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Of 15 Peptostreptococcus sp. strains isolated between 1975 and 1984, 13 hybridized with the Tet K, Tet M, or Tet O determinant. A donor Peptostreptococcus anaerobius strain carrying the three determinants could transfer Tet M to P. anaerobius and Fusobacterium nucleatum recipients but not to an Enterococcus faecalis recipient, while neither Tet K nor Tet O was transferred.
The activities of erythromycin and clindamycin against 350 Peptostreptococcus strains were studied during a 5-year period (1986 to 1991). In 5.1% of the Peptostreptococcus strains, which presented dissociated resistance (clindamycin MIC, less than or equal to 1 microgram/ml; erythromycin MIC, greater than 8 micrograms/ml), evidence of inducible macrolide-lincosamide resistance was shown. A total of 17.7% of the strains presented a constitutive phenotype; the clindamycin and erythromycin MICs for these strains were greater than 8 micrograms/ml.
Eighty percent (21 of 26) of macrolide-resistant Peptostreptococcus strains studied harbored the ermTR gene. This methyltransferase gene is also the most frequently found gene among macrolide-lincosamide-streptogramin B-resistant Streptococcus pyogenes strains. Transfer of the ermTR gene from Peptostreptococcus magnus to macrolide-susceptible S. pyogenes strains indicates that this resistance determinant may circulate among gram-positive aerobic and anaerobic species of the oropharyngeal bacterial flora.
A monensin-sensitive ruminal peptostreptococcus was able to grow rapidly (growth rate of 0.5/h) on an enzymatic hydrolysate of casein, but less than 23% of the amino acid nitrogen was ever utilized. When an acid hydrolysate was substituted for the enzymatic digest, more than 31% of the nitrogen was converted to ammonia and cell protein. Coculture experiments and synergisms with peptide-degrading strains of Bacteroides ruminicola and Streptococcus bovis indicated that the peptostreptococcus was unable to transport certain peptides or hydrolyze them extracellularly. Leucine, serine, phenylalanine, threonine, and glutamine were deaminated at rates of 349, 258, 102, 95, and 91 nmol/mg of protein per min, respectively. Deamination rates for some other amino acids were increased when the amino acids were provided as pairs of oxidized and reduced amino acids (Stickland reactions), but these rates were still less than 80 nmol/mg of protein per min. In continuous culture (dilution rate of 0.1/h), bacterial dry matter and ammonia production decreased dramatically at a pH of less than 6.0. When dilution rates were increased from 0.08 to 0.32/h (pH 7.0), ammonia production increased while production of bacterial dry matter and protein decreased. These rather peculiar kinetics resulted in a slightly negative estimate of maintenance energy and could not be explained by a change in fermentation products. Approximately 80% of the cell dry matter was protein. When corrections were made for cell composition, the yield of ATP was higher than the theoretical maximum value. It is possible that mechanisms other than substrate-level phosphorylation contributed to the energetics of growth.
