulated by the alcohols. The possibility is presented based on fractionation of crude enzyme on a diethylamino-ethyl cellulose column that different species of penicillinase exist in S. aureus.

Penicillinase↗
PubMed1967

Relation between iron uptake, pH of growth medium, and penicillinase formation in Staphylococcus aureus.

The uptake of iron and the formation of penicillinase was examined in cultures of wild-type Staphylococcus aureus. Uptake of iron was about twice as great at pH 4.7 as at pH 7.4 At pH 4.7, increase in iron uptake in the range of 1.0 to 4.0 mug per mg of bacterial protein was associated with a progressive increase in the rate of penicillinase formation, but a direct correlation between cellular iron content and rate of enzyme formation was not demonstrated. Addition of iron to deferrated medium enhanced penicillinase formation at pH 6.5 to 7.4 two- to fourfold in cultures induced with benzylpenicillin and in uninduced cultures. To demonstrate an effect on the uninduced cells, it was necessary to increase iron uptake by preliminary incubation of cells with iron in buffer. Calcium and certain other ions depressed iron uptake at acidic and at neutral pH, and, presumably as a result of this action, depressed the formation of penicillinase. Iron did not enhance penicillinase formation at pH 4.7 by two penicillinase constitutive mutants nor by wild-type cells undergoing induction at pH 6.5 by cephalosporin C or methicillin. After removal of cephalosporin C or methicillin during an early phase of induction, residual synthesis of enzyme was increased by prior uptake of iron. The results are considered compatible with the concept that uptake of iron, especially at acidic pH, interferes with the formation or function of penicillinase repressor.

Bacterial Proteins↗
PubMed1963

INDUCTION OF STAPHYLOCOCCAL PENICILLINASE BY BENZYLPENICILLIN: EFFECT OF PH, CONCENTRATION OF FERROUS ION AND INDUCER, AND DURATION OF EXPOSURE OF CELLS TO INDUCER.

Leitner, Felix (Michael Reese Hospital and Medical Center, Chicago, Ill.), Helen M. Sweeney, T. F. Martin, and Sidney Cohen. Induction of staphylococcal penicillinase by benzylpenicillin: effect of pH, concentration of ferrous ion and inducer, and duration of exposure of cells to inducer. J. Bacteriol. 86:717-727. 1963.-The kinetics of induction of penicillinase by benzylpenicillin in exponentially multiplying Staphylococcus aureus strain 55-C-1 were shown to vary with the pH. At pH 7.3 in the absence of free inducer, the rate of increase of penicillinase activity rapidly declined and came to a halt. At pH 5.4 to 5.5 and in the presence of optimal concentrations of Fe(++), the penicillinase activity of the induced culture increased linearly with time for 2.5 or more generations, but the rate of increase usually declined eventually. Evidence was advanced to support the concept that the acidic pH and optimal Fe(++) concentration maintain the induced formation of enzyme. The induced increase in penicillinase activity appeared 3 to 4 min after the addition of benzylpenicillin. The degree of induction of penicillinase varied with the duration of exposure of the staphylococci to the inducer and with the concentration of inducer. Maximal induction under our conditions was attained by exposure for 15 min to benzyl-penicillin at an initial concentration between 0.6 and 2 units/ml.

Hydrogen-Ion Concentration↗
PubMed1979

Cefoxitin as a single-dose treatment for urethritis caused by penicillinase-producing Neisseria gonorrhoeae.

Gonococci that resist standard penicillin regimens by production of a penicillinase are now well established in certain areas of the world. Because cefoxitin, a semisynthetic cephamycin, resists gonococcal penicillinase in vitro, we compared procaine penicillin G and cefoxitin in treatment of gonorrhea in an area where 40 per cent of isolates produce penicillinase. One hundred and seven men with culture-proved gonococcal urethritis were given a single dose of either procaine penicillin G, 4.8 million U, or cefoxitin, 2 g, intramuscularly. Both groups took 1 g of probenecid orally; cefoxitin was given with lidocaine to reduce pain at the injection site. In men infected with penicillinase-negative gonococci, both cefoxitin and penicillin were highly effective. Penicillin failed in 77 per cent of men with penicillinase-positive strains, whereas cefoxitin was completely successful. Cefoxitin is an effective alternative to spectinomycin for single-session therapy of urethritis caused by penicillinase-producing Neisseria gonorrhoeae.

