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PubMed1993

[Studies of epitope specificity of polyclonal antibodies against Proteus mirabilis R mutants].

The chemical structure of the following P. mirabilis R mutants lipopolysaccharide (LPS) were already established: R110/1959 (Ra), R4/028 (Rc) and R45/1959 (Re). In this report we focus on P. mirabilis R5/O28, R13/1959 and R14/1959 and R14/1959. The last one corresponds to Salmonella transient forms, and synthesis truncated core oligosaccharide lacking terminal DD-Hep and nevertheless substituted by T polysaccharide whose structure occurred to be similar to P. penneri 42 O-repeating unit. The knowledge of chemical structure of P. mirabilis R mutants lipopolysaccharides led us to the study of the epitope specificity of rabbit polyclonal R specific antisera. The results show strong structural and serological relatedness of LPS from P. mirabilis R110 and R13. Antibodies against P. mirabilis R4 recognize in homologous LPS an epitope sharing oligosaccharide Glc-Hep. The serological studies revealed also close similarities of LPS from P. mirabilis R14 and P. mirabilis S1959, O28 as well as P. penneri 42. These data indicate that polyclonal antibodies against P. mirabilis R14 are directed against four epitopes: two in T-polysaccharide (D-Glc-(beta 1,4)-D-Glc and terminal GalA residue) and two in core oligosaccharide (D-Glc-(alfa 1,6)-D-Glc and terminal GlcNAc residue) of lipopolysaccharide molecule.

Animals↗
PubMed1999

Amplification of Proteus mirabilis chromosomal DNA using the polymerase chain reaction.

A Proteus mirabilis-specific polymerase chain reaction (PCR) was developed and standardized. The origin of the primers was a recombinant clone that contained P. mirabilis-specific Hind III fragment DNA of 3.5-kilobase pairs. Based on the sequence data of P. mirabilis recombinant clone, two primers designated MMKAP 1 and MMKAP 2 were synthesized for use in the PCR. A P. mirabilis-specific 3.5-kb pair DNA product was amplified by the primers from 18 strains of P. mirabilis, but not from other Protease species and bacteria. The minimum amount of target DNA detected by P. mirabilis PCR was 10 fg using ethidium bromide/ultraviolet exposure of gels or Southern blot hybridization with a P. mirabilis recombinant DNA probe.

Bacteria↗
PubMed2004

Mucosal vaccination of mice with recombinant Proteus mirabilis structural fimbrial proteins.

Proteus mirabilis, a common cause of urinary tract infection (UTI), expresses several types of fimbria including mannose-resistant/Proteus-like fimbriae (MRP), uroepithelial cell adhesin (UCA), renamed non-agglutinating fimbriae (NAF) by some authors, and P. mirabilis fimbriae (PMF), which are potentially involved in adhesion to the uroepithelium. In this study, we immunised different groups of mice with recombinant structural subunits of these fimbriae (MrpA, UcaA and PmfA) using two mucosal routes (nasal and transurethral) and we transurethrally challenged the animals with a P. mirabilis uropathogenic isolate. Induction of specific serum and urine IgG and IgA was measured to assess the potential role of the humoral immune response in protection against experimental ascending P. mirabilis UTI. Intranasally MrpA- and UcaA-immunised mice were protected against P. mirabilis ascending UTI, since recovery of bacteria from kidneys and bladders was significantly lower than in PBS-treated mice, and both fimbrial subunits significantly induced specific serum and urine antibodies. Only MrpA and PmfA transurethrally immunised animals were protected only at the kidney level, and in this case only MrpA-immunised mice exhibited significant serum IgG induction. Correlation analysis did not show a significant relationship between serum and urine specific antibody response and protection observed against infection. Our results suggest that an immunisation strategy based on structural fimbrial proteins may be useful to prevent P. mirabilis UTI. Further studies are being carried out to characterise the immune and inflammatory response induced by P. mirabilis recombinant fimbrial subunits.

