The differentiation of Aerobacter aerogenes and Aerobacter cloacae.
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Enterobacter↗
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The distribution of polysaccharide production in Aerobacter and Escherichia strains and its relation to antigenic character; with a note on the influence of potassium deficiency upon production of polysaccharide by Aerobacter aerogenes.
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Carbohydrate Metabolism↗
Frequency of R factor-mediated multiple drug resistance in Klebsiella and Aerobacter.
A comparative study was done on the transfer frequency of R factors from 90 strains of multiple drug-resistant Aerobacter and 81 strains of Klebsiella to Escherichia coli CSH-2 (F(-), met(-), pro(-), Nal-r). The most common resistance patterns for the Aerobacter isolants were ampicillin streptomycin chloramphenicol tetracycline and ampicillin streptomycin chloramphenicol tetracycline kanamycin neomycin; for the Klebsiella isolants, the most common resistance pattern was ampicillin kanamycin streptomycin tetracycline chloramphenicol neomycin. R factors were isolated from 14.1% of the Aerobacter strains; 61.5% of these R factors harbored R determinants for ampicillin streptomycin tetracycline. R factors were isolated from 79.1% of the Klebsiella strains; four R factors were isolated with significant frequency; streptomycin chloramphenicol kanamycin neomycin, 37.5%; ampicillin streptomycin tetracycline kanamycin neomycin, 14.1%; ampicillin streptomycin tetracycline, 12.5%; and streptomycin chloramphenicol tetracycline, 12.5%.Chloramphenicol, kanamycin, and neomycin resistance was rarely transferred from the Aerobacter strains, although over 50% of the clinical isolants possessed resistance to these antibiotics. In contrast, over 75% of the Klebsiella strains transferred resistance to chloramphenicol, kanamycin, neomycin. Highest frequency of transferred resistance to individual drugs in the Aerobacter strains was to streptomycin (14.8%), whereas in the Klebsiella group resistance to four drugs was transferred at a very high frequency: streptomycin (80.8%), chloramphenicol (78.5%), kanamycin (76.4%), and neomycin (75.9%).
Ampicillin↗
The aerogenic response of Escherichia coli and strains of Aerobacter in EC broth and selected sugar broths at elevated temperatures.
Gas formation by 116 strains of Escherichia coli and 104 strains of Aerobacter was determined in a specially constructed and accurately controlled water bath employing EC, lactose, maltose, sucrose, glucose, levulose, and galactose broths at temperatures ranging from 44.5 to 46.5 C. Greatest gas activity occurred in EC broth. In the range 44.9 to 45.5 C over 92% of the E. coli cultures formed gas, but the Aerobacter strains dropped from 68 to 2%. A natural point of separation of the two groups occurred at 45.5 C. Inhibition of the gas-forming mechanism rather than death is the universal response of the Escherichia organisms to these temperatures. The inhibition increases with rising temperatures and is readily reversible. At 46.5 C, 64.5% of all the Escherichia cultures were inhibited and 69.1% of all the cultures were actually viable. In EC broth it was found that as a group atypical E. coli (-+--) were the most resistant gas-positive types. Least resistant in EC broth was a group of known typical fecal isolates of E. coli (++--). Of intermediate resistance between the two groups was the large body of typical E. coli (++--) organisms. Certain individual strains of E. coli excelled in the production of gas in the variety of sugar broths tested at elevated temperatures. The Aerobacter strains did not exhibit this property. Finally it is suggested that elevated temperature incubation studies of this type be conducted in critically controlled water baths with an ascertained accuracy in the vicinity of 45.5 +/- 0.1 C under full load.
Culture Media↗
Effect of L-cystine on initiation of anaerobic growth of Escherichia coli and Aerobacter aerogenes.
Gorini, Luigi (Harvard Medical School, Boston, Mass.). Effect of l-cystine on initiation of anaerobic growth of Escherichia coli and Aerobacter aerogenes. J. Bacteriol. 82:305-312. 1961.-Under anaerobic conditions Escherichia coli and Aerobacter aerogenes, inoculated in a mineral-citrate-glucose medium at densities up to 10(6) bacteria per ml, exhibit a long lag, or fail to initiate growth at all. Growth is initiated rapidly if the medium is supplemented with various SH or SS compounds. Of these the most active is l-cystine, which is fully effective at 1 to 2 mum. In a heavily seeded semisolid medium without cystine, turbidity rapidly appears at the aerobic surface and then slowly extends throughout the anaerobic region of the culture. This finding implies that a sufficiently dense anaerobically growing culture creates conditions in the medium which eliminate the requirement for cystine. The nature of this effect on the medium has not been determined, but certain possibilities (pH, pCO(2)) have been eliminated. The anaerobic cystine requirement becomes more pronounced in the presence of Cu(++), at concentrations far lower than those required for inhibition under aerobic conditions. While it is possible that cystine is acting by complexing the toxic metal ion, it seems more likely that l-cystine is an essential metabolite, poorly produced under anaerobic conditions, and that the marked toxicity of Cu(++) under anaerobic conditions depends on its complexing of cystine.
