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Canadian Journal of Microbiology Mar 1998One hundred Peptostreptococcus isolates from five species were assessed for their ability to hydrolyze gelatin. Most Peptostreptococcus magnus (95.8%) and...
One hundred Peptostreptococcus isolates from five species were assessed for their ability to hydrolyze gelatin. Most Peptostreptococcus magnus (95.8%) and Peptostreptococcus micros isolates (79.0%) hydrolyzed gelatin in contrast to Peptostreptococcus asaccharolyticus (8.0%), Peptostreptococcus anaerobius (10.0%), and Peptostreptococcus prevotii isolates (16.7%). Gelatin hydrolysis in Peptostreptococcus magnus and Peptostreptococcus micros isolates correlated (r = 0.80; P = 0.0019) with more aminopeptidases produced than Peptostreptococcus asaccharolyticus, Peptostreptococcus anaerobius, or Peptostreptococcus prevotii. The five species were further classified into three groups using the extended Tukey test (P < 0.0001) based on the mean percentage of aminopeptidases produced by each species with Peptostreptococcus magnus and Peptostreptococcus micros belonging to group I, Peptostreptococcus asaccharolyticus and Peptostreptococcus prevotii belonging to group II, and Peptostreptococcus anaerobius forming group III. An analysis of possible proteolytic activity of four selected Peptostreptococcus magnus isolates indicated that only 5 of 11 substrates were hydrolyzed as compared to a control isolate of Porphyromonas gingivalis W83, which had a strong proteolytic profile. Therefore, gelatin hydrolysis by Peptostreptococcus spp., in particular Peptostreptococcus magnus and Peptostreptococcus micros, is probably due to a variety of aminopeptidases rather than proteinases.
Topics: Aminopeptidases; Gelatin; Humans; Hydrolysis; Peptostreptococcus; Species Specificity; Substrate Specificity
PubMed: 9606913
DOI: No ID Found -
Antimicrobial Agents and Chemotherapy Dec 1981Peptostreptococcus anaerobius VPI 4330-1 was tested under various conditions for examination of the bactericidal effect of hydrogen peroxide. The cells were most rapidly...
Peptostreptococcus anaerobius VPI 4330-1 was tested under various conditions for examination of the bactericidal effect of hydrogen peroxide. The cells were most rapidly killed by hydrogen peroxide when they were in the exponential-growth phase. Cooling or starving the cells decreased the bactericidal effect of hydrogen peroxide. The ionophore nigericin and the metal ion chelating agent 2,2'-bipyridine stopped macromolecular syntheses and greatly decreased the bactericidal effect of hydrogen peroxide. The ionophore valinomycin and the glycolytic inhibitor iodoacetate also stopped the syntheses of the macromolecules but only slightly decreased the bactericidal effect of hydrogen peroxide. Novobiocin, an inhibitor of deoxyribonucleic acid gyrase, and chloramphenicol, an inhibitor of protein synthesis, were not able to decrease the bactericidal effect of hydrogen peroxide. These findings implicate metal ions and an active metabolism of the organism in the bactericidal effect of hydrogen peroxide.
Topics: Antimetabolites; Bacterial Proteins; DNA, Bacterial; Hydrogen Peroxide; Peptostreptococcus; RNA, Bacterial; Temperature; Time Factors
PubMed: 6173014
DOI: 10.1128/AAC.20.6.726 -
American Journal of Ophthalmology Aug 1985
Topics: Aged; Anaerobiosis; Bacterial Infections; Corneal Transplantation; Culture Media; Female; Humans; Keratitis; Peptostreptococcus; Postoperative Complications
PubMed: 3895968
DOI: 10.1016/0002-9394(85)90810-4 -
Microbiology (Reading, England) May 1995The surface ultrastructure of three anaerobic Gram-positive cocci frequently encountered in oral infections, Peptostreptococcus micros, P. magnus and P. anaerobius, was... (Comparative Study)
Comparative Study
The surface ultrastructure of three anaerobic Gram-positive cocci frequently encountered in oral infections, Peptostreptococcus micros, P. magnus and P. anaerobius, was studied. The type strains of P. micros (DSM 20468) and P. anaerobius (ATCC 27337), several clinical isolates of both species and the type strain of P. magnus (DSM 20470) were included. Thin-sectioned cells studied by electron microscopy revealed a homogeneous layer outside the peptidoglycan layer in P. anaerobius. In P. micros and P. magnus a more amorphous layer was present. No periodic structures were seen in negatively stained whole cells of these three species. However, in freeze-etched cells of P. anaerobius a crystalline surface protein layer (S-layer) was detected. No periodicity was seen in any of the P. micros strains or the P. magnus type strain by the methods used, but a periodic pattern was observed in negatively stained specimens of cell wall fragments of sonicated P. anaerobius cells. No capsular material was visible outside the S-layer in P. anaerobius. The cells of the Peptostreptococcus spp. were extracted for 30 min with detergents and urea. One per cent SDS and M urea both extracted a major 78 kDa protein from all strains of P anaerobius. Extraction of P. micros and P. magnus cells did not reveal any major protein bands comparable to that of P. anaerobius. Surface biotinylation of cells followed by Western blotting and detection by alkaline-phosphatase-conjugated extravidin showed strong staining of the 78 kDa band in P. anaerobius, further indicating that this molecule is located on the surface of the cell and is the S-protein.(ABSTRACT TRUNCATED AT 250 WORDS)
Topics: Bacterial Proteins; Blotting, Western; Cell Membrane; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Freeze Etching; Humans; Membrane Proteins; Microscopy, Electron; Peptostreptococcus; Species Specificity
PubMed: 7773401
DOI: 10.1099/13500872-141-5-1065 -
Antimicrobial Agents and Chemotherapy Jun 2007Peptostreptococcus anaerobius sensu lato, currently including two closely related species, P. anaerobius and P. stomatis, is known to be more resistant than other...