Cefoxitin↗
PubMed1978

A rapid slide test for penicillinase.

The authors developed a rapid slide test modification of the iodometric method for detection of penicillinase produced by organisms growing on routine plating media. A loopful of colonies is scraped from the agar surface and emulsified in one drop of an iodine-penicillin solution on a glass slide. Addition of a drop of 0.4% starch solution results in a purple color when penicillinase is not present; a colorless reaction denotes a positive test. The slide test yielded positive results identical to those of a starch agar-plate method with 26 Staphylococcus aureus isolates; a further seven showed comparable negative tests. Penicillinase production was associated with a S. aureus penicillin MIC of greater than or equal to 0.5 micron/ml. All 15 Staphylococcus epidermidis isolates gave negative test results, as did 22 Bacteroides fragilis (MIC greater than or equal to 3.1). Twenty ampicillin-susceptible Haemophilus influenzae were negative by both the slide test and a Levinthal broth method; an additional five resistant (MIC greater than or equal to 10) isolates were positive by both methods. Twenty-eight (penicillin MIC greater than or equal to 0.8) of 50 Bacteroides melaninogenicus were slide test-positive for penicillinase. Two penicillinase-producing strains of Neisseria gonorrhoeae gave positive slide tests, while eight other non-penicillinase-producers were negative.

Bacteria↗
PubMed1985

Effect of in vitro DNA rearrangement in the NH2-terminal region of the penicillinase gene from Bacillus licheniformis on the mode of expression in Bacillus subtilis.

We have constructed secretion vector plasmids that have unique BglII sites within or near the signal sequence of Bacillus licheniformis penicillinase, and have also constructed penicillinase cartridges that lack either one, two or three of the processing sites for the membrane-bound, exo-large and exo-small enzymes. Each of these penicillinase cartridges was cloned on secretion vectors in Bacillus subtilis, and enzyme production was examined. The presence of both the signal sequence and the three host-specific processing sites on the secretion vector was required for an effective expression of the enzyme in B. subtilis. The presence of any of the processing sites on the cartridge reduced the accumulation of penicillinase in the culture medium. When a vector plasmid lacking part of the hydrophobic region of the signal sequence and lacking the three processing sites was used, total penicillinase production decreased and enzyme accumulation in the medium was extremely low, despite the complete or incomplete presence of the processing sites on the cartridge. Molecular mass determination of these extracellular penicillinases suggested the existence of a new cleavage site for the enzyme.

Amino Acid Sequence↗
PubMed1983

Effects of penicillinase on bactericidal and complement activities in normal human serum.

During routine addition of penicillinase (beta-lactamase) to patients sera, we found that the capacity of some of these sera to kill serum-sensitive gram-negative organisms was significantly decreased. Further controlled studies showed that penicillinase decreased both the bactericidal activity of normal human sera and the total hemolytic activity (CH50) of complement in these sera. The decreased bactericidal activity correlated significantly (r = 0.57, P less than 0.05) with the reduction of CH50 in eight normal sera. These effects of penicillinase were time and temperature dependent. Measurement of individual complement component activities showed that penicillinase decreased the activity of C2, C4, and C3-C9, suggesting that the penicillinase preparation activated the classical pathway. These results cast doubts on the validity of bactericidal determinations when sera are pretreated with penicillinase.

Bacteria↗
PubMed1984

Influence of inoculum size on comparative susceptibilities of penicillinase-positive and -negative Neisseria gonorrhoeae to 31 antimicrobial agents.

