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PubMed2005

Interleukin-8 response in cells from the human urinary tract induced by lipopolysaccharides of Proteus mirabilis O3 and O18.

PURPOSE: Proteus mirabilis is a common pathogen associated mainly with complicated urinary tract infections and sometimes with septicemia. There is great serological diversity of the microorganism. While P. mirabilis O3 is commonly found in patients with infections, the serotype O18 rarely occurs. The O18 lipopolysaccharide contains a phosphocholine substitute, which makes it unique among Proteus strains. To explain different clinical significance of the strains we evaluated the biological activity of the lipopolysaccharides of P. mirabilis O3 and O18, as measured by interleukin-8 (IL-8) production. MATERIALS AND METHODS: Three cell lines were used, namely uroepithelial cells, renal epithelial cells and monocytes. IL-8 production was determined on the protein and mRNA levels using enzyme-linked immunosorbent assay and real-time polymerase chain reaction, respectively, and CD14 expression on the cell surface was studied using flow cytometry. RESULTS: Uroepithelial cells and monocytes reacted to lipopolysaccharides by higher IL-8 production compared with renal epithelial cells. Cell specific IL-8 response corresponded to the cell expression of CD14. Renal epithelial cells produced more IL-8 after stimulation with the phosphocholine rich lipopolysaccharide O18, although adding phosphocholine alone did not induce or increase IL-8 production. CONCLUSIONS: Our data suggest that different cells within the human urinary tract have different roles during urinary tract infection. The biological activity and pathogenicity of P. mirabilis lipopolysaccharides might be determined by their specific chemical structure.

Cell Line↗
PubMed1995

Replacement of NCTC 4175, the current type strain of Proteus vulgaris, with ATCC 29905. Request for an opinion.

The current type strain of Proteus vulgaris, NCTC 4175 (= ATCC 13315), differs substantially from typical strains of this species both biochemically and chemotaxonomically. DNA relatedness studies revealed that strains previously classified as P. vulgaris belong to six genomospecies. One of these genomospecies contains strains that are negative in indole, salicin, and esculin reactions (biogroup 1) and has been named Proteus penneri. A second genomospecies, which is most frequently isolated from human urine, contains typical P. vulgaris strains that are positive in indole, salicin, and esculin reactions (biogroup 2). The members of the remaining four genomospecies are indole positive and negative in salicin and esculin reactions (biogroup 3). Of 36 biogroup 3 strains studied, only strain NCTC 4175T (T = type strain) and one other strain, CDC 1732-80, belong to genomospecies 3. To retain NCTC 4175 as the type strain of P. vulgaris would restrict this species to these two strains, whose origins are unknown. This would mean that hundreds of strains for which the description of P. vulgaris was written and which have been representatives of this species for the past 50 years would have to be renamed as members of a new species. To prevent this confusion, we request that biogroup 2 reference strain ATCC 29905 (= CDC PR1) replace NCTC 4175 as the type strain of P. vulgaris.

DNA, Bacterial↗
PubMed1980

Expression of the lactose transposon Tn951 in Escherichia coli, Proteus and Pseudomonas.

The control of beta-galactosidase specified by the lactose transposon Tn951 (inserted into RP1 to give pGC9114) has been studied in Escherichia coli K12, Proteus mirabilis, Pseudomonas aeruginosa and Pseudomonas putida; in the first two species comparison could be made with Flac. In E. coli K12, the Tn951 and chromosomally encoded enzymes showed marked qualitative differences in regulatio, the former giving a substantially lower maximum induced level and induction ratio. Several parameters were slightly affected by strain background. In P. mirabilis, beta-galactosidase control determined by both Flac (in accord with earlier work) and pGC9114 was markedly different from E. coli in that maximal induced levels were about an order of magnitude lower and the induction ratio was reduced to 3 to 5. In Ps. aeruginosa and Ps. putida, Tn951-specified lac expression was qualitatively similar to that in P. mirabilis. Possible reasons for anomalous expression in Proteus and Pseudomonas are discussed.

DNA Transposable Elements↗
PubMed1984

Proteus mirabilis chromosome mobilization by plasmid D: a physical characterization.