A recently isolated ruminal peptostreptococcus which produced large amounts of branched-chain volatile fatty acids grew rapidly with leucine as an energy source in the presence but not the absence of Na. Leucine transport could be driven by an artificial membrane potential (delta psi) only when Na was available, and a chemical gradient of Na+ (delta uNa+) also drove uptake. Because Na+ was taken up with leucine and a Z delta pH could not serve as a driving force (with or without Na), it appeared that leucine was transported in symport with Na+. The leucine carrier could use Li as well as Na and had a single binding site for Na+. The Km for Na was 5.2 mM, and the Km and Vmax for leucine were 77 microM and 328 nmol/mg of protein per min, respectively. Since valine and isoleucine competitively inhibited (Kis of 90 and 49 microM, respectively) leucine transport, it appeared that the peptostreptococcus used a common carrier for branched-chain amino acids. Valine or isoleucine was taken up rapidly, but little ammonia was produced if they were provided individually. The lack of ammonia could be explained by an accumulation of reducing equivalents. The ionophore, monensin, inhibited growth, but leucine was taken up and deaminated at a slow rate. Monensin caused a loss of K, an increase in Na, a slight increase in delta psi, and a decrease in intracellular pH. The inhibition of growth was consistent with a large decrease in ATP.(ABSTRACT TRUNCATED AT 250 WORDS)
Gas-liquid chromatography was employed to analyze the volatile and nonvolatile acids produced in modified norleucine-tyrosine (MNT) broth by various gram-positive cocci. The MNT broth consists of 0.5% Trypticase (BBL Microbiology Systems, Cockeysville, Md.), 0.5% yeast extract (Difco Laboratories, Detroit, Mich.), 0.2% L-norleucine, and 0.1% L-tyrosine. The microorganisms included reference strains and clinical isolates of Peptostreptococcus spp. (P. anaerobius, P. asaccharolyticus, P. indolicus, P. magnus, and P. prevotii), Staphylococcus spp. (S. aureus, S. epidermidis, and S. saccharolyticus), and Streptococcus spp. (S. agalactiae, S. intermedius, S. mutans, S. sanguis I, and S. sanguis II). Only Peptostreptococcus anaerobius strains produced caproic and valeric acids in MNT broth cultures. All 11 P. anaerobius strains produced valeric acid in MNT broth, and only 1 strain failed to produce caproic acid in the medium. This unique feature aids in rapid, reliable identification of P. anaerobius with a minimum number of tests.
Fifty-four strains of Peptostreptococcus magnus (11 were recovered from abdominal infections, 18 were from nonpuerperal breast abscesses, and 21 were from diabetic foot infections; the type strain and three other strains were from the American Type Culture Collection, Rockville, Md.) and the type strain of Peptostreptococcus micros were tested for their ability to produce various enzymes, including catalase, hippurate hydrolase, serine dehydratase, threonine dehydratase, collagenase, gelatinase, alkaline phosphatase, and esterase C4. The data were analyzed by cluster analysis. The results showed that all but one strain could be assigned to either of two distinct, valid clusters. The first cluster of 11 strains was composed of strains that were relatively inactive, having produced one or two of the eight strain-dependent enzymes. The second was a large cluster of strains (n = 43) that were considerably more active, all having produced at least three enzymes; the vast majority of strains (89%) produced four or more enzymes. The unclustered strain produced one enzyme that was different from that produced by the strains in the first cluster. The chi 2 test of homogeneity applied to the clustering solution indicated that greater enzyme activity was significantly associated with the site of infection (P less than 0.001). The more enzymatically active P. magnus strains were recovered significantly more often from nonpuerperal breast abscesses and diabetic foot infections than they were from abdominal infections. These results may provide insight into the nature of certain polymicrobial soft tissue infections and suggest that (i) P. magnus may participate more in nonpuerperal breast and diabetic foot infections than in abdominal infections and that (ii) peptostreptococcal production of proteolytic enzymes may have an important adjunctive effect on the pathogenesis of certain soft tissue infections.
A new tyrosine medium was developed and evaluated for the differentiation of Peptostreptococcus anaerobius from other anaerobic, gram-positive cocci. The strains included 159 originating from clinical specimens and 13 reference strains received from other workers in the field. Only one strain of each species was included in the study from multiple cultures from the same patient. This medium is simple to prepare and can be used in a small clinical laboratory. One hundred seventy-two strains of anaerobic gram-positive cocci were grown and evaluated with the new tyrosine medium; 36 strains (100%) of P. anaerobius degradated the tyrosine crystals when incubated at 37 degrees C under anaerobic conditions in a GasPak jar (Baltimore Biological Laboratory) for approximately 72 h. On the other hand, 135 of 136 other anaerobic gram-positive cocci were negative for tyrosine degradation, but grew on the tyrosine agar plate when incubated anaerobically. The single strain that degraded tyrosine was 1 of the 13 isolates of Peptostreptococcus micros studied.
