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European Journal of Biochemistry May 1998A neutral O-specific polysaccharide obtained from the lipopolysaccharide of Proteus penneri strain 26 was studied using sugar analysis and 1H and 13C NMR spectroscopy,...
Structure and cross-reactivity of the O-specific polysaccharide of Proteus penneri strain 26, another neutral Proteus O-antigen containing 2-acetamido-2,6-dideoxy-L-glucose (N-acetyl-L-quinovosamine).
A neutral O-specific polysaccharide obtained from the lipopolysaccharide of Proteus penneri strain 26 was studied using sugar analysis and 1H and 13C NMR spectroscopy, including two-dimensional NMR techniques. The following structure of the trisaccharide repeating unit was established: -->6)-alpha-D-GlcpNAc-(1-->3)-alpha-L-QuipNAc-(1-->3)-alpha-D-Glcp NAc-(1--> where L-QuiNAc is 2-acetamido-2,6-dideoxy-L-glucose (N-acetyl-L-quinovosamine). Cross-reactivity of the Proteus penneri 26 anti-O serum with other strains of P. penneri isolated in Poland and USA and one strain of P. vulgaris is discussed.
Topics: Acetylglucosamine; Animals; Carbohydrate Conformation; Carbohydrate Sequence; Cross Reactions; Hemagglutination Tests; Hemolysis; Immune Sera; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; O Antigens; Proteus; Rabbits
PubMed: 9654072
DOI: 10.1046/j.1432-1327.1998.2530730.x -
Heart & Lung : the Journal of Critical... 1998Proteus penneri has been isolated from many different clinical sources, including surgical wound infections, urine, and blood. We describe the first reported case of P....
Proteus penneri has been isolated from many different clinical sources, including surgical wound infections, urine, and blood. We describe the first reported case of P. penneri nosocomial urosepsis in a patient with diabetes. P. penneri was subsequently isolated from bronchoalveolar lavage fluid and a pulmonary artery catheter tip.
Topics: Aged; Cross Infection; Diabetes Complications; Female; Humans; Proteus; Proteus Infections; Urinary Tract Infections
PubMed: 9548071
DOI: 10.1016/s0147-9563(98)90023-1 -
Microbiology and Molecular Biology... Mar 1997The object of this review is the genus Proteus, which contains bacteria considered now to belong to the opportunistic pathogens. Widely distributed in nature (in soil,... (Review)
Review
The object of this review is the genus Proteus, which contains bacteria considered now to belong to the opportunistic pathogens. Widely distributed in nature (in soil, water, and sewage), Proteus species play a significant ecological role. When present in the niches of higher macroorganisms, these species are able to evoke pathological events in different regions of the human body. The invaders (Proteus mirabilis, P. vulgaris, and P. penneri) have numerous factors including fimbriae, flagella, outer membrane proteins, lipopolysaccharide, capsule antigen, urease, immunoglobulin A proteases, hemolysins, amino acid deaminases, and, finally, the most characteristic attribute of Proteus, swarming growth, enabling them to colonize and survive in higher organisms. All these features and factors are described and commented on in detail. The questions important for future investigation of these facultatively pathogenic microorganisms are also discussed.
Topics: Bacterial Outer Membrane Proteins; Bacterial Proteins; Carbohydrate Sequence; Disease Susceptibility; Drug Resistance, Microbial; Fimbriae, Bacterial; Flagella; Hemolysin Proteins; Humans; Hydro-Lyases; Lipid A; Lipopolysaccharides; Metalloendopeptidases; Molecular Sequence Data; Polymyxins; Proteus; Proteus Infections; Proteus mirabilis; Proteus vulgaris; Serine Endopeptidases; Urease
PubMed: 9106365
DOI: 10.1128/mmbr.61.1.65-89.1997 -
European Journal of Biochemistry Aug 1996An acidic O-specific polysaccharide isolated from Proteus penneri 52 contains D-galacturonic acid, 2-acetamido-2-deoxy-D-glucose, and 2-acetamido-2-deoxy-D-galactose in...
An acidic O-specific polysaccharide isolated from Proteus penneri 52 contains D-galacturonic acid, 2-acetamido-2-deoxy-D-glucose, and 2-acetamido-2-deoxy-D-galactose in the ratio 1:2:2. On the basis of sugar analysis and NMR spectroscopy, which included one-dimensional TOCSY, two-dimensional COSY, heteronuclear 13C, 1H-COSY, and rotating-frame NOE spectroscopy, the following structure of the pentasaccharide repeating unit of the O-specific polysaccharide was established: [sequence: see text] Cross-reactivity of the anti-P-penneri 52 O-serum with other strains of P. penneri isolated in Germany. Poland, USA, and Canada is discussed and a new Proteus serogroup is proposed.
Topics: Carbohydrate Conformation; Carbohydrate Sequence; Cross Reactions; Immune Sera; Magnetic Resonance Spectroscopy; Molecular Sequence Data; O Antigens; Oligosaccharides; Proteus
PubMed: 8797860
DOI: 10.1111/j.1432-1033.1996.0245h.x -
European Journal of Biochemistry Jun 1995O-specific polysaccharide was isolated from Proteus penneri strain 12 (ATCC 33519) lipopolysaccharide (LPS) and studied using NMR spectroscopy, including selective...