Plasmid D, a hybrid of plasmids P-lac and R1 drd19, mediates polarized chromosome mobilization from one origin in Proteus mirabilis strain PM5006, while the parental plasmids neither individually nor combined mobilize this chromosome. To elucidate its acquired mobilizing ability plasmid D was characterized physically in relation to P-lac and R1 drd19. Restriction patterns of these plasmids were compared and it was shown that D consists of P-lac and only the r-determinant (r-det) of R1 drd19. A mechanism for the formation of plasmid D, via transduction of the r-det and subsequent transposon-like integration into P-lac, involving insertion sequence IS1, was suggested. Evidence for aberration in plasmid D DNA as a result of r-det integration into P-lac was attributed to IS1 elements which flank the r-det. Recombination regions of parental plasmid DNA were located on HindIII fragments alpha and beta of plasmid D and were subsequently inserted in vitro into IncP-1 plasmid RP4 that fails to mobilize the P. mirabilis chromosome. RP4::HindIII alpha plasmids did not mobilize the latter chromosome, but rendered the Proteus host lac+. RP4::HindIII beta plasmids pMC1 and pMC17, containing the fragment in opposite orientations, mobilized the P. mirabilis chromsome. For pMC17, mobilization was indistinguishable from that of plasmid D, i.e. having the same orientation and the same single origin. However, mobilization promoted by pMC1 was from two distinctly different origins, different from that of pMC17. This apparently deviates from known examples where inversion of homologous DNA inserted into plasmids leads to mobilization from the same origin but in reverse direction.

Chromosome Mapping↗
PubMed1998

A swarming-defective mutant of Proteus mirabilis lacking a putative cation-transporting membrane P-type ATPase.

The motile TnphoA mutant IC24 of Proteus mirabilis U6450 generates an aberrant swarming colony, and was shown to be impaired in swarm cell differentiation, i.e. cell elongation and hyperflagellation, causing delayed and slower population migration across a solid growth medium. Levels of transcript from the flagellin filament gene fliC, the flagellar master operon flhDC, and the leucine-responsive regulatory protein gene lrp, a regulator of swarming differentiation, were reduced in IC24 mutant swarm cells. The transposon had inserted into a gene encoding a putative P-type ATPase closely related to those transporting cations across bacterial membranes. This ppa gene (Proteus P-type ATPase) was maximally expressed in differentiated swarm cells. The data suggest an effect of ion homeostasis on swarm cell differentiation, possibly mediated via the lrp-flhDC pathway.

Adenosine Triphosphatases↗
PubMed1981

A rapid and simple method for distinguishing colonies of proteus from those of Salmonella and Shigella.

A rapid and simple method is described by which colonies of Proteus can be distinguished from those of Salmonella and Shigella and other non-lactose-fermenting organisms growing on MacConkey's agar or desoxycholate citrate agar. The method is based on the ability of Proteus to produce urease constitutively. The enzyme was detected by the degradation of urea by the inoculum, thereby creating an alkaline reaction on pH-indicator paper.

Bacteriological Techniques↗
PubMed1982

Colonial variants of proteus species: their growth requirements, biochemical characters and resistance to antibacterial agents.

Stable small-colony variants of Proteus species were isolated and characterised. They differed from typical organisms in their morphology, biochemical properties and drug resistance. They were found most frequently in culture media of low osmolarity. Their growth rate was depressed at high concentrations of salts, which had only a small effect on typical organisms. This may be important in the routine isolation of proteus spp. and in testing of disinfectants.

Anti-Bacterial Agents↗
PubMed1982

Haemagglutinins and fimbriae of Morganella, Proteus and Providencia.

One hundred and thirteen strains of Morganella, Proteus and Providencia, grown in different cultural conditions, were examined for their ability to produce haemagglutinins (HAs). Three main kinds of HA (MS, MR/K and MR/P) were detected, and 89% of the 112 HA+ strains were capable of producing two or three of the different HAs in the same or different cultures. The properties of the three HAs were partly defined and the difficulties of identifying their separate HA activities when present together are discussed. Electronmicroscopic examination of bacteria from HA+ cultures showed at least six distinct fimbrial types, the properties of which are described. We tried, with limited success, to correlate the presence of the different HAs with that of the different fimbrial types. The significance of our findings is reviewed in the light of recent taxonomic changes for this group of enterobacteria. The distribution of HAs and fimbriae in the species of Morganella, Proteus and Providencia is more complex than that so far described for other genera of Enterobacteriaceae.

Enterobacteriaceae↗
PubMed1993

The production of HlyA toxin by Proteus penneri strains.