Extracts from several species of gram-positive cocci were prepared by a modification of the Rantz-Randall autoclave method and tested for reactions with rabbit anti-Peptostreptococcus anaerobius (ATCC 27337 and VPI 5737) sera in a capillary precipitin test. Antigen preparations from two reference strains of P. anaerobius (ATCC 27337 and VPI 5737) and six clinical isolates of P. anaerobius reacted with the P. anaerobius antisera. These extracts formed a line of identity by immunodiffusion and displayed at least one precipitin line by immunoelectrophoresis. Absorption of the antisera with either the autoclaved extract or a 10% whole-cell suspension from each of the eight P. anaerobius strains removed the precipitin line(s) observed during immunodiffusion and immunoelectrophoresis. Extracts prepared to other species of Peptococcus, Peptostreptococcus, and Streptococcus did not react with the P. anaerobius antisera in a capillary precipitin test. In addition antisera to Lancefield groups A to G did not react with the extracts from the eight P. anaerobius strains. Preliminary chemical analysis of the extracts from the eight strains showed that they contained approximately 0.2 mg of carbohydrate per ml and 3.6 mg of protein per ml. The rabbit anti-P. anaerobius sera used in this study detected a common antigen(s) shared by strains of P. anaerobius, but did not react with autoclave extracts prepared from other species of gram-positive cocci. This extractable antigen could be used in a capillary precipitin test to rapidly identify P. anaerobius strains isolated in the clinical microbiology laboratory.
We describe a 30-year-old female presenting with synovitis of the left 4th proximal interphalangeal joint. Anaerobic cultures of the synovial membrane grew Peptostreptococcus magnus. The synovitis resolved after a course of intravenous penicillin G. The role of the anaerobic bacterium Peptostreptococcus magnus in joint infections is reviewed.
Peptostreptococcus ivorii, a recently described species of gram-positive anaerobic coccus, has so far rarely been found in human infections. The isolation of this anaerobe from a polybacterial skin abscess in a HIV-infected patient, which formed after antiretroviral therapy had been discontinued is reported. Local treatment led to the abscess healing without specific antibiotics. As the type strain was isolated from a mixed infected leg ulcer, Peptostreptococcus ivorii could play an important role in synergistic infections of the skin.
Members of genus Peptostreptococcus have previously been found to be distantly related to the type species, Peptostreptococcus anaerobius, on the basis of 16S rDNA sequence similarities. They were divided into three major phylogenetic groups, and their peptidoglycan structure and biochemical traits differed between groups. The reclassification of the species of these three groups into three new genera, Peptoniphilus gen. nov., Anaerococcus gen. nov. and Gallicola gen. nov., is proposed. The genus Peptoniphilus gen. nov. includes the following butyrate-producing, non-saccharolytic species that use peptone and amino acids as major energy sources: Peptoniphilus asaccharolyticus comb. nov. (type species), Peptoniphilus lacrimaris comb. nov., Peptoniphilus harei comb. nov., Peptoniphilus indolicus comb. nov. and Peptoniphilus ivorii comb. nov. The genus Anaerococcus gen. nov. contains the saccharolytic, butyrate-producing species Anaerococcus prevotii comb. nov. (type species), Anaerococcus tetradius comb. nov., Anaerococcus lactolyticus comb. nov., Anaerococcus hydrogenalis comb. nov., Anaerococcus vaginalis comb. nov. and Anaerococcus octavius sp. nov. The genus Gallicola gen. nov. contains a single species, Gallicola barnesae comb. nov.
BACKGROUND: Transvaginal ultrasound-guided aspiration of ovarian endometrioma has been applied and emphasized as a safe and simple procedure. CASE: Two 27-year-old infertile women, both gravida 0, para 0, underwent medical follow-up examinations for cases of ovarian endometrioma. Both had undergone transvaginal ultrasound-guided aspiration of ovarian endometrioma. Because both were continuously febrile and had abdominal pain and cysts with tenderness in spite of antibiotic therapies, both underwent laparotomies for treatment. In both cases, enucleation of the ovarian abscess revealed purulent and malodorous fluid that demonstrated Peptostreptococcus magnus in culture. CONCLUSION: We theorize that following transvaginal ultrasound-guided aspiration of ovarian endometrioma and fixation with pure ethanol, anaerobic infection by P. magnus occurred, and a cyst formed in the abscess.