Administration, Intranasal↗
PubMed1987

Adherence of Escherichia coli and Proteus mirabilis to human transitional cells.

This study utilizes a light microscopy assay for bacterial adherence to human male transitional cells. Prior light microscopy studies have used voided squamous cells, periurethral cells or scraped vaginal cells, which are less representative of the cells lining the majority of the urinary tract. Using a modification of previous bacterial adherence assays, the mean adherence for 28 strains of E. coli in 92 bacteria-cell incubations was 10.2 +/- 11.5 (standard deviation) bacteria per cell. The mean adherence for 20 strains of P. mirabilis in 60 bacteria cell incubations was 8.1 +/- 11.4. No statistically significant difference in adherence between E. coli and P. mirabilis was found (p greater than 0.05). Studies comparing the adherence of E. coli isolated from the urine of patients with pyelonephritis (eight strains), cystitis (10 strains) and anal swabs of females without urinary tract infections (10 strains), showed no statistically significant differences in mean adherence (p greater than 0.05). However, there was a trend toward higher adherence in the more virulent groups. Experiments comparing the adherence of P. mirabilis isolated from infected renal stones to P. mirabilis isolated from anal swabs of female patients without history of P. mirabilis UTI revealed no statistically significant differences in mean adherence between the two groups (p greater than 0.05). These data do not support previous contentions that P. mirabilis adhere poorly to human transitional cells. The absence of a significant difference in adherence among strains of E. coli and P. mirabilis that differ in clinical pathogenicity suggests that factors other than adherence contribute to their virulence.

Bacterial Adhesion↗
PubMed2002

Frequent association with neurosurgical conditions in adult Proteus mirabilis meningitis: report of five cases.

Adult Proteus (P.) mirabilis meningitis is relatively rare and has not been examined individually in the English-language literature. During a period of 15 years (January 1986-December 2000), four adult patients with P. mirabilis meningitis and one adult patient with mixed bacterial meningitis involving P. mirabilis were identified at Chang Gung Memorial Hospital, Kaohsiung. These five patients included one man and four women, aged from 19 to 74 years (mean age=55.4). P. mirabilis infection accounted for 1.7% (4/229) of cases of our culture-proven monomicrobial adult bacterial meningitis and was involved in 7.1% (1/14) of cases of our adult mixed bacterial meningitis during this period. Underlying debilitating conditions including diabetes mellitus and neurosurgical disorders were common in these five cases. Adult P. mirabilis meningitis had an acute clinical course, with fever and consciousness-disturbance occurring as most prominent clinical manifestations in all patients. Other common manifestations included hydrocephalus, seizure, septic shock and wound infection. Hematogenous spread would appear to be the most likely mechanism. Multi-antibiotic resistant strains of P. mirabilis were not found in our patients. All strains were susceptible to third-generation cephalosporins, imipenem, aztreonam and ciprofloxacin. The results of treatment for adult P. mirabilis meningitis were not satisfactory, most of the patients surviving with severe neurological deficit.

Adult↗
PubMed2001

Structure of the O-specific polysaccharide of Proteus mirabilis D52 and typing of this strain to Proteus serogroup O33.

The acidic O-specific polysaccharide chain (O-antigen) of the lipopolysaccharide (LPS) of Proteus mirabilis strain D52 was studied using chemical analyses along with 1H-NMR and 13C-NMR spectroscopy, including 2D COSY, TOCSY, ROESY, H-detected 1H,13C and 1H,31P HMQC experiments. The polysaccharide was found to contain D-ribitol 5-phosphate (D-Rib-ol-5-P) and ethanolamine phosphate (Etn-P) and has the following structure: D-Rib-ol-5-P (3) approximately 75% EtnP(6)-->2)-beta-D-Galp-(1-->3)-alpha-D-GlcpNAc-(1-->3)-beta-D-Glcp-(1-->3)-beta-D-GlcpNAc-(1-->). This structure is identical with that of the O-polysaccharide of P. mirabilis O33 strain 59/57, and, hence, P. mirabilis D52 belongs to the same Proteus serogroup O33. Serological studies with O-antiserum against P. mirabilis D52 confirmed this but showed that the LPS species of P. mirabilis 59/57 and D52 are not identical, having different epitopes in the core region. A serological cross-reactivity of P. mirabilis D52 O-antiserum was observed with LPS of two other Proteus strains, P. mirabilis O16 and P. penneri 103, which have structurally different O-polysaccharides. The role of charged groups, Rib-ol-5-P and Etn-P in the immunospecificity is discussed.