Twelve diverse strains of Proteus penneri of clinical origin all produced a calcium-dependent haemolysin, unlike most other Proteus spp. In most strains the haemolysin was secreted into the medium during early exponential growth and lysed not only of a variety of erythrocyte types from several animals including man, but also human neutrophils and human embryo lung fibroblasts. The haemolysin was a protein of 107 kDa, the same size as Escherichia coli HlyA, and it reacted with antiserum to E. coli HlyA. Because of its similarity in size, antigenicity and range of action to the HlyA virulence factor of E. coli, P. penneri HlyA is believed to be an important virulence factor for this organism. It was degradable by an EDTA-sensitive protease--probably the IgA protease--to inactive fragments. The interaction of P. penneri HlyA and IgA protease in vivo and the origin of HlyA, which has now been found in many diverse bacteria, are discussed.

Amino Acid Sequence↗
PubMed1998

Structural and immunochemical studies of two cross-reactive Proteus mirabilis O-antigens, O6 and O23, containing beta1-->3-linked 2-acetamido-2-deoxy-D-glucopyranose residues.

A marked serological cross-reactivity was observed by ELISA and a precipitation test between anti-Proteus mirabilis O23 serum and the lipopolysaccharide as well as the O-specific polysaccharide from the Proteus mirabilis strain belonging to serogroup O6. The structures of the O-specific polysaccharides were elucidated using chemical and NMR spectroscopic analyses, and the only common component, 2-acetamido-2-deoxy-beta-D-glucopyranose (beta-D-GlcNAc), was revealed, which was suggested to be responsible for the cross-reactivity observed. Both anti-O23 and anti-O6 sera were shown to react with 1, 3-Linked beta-D-GlcNAc-containing O-antigen from Salmonella enterica ssp. arizonae O59 also. The lack of reactivity of Smith-degraded P. mirabilis O6 O-specific polysaccharide with homologous antiserum indicated the crucial role of alpha-D-glucuronic acid in specific antibody binding.

Acetylglucosamine↗
PubMed1995

Unusual distribution of enamel hypoplasia in an 11-year-old child with Proteus syndrome.

An 11-year-old girl with Proteus syndrome attended our dental department because her teeth were sensitive to cold stimuli and because of the poor appearance of her anterior teeth. Extraoral examination revealed several of the previously reported craniofacial features of Proteus syndrome: facial and skull asymmetry, exostoses of the nasal bridge, and mandibular prognathism. Intraoral examination revealed enamel hypoplasia of primary and permanent teeth. The distribution of hypoplasia was unusual in that only teeth on the right side of the mouth were affected, and also in that only the distal half of the crown of the maxillary right permanent central incisor was affected. Behavioural problems necessitated treatment under general anaesthesia; the affected primary teeth were extracted and the hypoplastic permanent teeth were restored, relieving the patient's symptoms and greatly improving aesthetics.

Child↗
PubMed1976

Phospholipid and lipopolysaccharide in Proteus mirabilis and its stable protoplast L-form. Difference in content and fatty acid composition.

Cells of the stable protoplast L-form of Proteus mirabilis contain 1.5 to 2 times more extractable lipid, mostly phospholipid, per dry weight than cells of the bacterial form. Under identical conditions of cultivation the qualitative and quantitiative composition of the phospholipid is very similar in both cell forms. The range of mole percentages of individual phospholipid species is 78-80 for phosphatidylethanolamine, 10-13 for phosphatidylglycerol, 3.9-5.5 for diphosphatidylglycerol and 1.0-2.1 for lysophospholipid. However, all phospholipid species in the L-form differ from those of the bacterial form by a lower content of long-chain fatty acids and a higher content of short-chain fatty acids. Growth of the L-form in the presence of growth-stimulating horse serum results in a change of phospholipid composition accompanied by the uptake of phospholipid and fatty acids from the serum into L-form phospholipid. L-form protoplasts synthesize the same two types of lipopolysaccharide, I and II, that were previously identified in the bacterial form of Proteus mirabilis. However, only small amounts of the more hydrophilic lipopolysaccharide II are present in the L-form. Lipopolysaccharides from both cell forms have virtually identical polysaccharide compositions but differ strikingly in the relative content of fatty acids in their lipid-A moieties. Molar ratios of tetradecanoic acid, hexadeconoic acid and 3-hydroxytetradecanoic acid are 5:1:6 in the bacterial form and 5:0:1:6 in the L-form grown in serum-free medium. The observated differences between the bacterial form and the protoplast L-form are interpreted as results of the adaptation of the L-form to life in the state lacking an envelope by formation of a physically more stable but still sufficiently fluid protoplast membrane. A rapid method based on fatty acid analysis for the simultaneous quantitative determination of phospholipid and lipopolysaccharide content of whole cells is reported.

Cell Division↗
PubMed1977

Ribitol-containing lipopolysaccharides from Proteus mirabilis and their serological relationship.