Citrates↗
Adsorption of influenza A virus by Aerobacter aerogenes spheroplasts.
Brown, Ronald J. (University of Kansas, Lawrence), Albert A. Benedict, and Nancy Armstrong. Adsorption of influenza A virus by Aerobacter aerogenes spheroplasts. J. Bacteriol. 83:1124-1130. 1962.-Aerobacter aerogenes spheroplasts adsorbed virus at a greater rate than whole A. aerogenes cells or cell-wall preparations. The largest fragments of sonic-disrupted spheroplasts were responsible for adsorption. Adsorption was characterized by rapid disappearance of viral hemagglutinin in about 8 min, elution of hemagglutinin, and followed again by complete adsorption of hemagglutinin. Viral activity was not recovered from spheroplasts after the final adsorption phase. Spheroplasts treated with heat, dilute periodate, or formaldehyde did not adsorb virus, and treatment of spheroplasts with receptor-destroying enzyme resulted in delayed adsorption.
Adsorption↗
PHENOTYPIC, GENOTYPIC, AND CHEMICAL CHANGES IN STARVING POPULATIONS OF AEROBACTER AEROGENES.
Harrison, Arthur P., Jr. (Vanderbilt University, Nashville, Tenn.) and Felix R. Lawrence. Phenotypic, genotypic, and chemical changes in starving populations of Aerobacter aerogenes. J. Bacteriol. 85:742-750. 1963.-Cells harvested from postlogarithmic (maximal stationary phase) Aerobacter aerogenes cultures and starved in dilute sodium phosphate at 40 C remained viable for many hours. On the other hand, most cells from logarithmic-phase cultures succumbed, although a relatively small number remained viable. This viable segment of the original population thus responded like cells from postlog-phase cultures and, in fact, had properties in common with them. The residual segment was comprised of cells of two kinds. The first were mutants; when cultivated, harvested during log-phase growth, and again starved, they were resistant. The second were wild-type; they responded exactly as before. During starvation, the mutant is at an advantage because it has the ability to convert from susceptible log-phase physiology to resistant postlog-phase physiology more rapidly than can wild-type. The mutant differs from wild-type in yet other ways. It is smaller in size, slower in growth rate, lower in ribonucleic acid (RNA)-deoxyribonucleic acid ratio, greater in light-scattering ability, and, during the first 4 hr of starvation, it loses a higher proportion of its RNA. Selection of mutants of low growth rate between periods of active clonal growth indicates that evolutionary advantage may not necessarily be with the fast-growing members of the clone.
Chemical Phenomena↗
ACTION OF FORMALDEHYDE ON MICROORGANISMS. II. FORMATION OF 1,3-THIAZANE-4-CARBOXYLIC ACID IN AEROBACTER AEROGENES TREATED WITH FORMALDEHYDE.
Neely, W. Brock (The Dow Chemical Co., Midland, Mich.). Action of formaldehyde on microorganisms. II. Formation of 1,3-thiazane-4-carboxylic acid in Aerobacter aerogenes treated with formaldehyde. J. Bacteriol. 85:1420-1422. 1963.-A culture of Aerobacter aerogenes was found to incorporate C(14)-labeled formaldehyde into 1,3-thiazane-4-carboxylic acid. The reaction was found to proceed nonenzymatically from homocysteine and formaldehyde. As a consequence of this reaction, the ability of homocysteine to counteract the effects of formaldehyde on A. aerogenes was investigated.
Carboxylic Acids↗
ACCUMULATION OF INORGANIC POLYPHOSPHATE IN AEROBACTER AEROGENES. I. RELATIONSHIP TO GROWTH AND NUCLEIC ACID SYNTHESIS.