The effects of two inoculum sizes (10(4) and 10(6) CFU) on the MICs of 20 beta-lactam antibiotics, 4 aminoglycosides, and 7 other antimicrobial agents were compared for 102 unselected strains of Neisseria gonorrhoeae (26 penicillinase positive and 76 penicillinase negative), with three replicates for each test. The method was agar plate dilution on Mueller-Hinton agar supplemented with 1% hemoglobin and 1% IsoVitaleX. For penicillinase-positive strains, a large inoculum (10(6) CFU) increased the MIC greater than or equal to 16-fold for benzylpenicillin, piperacillin, azlocillin, and mezlocillin and increased the MIC greater than or equal to 8-fold for ampicillin, cefoperazone, ceftazidime, cefonicid, and cefamandole. The inoculum size had little or no influence on MICs of any antimicrobial agent for penicillinase-negative strains. For penicillinase-positive strains, the most active antibiotics (MIC, less than or equal to 0.001 microgram/ml) were the new cephalosporins: cefotaxime, ceftazidime, ceftizoxime, ceftriaxone, and cefmenoxime. For penicillinase-negative strains, the most active antibiotics were piperacillin, ceftriaxone, ceftizoxime, and cefmenoxime (MIC, less than or equal to 0.001 microgram/ml), closely followed by ceftazidime, moxalactam, azlocillin, mezlocillin, and cefuroxime.

Anti-Bacterial Agents↗
PubMed1973

Formation and secretion of induced penicillinase in protoplasts of Staphylococcus aureus.

Conditions suitable for induced formation and secretion of penicillinase (EC 3.5.2.6) in protoplasts of Staphylococcus aureus were determined. No requirement was found for cells to be exposed to inducer prior to formation of protoplasts. Neither cell wall components nor mesosomes appeared to be necessary for induction or secretion. In medium containing 1.1 M sucrose about half of the formed enzyme was soluble, whereas in medium containing 0.37 M sodium succinate only about 10% of the penicillinase remained protoplast-bound. Low concentrations of polyanions (dextran sulfate and potassium polyvinyl-sulfonate) inhibited the formation of induced penicillinase, as did 4-acetamido-4'-isothiocyano-stilbene 2,2'-disulfonic acid. None of these compounds inhibited the activity of native penicillinase, and none would be expected to pass through the protoplast membrane. Penicillinase, denatured in 4 M urea, could be renatured by dilution in the presence of benzylpenicillin, and the above three inhibitors interfered strongly with this process. The results are taken as evidence that penicillinase may be secreted through the protoplast membrane in an incompletely folded form.

Enzyme Induction↗
PubMed1967

Microbial penicillinase in soft types of cheese.

Penicillinase activity was found in commercial samples of Limburger, Liederkranz, and Brick, as well as in Roquefort and Danish Blue cheeses. The numbers of penicillinase-producing bacteria in the cheese flora were estimated by use of the most probable numbers technique coupled with penicillinase determinations on the individual cultures. Although streptococci constituted the predominant flora in most of the samples, significant numbers of penicillinase-producing bacteria were also observed. Six of seven penicillinase-producing isolates that were studied in detail were micrococci; the other was an unidentified gram-positive, catalase-positive rod. The results suggest the widespread occurrence of penicillinase-forming micrococci on the surfaces of soft types of cheese.

Bacteria↗
PubMed1970

Investigation of the penicillinase activity in L colonies of Staphylococcus aureus.

Penicillinase-producing strains of Staphylococcus aureus are transformed into stable L colonies by 70 to 100 subcultures on methicillin-containing medium with a suitable high osmolarity. During transformation, the penicillinase activity is lost. This loss in activity is not the result of only the penicillinase-negative mutants transforming to L colonies. If unstable L colonies are filtered through 0.45-mum membrane filters immediately after transformation, still no penicillinase activity is seen; this is also the case if the filtrated L colonies are reverted into coccal forms. The mechanism responsible for the loss of penicillinase activity is discussed. A loss of the penicillinase plasmid is proposed as the most reasonable explanation.

Bacillus subtilis↗
PubMed1971

Effects of ethidium bromide on growth and on loss of the penicillinase plasmid of Staphylococcus aureus.