Animals↗
PubMed2005

Elevated levels of IgM and IgA antibodies to Proteus mirabilis and IgM antibodies to Escherichia coli are associated with early rheumatoid factor (RF)-positive rheumatoid arthritis.

OBJECTIVE: Antibodies to Proteus mirabilis were previously detected in patients with established rheumatoid arthritis (RA). We examined the prevalence of antibodies to P. mirabilis and their associations with RA in early synovitis patients. METHODS: Two hundred and forty-six patients with inflammatory arthritis for less than 1 yr were prospectively evaluated for 1 yr. Of these patients, 30% had rheumatoid factor (RF)-positive RA, 16% RF-negative RA, 17% a spondyloarthropathy and 37% undifferentiated arthritis. Serum antibodies to P. mirabilis, Escherichia coli and other potentially arthritogenic organisms (Chlamydia, Salmonella, Shigella, Campylobacter, Yersinia and parvovirus B19) and for antibodies specific for immunoglobulin (Ig) G damaged with advanced glycation end-products (anti-IgG-AGE) were measured. RESULTS: IgM and IgA anti-Proteus antibodies were significantly higher in patients with RF-positive RA compared with all other patient groups (P < 0.0005 and P < 0.005). Anti-P. mirabilis IgG, and IgG, IgA, and IgM antibodies to other potentially arthritogenic pathogens did not differ in the patient groups. IgM antibodies to E. coli were elevated in RF-positive RA patients. Anti-P. mirabilis IgM and IgA results were not explained by false-positive reactions, because after absorption of RF there was no decrease in antibodies to Proteus in 10 of 12 patients. Proteus and E. coli antibodies were highest in patients positive for both RF and anti-IgG-AGE antibodies (P<0.001). Patients with erosions tended to have higher IgA anti-Proteus titres, but no association with the shared HLA epitope or treatment was detected. CONCLUSION: Anti-P. mirabilis IgM and IgA and anti-E. coli IgM antibody elevations are associated with early seropositive RA and the presence of anti-IgG-AGE antibodies. The role that P. mirabilis or E. coli plays in early RF-positive RA requires further investigation.

Adult↗
PubMed2004

Mannose-resistant Proteus-like fimbriae are produced by most Proteus mirabilis strains infecting the urinary tract, dictate the in vivo localization of bacteria, and contribute to biofilm formation.

Proteus mirabilis, an etiologic agent of complicated urinary tract infections, expresses mannose-resistant Proteus-like (MR/P) fimbriae whose expression is phase variable. Here we examine the role of these fimbriae in biofilm formation and colonization of the urinary tract. The majority of wild-type P. mirabilis cells in transurethrally infected mice produced MR/P fimbriae. Mutants that were phase-locked for either constitutive expression (MR/P ON) or the inability to express MR/P fimbriae (MR/P OFF) were phenotypically distinct and swarmed at different rates. The number of P. mirabilis cells adhering to bladder tissue did not appear to be affected by MR/P fimbriation. However, the pattern of adherence to the bladder surface was strikingly different. MR/P OFF colonized the lamina propria underlying exfoliated uroepithelium, while MR/P ON colonized the luminal surfaces of bladder umbrella cells and not the exfoliated regions. Wild-type P. mirabilis was usually found colonizing intact uroepithelium, but it occasionally adhered to exfoliated areas. MR/P ON formed significantly more biofilm than either P. mirabilis HI4320 (P = 0.03) or MR/P OFF (P = 0.05). MR/P OFF was able to form a biofilm similar to that of the wild type. MR/P ON formed a three-dimensional biofilm structure as early as 18 h after the initiation of the biofilm, while MR/P OFF and the wild type did not. After 7 days, however, P. mirabilis HI4320 formed a 65-mum-thick biofilm, while the thickest MR/P ON and MR/P OFF biofilms were only 12 mum thick. We concluded that MR/P fimbriae are expressed by most P. mirabilis cells infecting the urinary tract, dictate the localization of bacteria in the bladder, and contribute to biofilm formation.