Harold, F. M. (National Jewish Hospital, Denver, Colo.). Accumulation of inorganic polyphosphate in Aerobacter aerogenes. I. Relationship to growth and nucleic acid synthesis. J. Bacteriol. 86:216-221. 1963.-Growing cells of Aerobacter aerogenes contain traces of inorganic polyphosphate, but large amounts often accumulate when growth ceases as the result of a nutritional deficiency. The reciprocal relationship between growth and polyphosphate accumulation was traced to competition between nucleic acid synthesis and polyphosphate for intracellular phosphorus. Polyphosphate accumulated only after nucleic acid synthesis had ceased. Resumption of nucleic acid synthesis (with or without concurrent cell growth) induced rapid degradation of the polyphosphate with transfer of the phosphorus to ribonucleic acid (RNA). At the same time, incorporation of P(32) into polyphosphate was reduced, though not abolished. Competition for adenosine triphosphate may be part of the explanation. In addition, it appears that polyphosphate degradation is accelerated under conditions which permit rapid nucleic acid synthesis, the phosphorus released being trapped in RNA.
DNA↗
ACCUMULATION OF INORGANIC POLYPHOSPHATE IN AEROBACTER AEROGENES. II. ENVIRONMENTAL CONTROL AND THE ROLE OF SULFUR COMPOUNDS.
Harold, F. M. (National Jewish Hospital, Denver, Colo.) and Susan Sylvan. Accumulation of inorganic polyphosphate in Aerobacter aerogenes. II. Environmental control and the role of sulfur compounds. J. Bacteriol. 86:222-231. 1963.-The accumulation of inorganic polyphosphate in Aerobacter aerogenes was shown to be a function of the growth medium. In low-phosphate medium, polyphosphate accumulated whenever nucleic acid synthesis ceased due to a nutritional deficiency, regardless of its nature. In high-phosphate medium polyphosphate accumulation was induced only by sulfur starvation. Polyphosphate accumulation could thus be induced or suppressed at will by manipulation of the sulfur and phosphorus content of the medium. The specific requirement for sulfur starvation was traced to the presence of an intracellular inhibitor of polyphosphate accumulation. This was depleted during sulfur starvation and replenished when sulfate was restored. The inhibitor was identified as oxidized glutathione or a closely related compound. Suppression of polyphosphate accumulation required the simultaneous presence of a high exogenous phosphate concentration and a high intracellular glutathione level. Suppression of polyphosphate accumulation resulted in a constant polyphosphate level, due to a steady state of polyphosphate synthesis and degradation. The former continued at half the original rate while the latter was sharply accelerated. The synthetic and degradative phases of polyphosphate metabolism could be completely dissociated by inhibitors of energy generation. It is proposed that the primary effect of glutathione plus phosphate is the stimulation of polyphosphate degradation. Polyphosphate synthesis appears to be a general consequence of the inhibition of nucleic acid synthesis, but net accumulation may be obscured by concurrent degradation.
Culture Media↗
METABOLISM OF PENTOSES AND PENTITOLS BY AEROBACTER AEROGENES. I. DEMONSTRATION OF PENTOSE ISOMERASE, PENTULOKINASE, AND PENTITOL DEHYDROGENASE ENZYME FAMILIES.
Mortlock, R. P. (Michigan State University, East Lansing) and W. A. Wood. Metabolism of pentoses and pentitols by Aerobacter aerogenes. I. Demonstration of pentose isomerase, pentulokinase, and pentitol dehydrogenase enzyme families. J. Bacteriol. 88:838-844. 1964.-Aerobacter aerogenes PRL-R3 is capable of utilizing as sole substrates for energy and growth seven of the eight aldopentoses and all of the four pentitols. Growth upon media containing either d-xylose, l-arabinose, d-ribose, d-arabitol, or ribitol occurred within 24 hr at 26 C. When d-arabinose or l-arabitol were used as growth substrates, growth was complete within 2 days; 4 days were required for growth on d-lyxose or xylitol, and 3 to 4 weeks for growth upon l-xylose. The versatility of this strain of A. aerogenes is due to an ability to synthesize in the presence of appropriate carbohydrates (inducers) families of enzymes which catalyze the metabolism of the carbohydrates (i.e., families of pentitol dehydrogenases, aldopentose isomerases, and pentulokinases). The specificity of induction for members of the enzyme families was found to vary, and cross induction of enzyme activity was common, especially among the pentitol dehydrogenases. Ribitol dehydrogenase activity was detected in extracts of cells grown on all of the above carbohydrates with the exception of d-xylose, l-arabinose, and d-ribose. The ribitol dehydrogenase activity of xylitol-grown cell extracts was fivefold higher than the activity in extracts of ribitol-grown cells.
Alcohols↗
METABOLISM OF PENTOSES AND PENTITOLS BY AEROBACTER AEROGENES. II. MECHANISM OF ACQUISITION OF KINASE, ISOMERASE, AND DEHYDROGENASE ACTIVITY.