Ethidium bromide (EB) was more efficient than ethyl violet or rifampin as a curing agent for the penicillinase plasmids of Staphylococcus aureus strains. The effects of EB on growth and on the loss of the penicillinase plasmid of PS 81 were studied in detail. The growth rates of PS 81 and an EB-cured derivative were identical in broth, but the cured derivative had a shorter lag in the presence of added 6 x 10(-6)m EB. The shortened lag was due to prior exposure to EB as the cured derivative and an EB-treated but uncured strain of PS 81 gave identical growth lag and growth rates in the presence of EB. The curing of PS 81 by EB occurs in three phases. After a 4 to 5 hr lag, there is a 100-fold increase in the number of penicillinase-negative cells, and the proportion of cured cells continues to rise until 10 to 12 hr. Thereafter, the population becomes refractory to further curing, and the proportion of penicillinase-negative cells remains constant at about 20% of the total. Penicillinase-positive survivors of EB treatment showed increased EB resistance and were cured at lower rates upon subsequent EB treatment. Isolated colonies of the parental strain PS 81 were heterogeneous in their EB sensitivity. Thus, EB does not competitively favor spontaneously cured penicillinase-negative cells but appears to act in a manner analogous to acridine orange on the plasmids of enteric bacteria.

Coloring Agents↗
PubMed1972

Polyfunctional penicillinase plasmid in Staphylococcus epidermidis: bacteriophage restriction and modification mutants.

Growth of multiply resistant Staphylococcus epidermidis BV strains at 45 C resulted in the independent elimination of tetracycline resistance, of kanamycin resistance coupled with oxacillin resistance, or of penicillinase activity. The pH optimum for the elimination of kanamycin and oxacillin resistance was 5.6, whereas that for elimination of penicillinase activity was 8.0. The genetic determinant for penicillinase activity was linked with the genetic determinants for the active uptake of mannitol and beta-glucosides, ribose fermentation, and phospho beta-glucosidase activity. The penicillinase linkage group also contained determinants for phage adsorption, restriction, and modification, and for growth factor requirements of still unknown nature. The same linkage group, which is apparently of extrachromosomal nature, was eliminated from several S. epidermidis BV strains. By selection for novobiocin resistance, deletion mutants affecting several loci of the penicillinase plasmid were isolated. The isolation of restriction-negative and modification-negative mutants which retained phage susceptibility allowed the investigation of restriction and modification phenomena. A preliminary deletion map of the polyfunctional penicillinase plasmid is proposed.

Carbon Isotopes↗
PubMed1977

Penicillinase-releasing protease of Bacillus licheniformis: purification and general properties.

The membrane penicillinase of Bacillus licheniformis 749/C is a phospholipoprotein which differs from the exoenzyme in that it has an additional sequence of 24 amino acid residues and a phosphatidylserine at the NH2 terminus. In exponential-phase cultures, the conversion of membrane penicillinase to exoenzyme occurs at neutral and alkaline pH. An enzyme that will cleave the membrane penicillinase to yield the exoenzyme is present (in small amounts) in exponential-phase cells and is released during their conversion to protoplasts. The enzyme is found in the filtrate of a stationary-phase culture of the uninduced penicillinase-inducible strain 749 and has been purified to apparent homogeneity from this source. The protease has an approximate molecular weight of 21,500 and requires Ca2+ ions for stabilization. It has a pH optimum of 7.0 to 9.5 for hydrolysis of casein and for the cleavage of membrane penicillinase. Both activities are inhibited by diisopropylfluorophosphate; hence, the enzyme is a serine protease. This enzyme may be entirely responsible for the formation of exopenicillinase by this organism, since the other neutral and alkaline proteases of strain 749 have little, if any, activity in releasing exopenicillinase. The enzyme has been termed penicillinase-releasing protease.

Bacillus↗
PubMed1968

Wild-type strain of Staphylococcus aureus containing two genetic linkage groups for penicillinase production.