Animals↗
PubMed2003

Natural antibiotic susceptibility of Proteus spp., with special reference to P. mirabilis and P. penneri strains.

The natural susceptibility of 102 Proteus mirabilis and 35 Proteus penneri strains to 71 antibiotics was examined. Minimum inhibitory concentrations (MICs) were determined by applying a microdilution procedure in IsoSensitest broth (for all strains) and cation-adjusted Mueller Hinton broth (for some strains). P. mirabilis and P. penneri were naturally resistant to penicillin G, oxacillin, all tested macrolides, lincosamides, streptogramins, glycopeptides, rifampicin and fusidic acid. Both species were uniformly, naturally sensitive to all tested aminoglycosides, acylureidopenicillins, some cephalosporins, carbapenems, aztreonam, quinolones, sulfamethoxazole and co-trimoxazole. Species-specific differences in natural susceptibility affecting clinical assessment criteria were seen with tetracyclines, several beta-lactams, chloramphenicol and nitrufurantoin. P. mirabilis was naturally resistant to all tested tetracyclines, and was naturally sensitive to all beta-lactams, except penicillin G and oxacillin. Strains of P. penneri were naturally sensitive or of intermediate susceptibility to tetracyclines, and naturally resistant to amoxicillin (but sensitive or of intermediate susceptibility to aminopenicillins in the presence of beta-lactamase inhibitors) and some cephalosporins (i.e. cefaclor, cefazoline, loracarbef, cefuroxime, cefotiam, and cefdinir). P. penneri was less susceptible than P. mirabilis to chloramphenicol; P. mirabilis was less susceptible than P. penneri to nitrofurantoin. Major medium-dependent influences on the MICs were seen with fosfomycin. The present study describes a database concerning the natural antibiotic susceptibility of P. mirabilis and P. penneri strains to a range of antibiotics, which can be applied to validate forthcoming antibiotic susceptibility tests of these bacteria. It was shown that ten of fifteen amoxicillin-sensitive P. mirabilis strains produced beta-lactamases at a low level, supporting the thesis of the presence of a naturally-occurring beta-lactamase in this species. Natural susceptibility patterns are compared with those of a recent study, dealing with natural susceptibilities of species of the P. vulgaris complex.

Anti-Bacterial Agents↗
PubMed1979

Conduit urinary diversion and urinary-tract infection. II. Raised serum antibody titers against Escherichia coli and Proteus mirabilis in relation to bacteriologic findings.

Elevated serum antibody titers against Escherichia coli and/or Proteus mirabilis were found in 35% of 89 patients with a conduit urinary diversion. Statistical analysis showed significant correlation between the titers and growth of E. coli or P. mirabilis in conduit urine. But 17 (24%) of 72 patients without E. coli in urine cultures had raised E. coli antibody titer. Only 3 (4%) of 68 patients without growth of P. mirabilis had raised P. mirabilis antibody titer. When the post-diversion observation period was more than five years, the frequency of antibody titer elevation was greater than in patients with shorter post-diversion follow-up. The volume of residual urine in the conduit showed statistically significant correlation with presence of bacteriuria and with the antibody titer level against P. mirabilis. Patients with high antibody titers tended to have high readings of serum creatinine. Antibiotic therapy reduced elevated E. coli and P. mirabilis antibody titers. Titration of antibodies to E. coli and P. mirabilis is recommended in the follow-up care of patients with conduit urinary diversion.