Mortlock, R. P. (Michigan State University, East Lansing), and W. A. Wood. Metabolism of pentoses by Aerobacter aerogenes. II. Mechanism of acquisition of kinase, isomerase, and dehydrogenase activity. J. Bacteriol. 88:845-849. 1964.-Aerobacter aerogenes PRL-R3 possesses the genetic information to synthesize, in the presence of the appropriate inducer, at least three members of the family of ketopentokinases, two members of the family of pentitol dehydrogenases, and two members of the family of aldopentose isomerases. That is, d-xylulokinase, d-ribulokinase, l-ribulokinase, ribitol dehydrogenase, d-arabitol dehydrogenase, d-xylose (--> d-xylulose) isomerase, and l-arabinose (--> l-ribulose) isomerase activities were detectable within 4 hr after addition of inducer. The possibility that mutation and selection are involved in the formation of l-xylulokinase, l-arabitol dehydrogenase, d-arabinose (--> d-ribulose) isomerase and d-lyxose (--> d-xylulose) isomerase could not be eliminated, because 11 hr or more of incubation after the addition of inducer were required before the appearance of these enzyme activities. d-Xylulokinase activity was induced in less than 2 hr when d-xylose or d-arabitol were inducers, but 45 hr were required for the appearance of activity when xylitol was the inducer, and 83 hr were required when d-lyxose was the inducer. Likewise, the time required for induction of ribitol dehydrogenase was 2 hr for ribitol, 12 hr for d-arabinose, and 45 hr for xylitol. The time required for the appearance of enzyme activity correlated with the time required for the beginning of cell growth and substrate utilization.
Alcohols↗
METABOLISM OF PENTOSES AND PENTITOLS BY AEROBACTER AEROGENES. 3. PHYSICAL AND IMMUNOLOGICAL PROPERTIES OF PENITOL DEHYDROGENASES AND PENTULOKINASES.
Mortlock, R. P. (Michigan State University, East Lansing), D. D. Fossitt, D. H. Petering, and W. A. Wood. Metabolism of pentoses and pentitols by Aerobacter aerogenes. III. Physical and immunological properties of pentitol dehydrogenases and pentulokinases. J. Bacteriol. 89:129-135. 1965.-Four pentulokinases and three pentitol dehydrogenases were purified from Aerobacter aerogenes PRL-R3, and the properties of the enzymes within each family were compared. d-Ribulokinase was purified from cells grown on ribitol, d-arabitol, and xylitol, and from a mutant constitutive for ribitol dehydrogenase; d-xylulokinase, from cells grown on d-xylose and xylitol; l-ribulokinase, from cells grown on l-arabinose; and l-xylulokinase, after growth on l-xylose. Similarly, ribitol dehydrogenase was purified after growth on ribitol, d-arabinose, and xylitol, and from the ribitol dehydrogenase-constitutive mutant. d-Arabitol dehydrogenase was obtained after growth on d-arabitol or d-xylose, and xylitol dehydrogenase was obtained after growth on xylitol. Except for l-xylulokinase, which also had a different S(20) value, the pentulokinases had identical pH optima, K(m) for the ketopentose, and sedimentation constants, and fractionated identically by a number of procedures. These kinases could be distinguished only by their substrate and immunological specificity. Ribitol dehydrogenase and d-arabitol dehydrogenase could be distinguished by several properties, but the properties of xylitol dehydrogenase were always similar to ribitol dehydrogenase. In all cases, individual kinases or dehydrogenases produced by different inducers had identical properties. These data constitute evidence against multiple forms of the same enzyme being produced by different inducers and against the dehydrogenase family containing essentially identical proteins differing only at the active site. For the kinases, three of the four appear to differ only at the active site.
Antibodies↗
DEGRADATION OF INORGANIC POLYPHOSPHATE IN MUTANTS OF AEROBACTER AEROGENES.
Harold, F. M. (National Jewish Hospital, Denver, Colo.), and Ruth L. Harold. Degradation of inorganic polyphosphate in mutants of Aerobacter aerogenes. J. Bacteriol. 89:1262-1270. 1965.-Extracts of Aerobacter aerogenes contained two enzymes capable of degrading polyphosphate, polyphosphatase and polyphosphate kinase. By use of a suicide technique, a mutant (Pn-4) blocked in polyphosphate degradation was isolated; this mutant was found to lack polyphosphatase. The results indicate that polyphosphatase mediates the main pathway of polyphosphate degradation, and, therefore, that polyphosphate does not serve as a microbial phosphagen. A second mutant (Pn-3) exhibited transient accumulation of polyphosphate when cells were transferred to fresh growth medium. This strain was constitutive for elevated levels of polyphosphate kinase, polyphosphatase, and alkaline phosphatase; the transient accumulation of polyphosphate may be due to the shifting ratios of the biosynthetic and degradative enzymes during growth. These mutants were employed in studies on the competitive relationship between polyphosphate and nucleic acids. It was concluded that nucleic acid synthesis inhibits polyphosphate synthesis and also stimulates polyphosphate degradation.