O-specific polysaccharide was isolated from Proteus penneri strain 12 (ATCC 33519) lipopolysaccharide (LPS) and studied using NMR spectroscopy, including selective spin-decoupling, one-dimensional NOE, two-dimensional homonuclear correlation spectroscopy, 13C,1H heteronuclear correlation spectroscopy and chemical methods (O-deacetylation, Smith degradation, partial acid hydrolysis followed by borohydride reduction and methylation). The amide of D-galacturonic acid with L-threonine [D-GalA(L-Thr)] was identified as a constituent of the polysaccharide and the following structure of the tetrasaccharide repeating unit was established: [formula: see text] where the degree of O-acetylation at either position varies over 20-40%. Serological study with LPS, its degradation products and related synthetic glycoconjugates (2-acrylamidoethyl glycosides of amides of alpha-D-GalA with L-amino acids copolymerised with acrylamide) showed that D-GalA(L-Thr) plays an important role in manifesting the serological specificity of the P. penneri 12 O-antigen. Serological cross reactions between LPSs of P. penneri 12 and Proteus mirabilis S1959, R14/S1959 (transient-like form), O23 and O28 are discussed.
Topics: Amides; Carbohydrate Conformation; Carbohydrate Sequence; Epitopes; Hexuronic Acids; Magnetic Resonance Spectroscopy; Molecular Sequence Data; O Antigens; Polysaccharides, Bacterial; Proteus; Serology; Threonine
PubMed: 7541754
DOI: No ID Found -
Journal of Clinical Microbiology Apr 1994The ability of the RapID onE system (Innovative Diagnostic Systems, Inc., Norcross, Ga.) to identify 364 strains in the family Enterobacteriaceae and 15...
The ability of the RapID onE system (Innovative Diagnostic Systems, Inc., Norcross, Ga.) to identify 364 strains in the family Enterobacteriaceae and 15 oxidase-negative, gram-negative, nonfermentative rods was evaluated. Kits were inoculated with no. 2 McFarland standard suspensions, and reactions were interpreted after 4 h of incubation at 35 degrees C. Overall, the method correctly identified (to the species level or to the genus level for salmonellas and non-Shigella sonnei Shigella species) 363 strains (95.8%) without additional tests. For four strains (1.0%), additional tests were required to delineate the correct identification from a range of two or more possibilities; these included one Serratia liquefaciens (Serratia marcescens or Serratia liquefaciens), one Serratia rubidaea (Serratia rubidaea or Serratia odorifera), one Salmonella typhi (Leminorella richardii or Salmonella sp.) and one Yersinia enterocolitica (Yersinia frederiksenii, Yersinia intermedia, or Yersinia enterocolitica). Twelve strains (3.2%) were misidentified or yielded codes with no identification; these comprised one Citrobacter amalonaticus (no identification), three Enterobacter hormaechei (not in the RapID onE database; two Enterobacter amnigenus, one Enterobacter sp.), one Serratia liquefaciens (Enterobacter cloacae), one Serratia rubidaea (no identification), four Serratia fonticola (not in RapID onE database; two Enterobacter aerogenes, one Serratia marcescens, one not identified), one Proteus mirabilis (Proteus penneri), and one Proteus vulgaris (Providencia rustigianii). If the seven strains not included in the database had been excluded, correct identification rates would have risen to 97.6% without additional tests and 98.7% with additional tests, with misidentification rates dropping to 1.3%. The RapID onE system is easy to set up and the results are easy to read, and the system provides an accurate, nonautomated commercially available method for the same-day identification of members of the family Enterobacteriaceae and oxidase-negative, gram-negative nonfermenters.
Topics: Bacteriological Techniques; Enterobacteriaceae; Evaluation Studies as Topic; Fermentation; Gram-Negative Bacteria; Humans; Oxidoreductases; Sensitivity and Specificity
PubMed: 8027345
DOI: 10.1128/jcm.32.4.931-934.1994 -
Infection and Immunity Jun 1992The proteinases secreted by pathogenic strains of Proteus mirabilis, P. vulgaris biotype 2, P. vulgaris biotype 3, and P. penneri were purified with almost 100% recovery...
The proteinases secreted by pathogenic strains of Proteus mirabilis, P. vulgaris biotype 2, P. vulgaris biotype 3, and P. penneri were purified with almost 100% recovery by affinity chromatography on phenyl-Sepharose followed by anion-exchange chromatography. The proteinase purified from the urinary tract pathogen P. mirabilis, which we had previously shown to degrade immunoglobulins A and G, appeared as a composite of a single band and a double band (53 and 50 kDa, respectively) on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The other Proteus proteinases had similar patterns but slightly different mobilities. In each case all proteinase activity in culture supernatants was demonstrated by gelatin-sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be associated with only the triple-band complex; all three bands were proteolytically active. The P. mirabilis proteinase was resistant to inhibitors of both serine and thiol proteinases but strongly inhibited by metal chelators, although it was not affected by phosphoramidon, an inhibitor of the thermolysin group of bacterial metalloproteinases. Active proteinase was detected in urine samples from P. mirabilis-infected patients; this is consistent with our detection of immunoglobulin A fragments of a size suggestive of P. mirabilis proteinase activity.