Adolescent↗
PubMed1999

Use of polymerase chain reaction to detect Proteus mirabilis and Ureaplasma urealyticum in urinary calculi.

In this study, we evaluated the efficacy of the polymerase chain reaction (PCR) in detecting urea-splitting microorganisms in desiccated urinary tract infection stones. Seventy-eight urinary tract stones were tested for the presence of Proteus mirabilis and Ureaplasma urealyticum by means of PCR with species-specific primers. Twenty-seven stone samples were composed of struvite and/or carbonate apatite (infection stone); 40 were calcium oxalate and/or calcium phosphate; seven were mixed, with struvite/carbonate apatite and calcium oxalate; and four were uric acid stones. PCR was performed with DNA extracted from pulverized stone pieces. Initial assays using the pulverized stone specimens spiked with microorganisms showed that PCR could not detect U. urealyticum at densities below 10(3) color changing units (CCU), or P. mirabilis at densities below 10(4) colony-forming units (CFU). PCR was negative for U. urealyticum and P. mirabilis in all metabolic stones from patients. P. mirabilis was detected by PCR in 10 of 34 patients with infection stones. Preoperative urine cultures grew P. mirabilis in three of these 10 patients, and were negative for P. mirabilis in the other seven. U. urealyticum was detected by PCR in stone samples from four patients, two of which were also PCR-positive for P. mirabilis. All four of these patients had infection stones: two had residual stones, and the other two had recurrence of urinary stones after their operations. These results demonstrate that microorganisms in urinary stones can be detected by PCR even when the voided urine culture is negative. Investigations into the role of bacterial infection in stone formation will require further improvements in the sensitivity of PCR assays for pathogen detection.

Adult↗
PubMed2000

The binding of Proteus mirabilis nonagglutinating fimbriae to ganglio-series asialoglycolipids and lactosyl ceramide.

Proteus mirabilis is a common opportunistic Gram-negative uropathogen that infects the upper urinary tract. We have examined the role of the nonagglutinating fimbriae (NAF) of P. mirabilis in mediating bacterial adhesion to cell surface receptors. Purified NAF of P. mirabilis were demonstrated to bind to a number of glycolipids, including asialo-GM1, asialo-GM2, and lactosyl ceramide (LacCer) in solid-phase binding assays and in thin layer chromatography (TLC) overlay assays. Furthermore, preincubation of the biotinylated NAF (Bt-NAF) with anti-NAF monoclonal antibodies resulted in inhibition of NAF binding to immobilized asialo-GM1, asialo-GM2, and LacCer. In adherence assays, P. mirabilis binding to Madin-Darby canine kidney (MDCK) cells was inhibited by murine anti-asialo-GM1 monoclonal antibodies H2G10 to about 50% of the binding level in the absence of the antibody, specific for the terminal beta-galactopyranosyl residue of asialo-GM1 (Harrison et al. 1998). The results of this study suggest that NAF of P. mirabilis recognize a GalNAc beta 1-4Gal moiety present in the ganglio-series of asialoglycolipids, and that the terminal beta-galactopyranosyl-containing glycoconjugates play a role in NAF-mediated adherence of P. mirabilis to MDCK cells. Similarly to other bacteria, P. mirabilis NAF was also shown to express the LacCer specificity.

Agglutination↗
PubMed1977

[Transmission of the R-plasmids and expression of their genes in Proteus mirabilis].

Resistance markers to individual antibiotics are transmitted in E. coli with the same frequency in the shape of a uniform linkage group, and in Proteus mirabilis--with a different one. Possibly in Proteus mirabilis plasmide R6 dissociated, this being expressed in a different incidence of transconjugates, characterized by a different set of antibiotic resistance genes. Tetracyclin resistance gene can be transmitted in P. mirabilis without being bound with other resistance determinants and with the functioning Tra-operon. The expression of individual antibiotic resistance genes of plasmide R6 in P. mirabilis differed, i.e. tetracycline resistance was inducible, and to kanamycin and chloramphenicol--constitutional. The level of expression of the gene controlling the tetracycline resistance was in noninduced condition in P. mirabilis, lower than in E. coli, P. mirabilis containing no R-factor possessed an inducible resistance mechanism to tetracycline, as in case of P. mirabilis strains containing R-factors.