Protein L is a multidomain cell wall constituent of certain strains of Peptostreptococcus magnus which binds to the variable domain of immunoglobulin kappa-light chains. A single immunoglobulin-binding domain of M(r) = 9000 from this protein has been isolated and crystallized. The crystals are of space group P4(2)2(1)2, with cell dimensions a = b = 66.9 A, c = 68.3 A, and diffract to at least 2.2 A resolution. The asymmetric unit of the crystal contains two molecules of the protein L domain, related by a noncrystallographic 2-fold axis, as revealed by a self-rotation function calculated with native diffraction data.
Enoate reductase present in Clostridium kluyveri and Clostridium spec. La 1 could be detected in three strains of C. tyrobutyricum and ten clostridia belonging to the groups of proteolytic and saccharolytic or proteolytic species, respectively. In C. pasteurianum, C. butyricum and C. propionicum enoate reductase could not be found even after growth on (E)-2-butenoate. A 2-oxo-carboxylate reductase was present in rather low activities in the non-proteolytic clostridia which produce enoate reductase. High activities (up to 10 U/mg protein) of 2-oxo-carboxylate reductase were found in six of ten proteolytic clostridia. The substrate specificities of the enoate reductase and the 2-oxo-carboxylate reductases from the proteolytic clostridia were determined with different alpha, beta-unsaturated carboxylates (enoates) and 2-oxo-carboxylates, respectively. Enoates as well as 2-oxo-carboxylates are intermediates of the pathway by which amino acids are degraded. An explanation is offered for the long known but not understood fact that in the Stickland reaction isoleucine always acts as an electron donor and leucine and phenylalanine can be electron acceptors as well as donors. Peptostreptococcus anaerobius converting some amino acids to the same products as C. sporogenes did this also with the intermediates which were found for the reductive deamination of amino acids in C. sporogenes, however, in crude extracts reduction of enoates occurred only in an activated form.
The determination of enzymatic activities in cell-free extracts of Acidaminococcus fermentans and Peptostreptococcus asaccharolyticus led to a refined scheme for the pathway of glutamate fermentation via (R)-2-hydroxyglutarate to acetate and butyrate. From the ratio of these products the amount of ATP generated by substrate level phosphorylation was calculated. Growth experiments with the organisms including Clostridium symbiosum and Clostridium tetanomorphum indicated that a sodium gradient contributed additional energy for growth. The high growth yields found in organisms containing the biotin dependent sodium pump glutaconyl-CoA decarboxylase could be reduced by the sodium ionophor monensin. In P. asaccharolyticus energy equivalent up to 0.6 mol ATP per mol of glutaconyl-CoA decarboxylated was conserved via the Na+ gradient. The data may explain the growth promoting effects of monensin in cattle.
We describe the favourable long-term outcome after late total knee joint prosthesis infection in an elderly RA patient. Peptostreptococcus micros and Propionibacterium acnes were cultured from the synovial fluid, and the finding of a coexistent abscess at the root of a wisdom tooth suggested a dental origin to the joint infection. Long-term antibiotics in conjunction with aspiration/irrigation resulted in salvage of the implant and an excellent functional outcome.
A continuous fluorometric assay that utilizes apoflavodoxin as a trapping agent for riboflavin 5'-phosphate (FMN) has been developed for flavokinase (ATP:riboflavin 5'-phosphotransferase, EC 2.7.1.26). Use of this assay is illustrated in a procedure for the partial purification of flavokinase from the strict anaerobe Peptostreptococcus elsdenii. The purified enzyme catalyzed the formation of 8.3 nmol FMN - min-1 - mg-1 at 37 degrees C and had apparent Km values for riboflavin and ATP of 10 and 4.7 micronM, respectively. ATP could be replaced by ADP (22% of the rate observed with ATP) but not by GTP. The enzyme also phosphorylated 5-deaza- and 8-bromoriboflavin with activities of 15 and 70%, respectively, of that with riboflavin; it was inactive with iso riboflavin and deoxyriboflavin.