Ribitol phosphate was recently identified as a constituent of lipopolysaccharides obtained from 'proteus mirabilis strain D52 giving 1:4-anhydroribitol during acid hydrolysis (Gmeiner, 1975). Two other Proteus mirabilis strains belonging to serogroups O16 and O33 were shown previously to contain an unknown compoound X as lipopolysaccharide constituent (Kotelko et al., 1975). In this report the identification of compound X as 1:4-anhydroribotol by gas-liquid chromatography, mass spectrometry and mass fragmentography is described. Serological investigations using passive hemagglutination, hemagglutination inhbition and semi-quantitative precipitin reactions indicate strongly that ribitol plays a role in the serological specificity of the respective lipopolysaccharides.

Hemagglutination Inhibition Tests↗
PubMed1983

Chemical structure of the lipid A component of the lipopolysaccharide from a Proteus mirabilis Re-mutant.

The chemical structure of the lipid A component from the lipopolysaccharide of a Proteus mirabilis Re-mutant (strain R45) was analysed. It consists of a beta(1-6)-linked D-glucosamine disaccharide which carries two phosphate groups, one being ester-linked to position 4' of the nonreducing glucosaminyl residue and the other being bound to the glycosidic hydroxyl group of the reducing glucosaminyl residue. The ester-bound phosphate group is quantitatively substituted by a 4-amino-4-deoxy-L-arabinopyranosyl residue, the glycosidic phosphoryl group appears to be unsubstituted. Two available hydroxyl groups of the disaccharadide (probably at positions 3 and 3') are acylated by approximately 1 mol each of (R)-3-tetradecanoyloxytetradecanoic and (R)-3-hydroxytetradecanoic acid/mol. The amino group of the nonreducing glucosaminyl residue carries (R)-3-tetradecanoyloxytetradecanoic and that of the reducing residue (R)-3-hydroxytetradecanoic acid. In addition smaller amounts of (R)-3-hexadecanoyloxytetradecanoic acid are present in amide linkage. The attachment site of the oligosaccharide portion to lipid A was also investigated. It was found that the hydroxyl group at position 6' of the nonreducing glucosaminyl residue carries 3-deoxy-D-manno-octulosonic acid. This indicates that the saccharide portion in this Proteus lipopolysaccharide is linked to lipid A via the primary hydroxyl group in position 6'.

Amino Sugars↗
PubMed1991

The structure of the O-specific polysaccharide chain of Proteus penneri strain 16 lipopolysaccharide.

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.

Carbohydrate Conformation↗
PubMed1995

The structure and serological specificity of Proteus mirabilis O43 O antigen.

On the basis of sugar analysis and NMR spectroscopy, including selective spin-decoupling, one-dimensional NOE, two-dimensional homonuclear and 13C,1H-heteronuclear correlation spectroscopy, the following structure of the acidic O-specific polysaccharide of Proteus mirabilis O43 was established: -->4)-alpha-D-GalpA-(1-->3)-alpha-D-GalpA-(1-->3)-alpha-D-Gl cpNAc-(1-->4)-alpha - D-Glcp-(1-->, where GalA is galacturonic acid and Galp is galactopyranose. No serological cross-reactivity was observed between lipopolysaccharides of P. mirabilis O43 and other studied Proteus strains, except for P. mirabilis O10. The O-specific polysaccharide of P. mirabilis O43 was serologically active in precipitation and inhibition tests but the activity was lost after periodate oxidation. These data suggest that the O43 specificity is determined by a wide epitope with the immunodominant role of 4-substituted D-Glc or/and D-GalA, which are destroyed by periodate oxidation.

Antibodies, Bacterial↗
PubMed1996

The structure of the O-specific polysaccharide of Proteus penneri 52.

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.

Carbohydrate Conformation↗
PubMed1995

Regional Proteus syndrome: report of an autopsy case.

An uncommon autopsy case involving Proteus syndrome with multiple hamartomatous lesions in a 52 year old woman is reported. At birth, hemihypertrophy was noted on the right side of the face. Leiomyoma of the urinary bladder was extirpated at 37 years of age. She died of sepsis due to a brain abscess. At autopsy, diffuse asymmetrical lipomatosis was noted on the right side of the face, scalp, lip, oral mucosa, tongue and on the left side of the cerebellar peduncle. Multiple meningiomas, cavernous hemangiomas and osseous hypertrophy overlapped in the intracranial regions. The present case is considered as a regional type of Proteus syndrome displaying a somatic mosaicism.

Brain Neoplasms↗