Anti-Bacterial Agents↗
PubMed1997

Evaluation of clonal relatedness of extended-spectrum beta-lactamase-producing Proteus mirabilis isolates by quantitative antibiogram and RAPD typing.

OBJECTIVE: To delineate, using two different typing systems, the clonal relatedness of 40 isolates of extended-spectrum beta-lactamase (ESbetaIa)-producing Proteus mirabilis obtained over a period of 7 years in six hospitals in the Paris area and two in Pas-de-Calais. METHODS: Random amplified polymorphic DNA (RAPD) polymerase chain reaction typing was applied by using three random primers on the ESbetaIa-producing P. mirabilis isolates and on isogenic Escherichia coli strains with or without plasmids encoding the representative resistance pattern transferred from P. mirabilis. Quantitative antibiogram typing, which was also applied to the P. mirabilis isolates, was used to define the euclidean distance between these strains. RESULTS: After having demonstrated that P. mirabilis plasmids did not influence chromosomal DNA amplification, we could classify the ESbetaIa-producing P. mirabilis isolates into 12 groups based on RAPD fingerprints. The same isolates were classified into 19 groups by quantitative antibiogram typing. Despite this difference in group numbers, general concordance between the typing systems was observed. This allowed us to show that the greater number of isolates in some hospitals belonged to a single strain and that single isolates obtained in different hospitals generally represented unique strains. CONCLUSIONS: A small number of ESbetaIa-producing P. mirabilis strains was isolated during 7 years in the eight medical centers studied, and the number of different strains identified suggested that inter-hospital transfer had not occurred.

Journal Article↗
PubMed2006

Classification of Proteus mirabilis TG 115 and CCUG 10701 into the Proteus O23 serogroup based on chemical and serological studies of O-polysaccharides.

INTRODUCTION: Bacteria of the genus Proteus are a common cause of urinary tract infections. The O-polysaccharide (OPS) chain of their lipopolysaccharide (LPS) defines the serological specificity of strains. Based on the OPS structures and the immunospecificity of the LPS, Proteus strains have been classified into 74 O-serogroups. MATERIALS AND METHODS: The OPS of P. mirabilis TG 115 was obtained by mild acid degradation of the LPS and studied by (1)H and (13)C nuclear magnetic resonance spectroscopy. Antisera were raised by immunization of rabbits with heat-killed bacteria. Serological studies were performed using enzyme immunosorbent assay, passive immunoheamolysis, inhibition experiments, absorption of O-antisera, and Western blot. RESULTS: The following structure of the P. mirabilis TG 115 OPS was established: --> 2)-beta-D-GalpA-(1--> 3)-alpha-D-GalpNAc-(1--> 4)-alpha-D-GalpA-(1--> 3)-beta-D-GlcpNAc-(1--> The same structure has been reported previously for the O-polysaccharides of P. mirabilis CCUG 10701 (O74) and P. mirabilis 41/57 (O23), except that they contain O-acetyl groups in non-stoichiometric quantities. Serological studies showed the antigenic identity of the three strains and their close serological relatedness to P. vulgaris 44/57. CONCLUSIONS: Based on the OPS structures and serological data, it is suggested to classify P. mirabilis 41/57, TG 115, and CCUG 10701 into one subgroup and P. mirabilis 42/57 and P. vulgaris 43/57 and 44/57 into another subgroup of the Proteus O23 serogroup.

Carbohydrate Sequence↗
PubMed1998

Antibiotic sensitivity and proticine typing of Proteus mirabilis strains associated with rheumatoid arthritis.