Peptostreptococcus anaerobius sensu lato, currently including two closely related species, P. anaerobius and P. stomatis, is known to be more resistant than other gram-positive anaerobic cocci. We reidentified potential Peptostreptococcus isolates and tested their susceptibilities to eight antimicrobials. Notably, P. anaerobius had constantly higher values for the MIC at which 50% of the isolates are inhibited (MIC(50)) and the MIC(90) than P. stomatis.
Topics: Anaerobiosis; Anti-Bacterial Agents; Bacteremia; Gram-Positive Bacterial Infections; Humans; Microbial Sensitivity Tests; Peptostreptococcus; Species Specificity
PubMed: 17403999
DOI: 10.1128/AAC.00056-07 -
Zhurnal Mikrobiologii, Epidemiologii I... 1996A case of an acute disease with a rapid clinical course and a fatal outcome in the presence of irreversible toxicoinfectious shock, appearing in two children after the... (Review)
Review
A case of an acute disease with a rapid clinical course and a fatal outcome in the presence of irreversible toxicoinfectious shock, appearing in two children after the consumption of sheep kidneys, is described. The post mortem examination of the children revealed the presence of hemorrhagic, erosive and necrotic areas on the mucous membrane of the stomach, the duodenum and the upper section of the small intestine. From the material obtained by probing the stomach of one of the children 6 hours before death P.asaccharolyticus and B.cereus were isolated. Hemorrhage, erosions and necrosis were also found in experimental mice, injected with the centrifugates of the gastric secretions of the patient and the cultures of the isolated bacteria, which was indicative of the presence of highly active exotoxin. On the basis of the above facts, compared with similar data in the literature, this case was considered to be etiologically related anaerobic Peptostreptococcus in symbiosis with B.cereus.
Topics: Acute Disease; Adolescent; Animals; Bacillaceae Infections; Bacillus cereus; Child; Fatal Outcome; Female; Foodborne Diseases; Gram-Positive Bacterial Infections; Humans; Mice; Peptostreptococcus; Shock, Septic
PubMed: 9103069
DOI: No ID Found -
Journal of Clinical Microbiology Apr 1976Of 13 species of anaerobic cocci, Peptostreptococcus anaerobius was the only species tested that was sensitive to 0.1% sodium polyanetholsulfonate (SPS). However, the... (Comparative Study)
Comparative Study
Of 13 species of anaerobic cocci, Peptostreptococcus anaerobius was the only species tested that was sensitive to 0.1% sodium polyanetholsulfonate (SPS). However, the sensitivity of P. anaerobius to SPS varied according to the media in which the cultures were grown. In supplemented peptone (B-D) and brain heart infusion media, most strain of P. anaerobius were not inhibited by SPS. Gelatin and proteose peptone were the medium components which were protective. The minimal inhibitory concentration of SPS for P. anaerobius was approximately 60-fold higher in media. However, the concentration of SPS required to neutralize the bactericidal properties of human serum was only four fold higher in media containing geltain. In a commerical medium containing SPS (0.03%) and gelatin (1.2%), SPS-sensitive strains of P. anaerobius were not inhibited by SPS, and the bactericdal action of human blood on Escherichia coli C and Serratia marcescens SM 29 was eliminated.
Topics: Anaerobiosis; Anticoagulants; Blood; Blood Bactericidal Activity; Caseins; Culture Media; Escherichia coli; Gelatin; Humans; Peptones; Peptostreptococcus; Serratia marcescens; Serum Albumin, Bovine
PubMed: 770497
DOI: 10.1128/jcm.3.4.393-396.1976 -
Journal of Pharmacobio-dynamics Oct 1985Peptostreptococcus intermedius, one of the dominant bacteria of human intestine, reduced sennidin and sennoside to rheinanthrone and 8-glucosyl-rheinanthrone,...