Topics: Chromatography, Affinity; Endopeptidases; Female; Humans; Hydrogen-Ion Concentration; Immunoglobulin A; Immunoglobulin G; Male; Proteus Infections; Proteus mirabilis
PubMed: 1587593
DOI: 10.1128/iai.60.6.2267-2273.1992 -
European Journal of Biochemistry Apr 1991O-Specific polysaccharide was obtained by mild acid degradation of Proteus penneri strain 16 lipopolysaccharide and found to contain D-glucose, D-glucuronic acid,...
O-Specific polysaccharide was obtained by mild acid degradation of Proteus penneri strain 16 lipopolysaccharide and found to contain D-glucose, D-glucuronic acid, 2-acetamido-2-deoxy-D-glucose, and 3,6-dideoxy-3-[(R)-3-hydroxybutyramido]- D-galactose in the ratio of 2:1:1:1 as well as a small proportion of O-acetyl groups. On the basis of one-dimensional 1H-NMR13C-NMR and NOE spectroscopy, two-dimensional homonuclear-shift-correlated spectroscopy with one-step and two-step relayed coherence transfer and heteronuclear 1H/13C NMR shift-correlated spectroscopy, it was concluded that the O-specific polysaccharide of P. penneri strain 16 has the following structure: (formula; see text) This structure was confirmed by methylation analysis and structural analysis of a linear tetrasaccharide fragment prepared by cleavage of the polysaccharide with anhydrous hydrogen fluoride followed by conversion of the alpha-tetrosyl fluoride obtained in to the corresponding free oligosaccharide and alditol. O-Acetyl groups were tentatively located at position 3 of the glucuronic acid residue and at position 4 of the 6-substituted glucose residue, the degree of acetylation being less than 20% of the total. Cross-reactions of P. penneri strain 16 anti-(O-specific polysaccharide) antiserum with lipopolysaccharides from several other Proteus strains and the role of 3,6-dideoxy-3-(R)-3-hydroxybutyramido-D-galactose in the serological specificity of P. penneri strain 16 are discussed.
Topics: Carbohydrate Conformation; Carbohydrate Sequence; Electrophoresis, Polyacrylamide Gel; Immune Sera; Immunoblotting; Indicators and Reagents; Lipopolysaccharides; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Oligosaccharides; Polysaccharides, Bacterial; Proteus vulgaris
PubMed: 2015828
DOI: 10.1111/j.1432-1033.1991.tb15886.x -
Journal of Clinical Microbiology Jul 1990Proteus penneri bacteremia and concomitant subcutaneous infection developed in a neutropenic patient with acute lymphocytic leukemia. The skin infection occurred while...
Proteus penneri bacteremia and concomitant subcutaneous infection developed in a neutropenic patient with acute lymphocytic leukemia. The skin infection occurred while the patient was being treated empirically with cefoperazone and metronidazole. This case demonstrates the invasive potential of this microorganism in the proper setting.
Topics: Abscess; Humans; Male; Middle Aged; Neutropenia; Precursor Cell Lymphoblastic Leukemia-Lymphoma; Proteus Infections; Sepsis; Skin Diseases, Infectious
PubMed: 2380386
DOI: 10.1128/jcm.28.7.1645-1646.1990 -
Journal of Clinical Microbiology Dec 1987Ten strains of Proteus penneri isolated from geographically diverse laboratories were tested for urease activity. Cell lysates from urea-induced cells had a mean... (Comparative Study)
Comparative Study
Ten strains of Proteus penneri isolated from geographically diverse laboratories were tested for urease activity. Cell lysates from urea-induced cells had a mean activity of 4.9 +/- 4.1 mumol of NH3 per min per mg of protein. On nondenaturing 6% polyacrylamide activity gels, the enzymes of P. penneri had very similar electrophoretic mobilities within species and within the Proteus genus but were distinct from the ureases of Providencia and Morganella species. On lower-percentage polyacrylamide, differences in mobilities of the ureases could be detected between the Proteus species. From representative strains, the P. penneri urease was found to be inducible by growth in urea and had an apparent molecular weight of 246,000 +/- 9,000, an isoelectric point of 5.1, and a Km for urea of 14 mM and was inhibitable by acetohydroxamic acid, hydroxyurea, and EDTA. In an in vitro model of struvite formation, a P. penneri strain produced abundant crystals on a glass rod submerged in synthetic urine in the absence but not presence of acetohydroxamic acid (500 micrograms/ml).
Topics: Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Hydrolysis; Isoelectric Focusing; Isoelectric Point; Kinetics; Molecular Weight; Proteus; Urea; Urease
PubMed: 3429622
DOI: 10.1128/jcm.25.12.2302-2305.1987