Urinary isolates of Proteus mirabilis, obtained from 49 RA patients and 44 healthy controls, were tested for susceptibility to antibiotics by the disc diffusion method. In addition, P. mirabilis isolates were also tested for proticine production and sensitivity (p/s) typing by the inhibition of growth of each test isolate against 13 reference strains of P. mirabilis. The P. mirabilis isolates from both RA patients and healthy controls were highly susceptible to norfloxacin, ciprofloxacin and trimethoprim, but less to minocycline. The urine of RA patients contained fewer different types of P. mirabilis strains than those isolated from healthy controls. All of the strains found in the RA patients were proticine producers (P < 0.001), mostly of proticine 3 (P < 0.005). The presence of such strains provides evidence of a sub-clinical upper urinary tract infection with P. mirabilis in some RA patients. Therapeutic intervention in RA with relevant antibiotics requires evaluation.

Adult↗
PubMed2001

Properties of multidrug-resistant, ESBL-producing Proteus mirabilis isolates and possible role of beta-lactam/beta-lactamase inhibitor combinations.

At our institution, isolation rates of clinical strains of ESBL-producing Proteus mirabilis increased to 8.8% of all P. mirabilis isolates during the period 1997-1999. To evaluate the susceptibility of ESBL-producing P. mirabilis strains against commonly used drugs, we studied 50 non-duplicated isolates selected on the basis of synergy between clavulanate and beta-lactams (ceftazidime, aztreonam, cefotaxime, and ceftriaxone). The presence of ESBL-coding genes was confirmed by colony hybridization with bla(TEM-1) and bla(SHV-1) probes. Minimum inhibitory concentrations of several antimicrobial agents for each isolate were obtained using the Etest method. All strains were encoding for TEM-derived enzymes. Gene sequencing showed that at least three different genes (TEM-15, TEM-20, and TEM-52) were present. These enzymes have not been previously reported in P. mirabilis. Isolates were characterized by: (a) reduced susceptibility or resistance to third- and fourth-generation cephalosporins (MIC > or = 2 mg/l), (b) resistance to piperacillin that was abolished by tazobactam (MIC > or = 256 vs. < or = 2 mg/l, respectively), (c) multiple antibiotic resistance that included gentamicin, fluoroquinolones and co-trimoxazole. Therapeutic failure and lack of eradication of ESBL-positive P. mirabilis by third-generation cephalosporins has been repeatedly observed both at our Institution and elsewhere. Piperacillin-tazobactam, as well as amikacin and meropenem appear to be important therapeutic options for infections due to multidrug-resistant, ESBL-producing P. mirabilis isolates.

Anti-Bacterial Agents↗
PubMed2003

Evaluation of Proteus mirabilis structural fimbrial proteins as antigens against urinary tract infections.

Proteus mirabilis is a common cause of urinary tract infection (UTI) and produce several types of different fimbriae, including mannose-resistant/Proteus-like fimbriae, uroepithelial cell adhesin (UCA), and P. mirabilis fimbriae (PMF). Different authors have related these fimbriae with different aspects of P. mirabilis pathogenesis, although the precise role of fimbriae in UTI has not yet been elucidated. In this work we expressed and purified recombinant structural fimbrial proteins of these fimbriae (MrpA, UcaA, and PmfA) and assessed their role as protective antigens using an ascending and a haematogenous model of UTI in the mouse. MrpA protected subcutaneously immunised mice in both models, suggesting that it could be taken into account as a promising vaccine candidate against P. mirabilis UTI. UcaA could also be an interesting subunit to be studied although it only protected mice that were challenged intravenously. All subunits elicited a strong specific serum IgG response but there was no significant correlation between antibody levels and protection. Only PmfA-immunised mice elicited a significant urinary antibody response but this protein was unable to confer protection against P. mirabilis experimental challenges. These results may contribute to the development of vaccines against P. mirabilis, an important cause of complicated UTI.

Animals↗