Acid Anhydride Hydrolases↗
Differentiation of Klebsiella-Enterobacter (Aerobacter)-Serratia by biochemical tests and antibiotic susceptibility.
Studies were undertaken for the differentiation of members of the Klebsiella-Enterobacter (Aerobacter)-Serratia division by biochemical tests and antibiotic susceptibility. A total of 67 cultures were tested. Strain identification was readily accomplished with the use of motility tests and arabinose fermentation. In addition, a practical schema, based on sensitivity pattern, proved valuable in the classification of the different strains. Most (if not all) Klebsiella strains were susceptible to cephalothin, and all were sensitive to colistin. Enterobacter strains were resistant to cephalothin but susceptible to colistin. In contrast to those other members of the group, all Serratia strains were resistant to both cephalothin and colistin. The combination of a limited number of biochemical reactions and single-disc sensitivity tests appears to be a logical approach for the tentative identification of Klebsiella-Enterobacter (Aerobacter)-Serratia strains.
Bacteriological Techniques↗
Citrate metabolism in Aerobacter cloacae.
Growth of Aerobacter cloacae on citrate either anaerobically or aerobically did not require and was not stimulated by the presence of Na(+) in the medium. Citrate was metabolized anaerobically via the fermentation pathway as evidenced by the (i) presence of oxalacetate decarboxylase, (ii) induction of citrate lyase, and (iii) repression of alpha-ketoglutarate dehydrogenase under anaerobic conditions. Thus, although all the other enzymes of the citric acid cycle were present in anaerobic cells, this pathway was not available for the metabolism of citrate. Citrate was metabolized aerobically via the citric acid cycle, since (i) citrate lyase but not oxalacetate decarboxylase was repressed and (ii) alpha-ketoglutarate dehydrogenase was induced under these conditions. The presence of Na(+) in the medium did not lead to a repression of alpha-ketoglutarate dehydrogenase as in the case of Aerobacter aerogenes. The oxalacetate decarboxylase was a soluble, constitutive enzyme, not activated by Na(+) nor inhibited by avidin. It was slightly inhibited by ethylenediaminetetraacetate but was not stimulated by Mg(2+) or Mn(2+). Thus, this enzyme differed markedly in its properties from the same enzyme found in citrate-grown A. aerogenes.
Aconitate Hydratase↗
Divergence of the aerobactin iron uptake systems encoded by plasmids pColV-K30 in Escherichia coli K-12 and pSMN1 in Aerobacter aerogenes 62-1.
Although the aerobactin-mediated iron uptake system has been characterized genetically in Escherichia coli, the siderophore aerobactin was chemically characterized after purification from culture supernatants of Aerobacter aerogenes 62-1, a member of the Klebsielleae. We have cloned and mapped the genes encoding the aerobactin system genes of A. aerogenes 62-1 and begun characterization of the relevant proteins and enzymatic activities of this plasmid-mediated aerobactin system. Published chemical data indicate that the siderophore aerobactin of E. coli is the same molecule as the aerobactin of Aerobacter aerogenes 62-1, but we have found that both the genes and the complement of proteins making up the biosynthetic enzymes in the two systems have diverged. In contrast, the outer membrane receptors for ferric aerobactin of the two systems showed immunologic cross-reactivity, were of the same molecular size (74 kilodaltons), and were encoded by homologous DNA sequences.
Cloning, Molecular↗
Action of penicillin on Aerobacter cloacae.
Hugo, W. B. (University of Nottingham, Nottingham, England), and A. D. Russell. Action of penicillin on Aerobacter cloacae. J. Bacteriol. 82:411-417. 1961.-A study has been made of the action of penicillin on a penicillinase-producing strain of Aerobacter cloacae. It has been found that in culture media rendered hypertonic by the addition of sucrose (0.33 to 0.66 m), provided a source of magnesium ions is present, cell wall lesions occur, giving rise to osmotically fragile spheroplasts. Evidence is also presented of a lethal effect not associated with cell wall damage. Penicillinase production is not a complete challenge to the action of penicillin and in certain experimental situations renders the cells more susceptible to penicillin action.
Enterobacter↗