Staphylococcus aureus strain 55C1, isolated from a patient in 1955, contained two genetic linkage groups for penicillinase formation. One was linked to genes that control resistance to cadmium and mercuric ions; it had properties of a plasmidborne gene. The other was not linked to resistance to these metal ions; it had properties of a chromosomal gene. Penicillinase formation by cells that contained either linkage group was inducible by penicillins. Induced penicillinase in cells that contained both linkage groups equalled the sum of that produced in cells containing each group singly. Exopenicillinase produced by cells containing either gene was serological type A. Constitutive penicillinase formation resulting from regulator gene mutations in either linkage group was repressed to differing extents by a wild-type determinant in the trans position. The genetic structure and the regulation of penicillinase formation in strain 55C1 resembled in general those for penicillinase linkage groups which Asheshov and Dyke described for diploid mutant strains of S. aureus PS 80. There were differences in detail, however.

Cadmium↗
PubMed1969

Naturally occurring penicillinase plasmids in Staphylococcus aureus.

A series of plasmids harbored by naturally occurring penicillin-resistant strains of Staphylococcus aureus were surveyed with a view toward exploring the variability in plasmid-linked marker patterns. Plasmids were transduced from their natural hosts to either of two plasmid-negative laboratory strains by selection for cadmium resistance, and the transductants were tested for all other markers previously found to be plasmid-linked. All of the strains that were able to serve as genetic donors to one of the two stock strains could donate cadmium and lead resistance as linked, plasmid-borne markers. Among the other plasmid markers, a wide variety of patterns was found, including four plasmids that did not carry the penicillinase determinant. Each of the 26 plasmids studied, including the latter 4, was found to belong to one of the two incompatibility sets of penicillinase plasmids previously identified. With the exception of the penicillinase-negative plasmids, which were found in both sets, all the plasmids of incompatibility set I directed the production of penicillinase type A; those belonging to set II directed either type A or type C. Those of set II without exception increased the sensitivity of their host strains to bismuth ion; those of set I carried determinants of bismuth resistance or did not affect the sensitivity of their host to this ion. No other perfect correlations between markers were encountered; in particular, there was no correlation between penicillinase serotype and the excretion of the enzyme. This finding allows the prediction that there is, in addition to all of the markers thus far identified, a plasmid-linked determinant of penicillinase excretion.

Cadmium↗
PubMed1977

Penicillinase production in community strains of staphylococcus aureus.

A survey of penicillinase production in 406 strains of Staphylococcus aureus isolated from wounds in the County of Uppsala in 1975 showed that 76% of strains from inpatients produced penicillinase compared to 69% of the outpatient strains. The frequency of penicillinase production in Staph. aureus strains from surgical staff was 59%. 51% of strains from school children and 38% of strains from healthy adults produced penicillinase. The conclusions are that ordinary penicillinase-sensitive penicillin should not be used for treating infections in outpatients unless the isolated aureus strain has been shown to be penicillinase-negative.

Adult↗
PubMed1999

[Characteristics of penicillinase plasmids from Staphylococcus aureus strains].

Penicillinase plasmids are present in most MRSA strains. They are very varying in their genotype and phenotype they confer. Penicillinase plasmids were transduced from 80 hospital MRSA strains to NCTC 8325 and the phenotype as well as the incompatibility group of plasmid were determined. Resistance to cadmium (high and low level), resistance to organic and nonorganic mercury compounds, arsenate/arsenite/antimonium resistance, resistance to bismuth and hypersensitivity to bismuth, resistance to macrolides as well as beta-lactamase production and its inductibility were checked. Among the examined strains 20 different phenotypes of penicillinase plasmids were found. Patterns of penicillinase plasmids were compared to DNA patterns of the investigated strains after digestion with SmaI and separation in pulsed field electrophoresis (PFGE). It was shown that strains with the same PFGE pattern often differ in the type of their penicillinase plasmid. Determining of penicillinase plasmid phenotype could be useful in differentiating S. aureus strains sharing the same pattern of PFGE.

Drug Resistance, Microbial↗