Peptostreptococcus intermedius, one of the dominant bacteria of human intestine, reduced sennidin and sennoside to rheinanthrone and 8-glucosyl-rheinanthrone, respectively, and these reduction rates were stimulated by the addition of nicotinamide adenine dinucleotide (reduced form) (NADH), flavin adenine dinucleotide (FAD) and glucose. The reduction was accelerated by removing oxygen from the incubation tubes, which indicates the inhibition of the reduction by O2. Thus, for the maximal activity, the reaction system required an anaerobic condition and cofactors, NADH and FAD. This bacterium also reduced methyl orange, whose mode of reduction resembled that of sennidin reduction. More than 80% of these activities were recovered in the supernatant fraction after sonication of the bacterial suspension, and these activities were purified together by means of Sephadex G-200 gel-filtration and diethylaminoethyl-cellulose column chromatography. The purified enzyme reduced FAD and benzyl viologen in the presence of NADH under an anaerobic condition.
Topics: Anthracenes; Anthraquinones; Azo Compounds; Flavin-Adenine Dinucleotide; Kinetics; Molecular Weight; NAD; Oxidation-Reduction; Oxidoreductases; Peptostreptococcus; Senna Extract; Sennosides; Spectrophotometry, Ultraviolet
PubMed: 3841560
DOI: 10.1248/bpb1978.8.800 -
Structure (London, England : 1993) Aug 2001Peptostreptococcus magnus protein L (PpL) is a multidomain, bacterial surface protein whose presence correlates with virulence. It consists of up to five homologous...
BACKGROUND
Peptostreptococcus magnus protein L (PpL) is a multidomain, bacterial surface protein whose presence correlates with virulence. It consists of up to five homologous immunoglobulin binding domains that interact with the variable (VL) regions of kappa light chains found on two thirds of mammalian antibodies.
RESULTS
We refined the crystal structure of the complex between a human antibody Fab fragment (2A2) and a single PpL domain (61 residues) to 2.7 A. The asymmetric unit contains two Fab molecules sandwiching a single PpL domain, which contacts similar VL framework regions of two light chains via independent interfaces. The residues contacted on VL are remote from the hypervariable loops. One PpL-Vkappa interface agrees with previous biochemical data, while the second is novel. Site-directed mutagenesis and analytical-centrifugation studies suggest that the two PpL binding sites have markedly different affinities for VL. The PpL residues in both interactions are well conserved among different Peptostreptococcus magnus strains. The Fab contact positions identified in the complex explain the high specificity of PpL for antibodies with kappa rather than lambda chains.
CONCLUSIONS
The PpL-Fab complex shows the first interaction of a bacterial virulence factor with a Fab light chain outside the conventional combining site. Structural comparison with two other bacterial proteins interacting with the Fab heavy chain shows that PpL, structurally homologous to streptococcal SpG domains, shares with the latter a similar binding mode. These two bacterial surface proteins interact with their respective immunoglobulin regions through a similar beta zipper interaction.
Topics: Amino Acid Sequence; Antigen-Antibody Complex; Bacterial Proteins; Crystallography, X-Ray; DNA-Binding Proteins; Humans; Hydrogen Bonding; Immunoglobulin Fab Fragments; Immunoglobulin M; Immunoglobulins; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptostreptococcus; Protein Binding; Protein Structure, Tertiary
PubMed: 11587642
DOI: 10.1016/s0969-2126(01)00630-x -
Journal of Bacteriology Dec 1975In Peptostreptococcus elsdenii, a three-component flavoprotein electron transfer system catalyzes the oxidation of lactate and the reduction of crotonyl-coenzyme A...
In Peptostreptococcus elsdenii, a three-component flavoprotein electron transfer system catalyzes the oxidation of lactate and the reduction of crotonyl-coenzyme A (CoA). Spectral evidence showed that D-lactate dehydrogenase, when reduced by D-lactate, was able to reduce butyryl-CoA dehydrogenase, but only in the presence of the electron-transferring flavoprotein. Reduced nicotinamide adenine dinucleotide could replace reduced D-lactate dehydrogenase. A reconstituted system, containing the three partially purified enzymes, excess D-lactate, and a limiting amount of crotonyl-CoA, reduced the crotonyl-CoA to butyryl-CoA, but only if all components were present. The electron-transferring flavoprotein activity, purified 22-fold, was separated into two major flavoprotein components, A and B, after polyacrylamide gel electrophoresis. Elution of the proteins and subsequent kinetic assays of the eluates showed that component B catalyzes the reduction of butyryl-CoA dehydrogenase by reduced D-lactate dehydrogenase, whereas component A does not. Both A and B catalyzed the reduction of butyryl-CoA dehydrogenase by reduced nicotinamide adenine dinucleotide. The results suggest that the D-lactate dehydrogenase-dependent reduction involves a heretofore unrecognized component of the electron-transferring protein group which may utilize an unusual flavin, 6-hydroxy-7,8-dimethyl-10-(ribityl-5'-adenosine diphosphate)-isoalloxazine.
Topics: Acrylates; Acylation; Butyrates; Coenzyme A; Crotonates; Electron Transport; Flavoproteins; L-Lactate Dehydrogenase; Lactates; NAD; Oxidation-Reduction; Oxidoreductases; Peptostreptococcus; Stereoisomerism
PubMed: 172488
DOI: 10.1128/jb.124.3.1447-1453.1975