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PubMed1995

Proteus syndrome with renal involvement.

We report on a case of an 11 year old girl with Proteus syndrome involving both kidneys morphologically and functionally. The patient had hemihypertrophy, scoliosis, overgrowth of lower extremities, partial macrodactyly, subcutaneous lipoma, and pigmented nevi compatible with the Proteus syndrome. She also had overgrowth of the right kidney with mildly impaired function and a small left kidney with severe dysfunction. Morphological involvement of visceral organs has previously been described; however, deteriorating renal function has not previously been reported in this syndrome.

Child↗
PubMed1976

The surgical significance of the proteus stone.

62 patients with staghorn calculi who underwent conservative surgery at the Liverpool Regional Urological Centre since 1962 have been reviewed. The evidence shows that stone disease due to proteus is more rapidly progressive than that due to other organisms. Recurrences of proteus stones continue to behave in the same manner. Complete kidney clearance at operation is an essential part of the management of these stones, if renal substance is to be preserved.

Humans↗
PubMed1998

Structure of the O-specific polysaccharide of Proteus penneri strain 41 from a new proposed serogroup O62.

O-specific polysaccharide of Proteus penneri strain 41 was studied using 1H- and 13C-NMR spectroscopy, including two-dimensional COSY, heteronuclear 13C,1H-correlation (HETCOR) and one-dimensional NOE spectroscopy, and the following structure of a non-stoichiometrically O-acetylated hexasaccharide repeating unit was established:[structure: see text] where RGlcNAc is 2-acetamido-4-O-[(S)-1-carboxyethyl]-2-deoxyglucose. Cross-reactivity of anti-P. penneri 41 O-serum with other P. penneri strains is discussed, and a new, separate O62 serogroup is proposed which is the next Proteus O-serogroup containing P. penneri strains only.

Animals↗
PubMed1995

Proteus syndrome: association with gingival hyperplasia.

A 9-year old Black boy with gigantism of the hands and feet, and recurrent gingival hyperplasia, diagnosed as Proteus syndrome is presented. The oral manifestations of this syndrome are described. To the best of our knowledge, this is the first reported case of gingival hyperplasia associated with Proteus syndrome.

Child↗
PubMed1977

Inducible high resistance to colistin in Proteus strains.

Wild-type Proteus strains are usually resistant to colistin. We have observed an increase in the level of colistin resistance in four clinical isolates of P. vulgaris, P. morganii, and P. rettgeri by prior treatment with subinhibitory concentrations of the drug. The enhanced resistance in these strains was lost after cultivating them in colistin-free medium, indicating that the enhanced resistance in the Proteus group is inducible.

Colistin↗
PubMed1987

Comparative in vitro activities of 13 antimicrobial agents against Morganella-Proteus-Providencia group bacteria from urinary tract infections.

We examined 741 urinary tract isolates of the Morganella-Proteus-Providencia group, including the recently defined species Proteus penneri, for susceptibilities to aminoglycosides, semisynthetic penicillins, and cephalosporins. The data emphasize the importance of identification to the species level on the basis of marked species differences in patterns of susceptibility.

Anti-Bacterial Agents↗
PubMed1987

Paradoxical antibacterial activity of cefmenoxime against Proteus vulgaris.

The growth-inhibitory effect of cefmenoxime against Proteus vulgaris was studied by using the broth dilution and paper disk diffusion methods. Cefmenoxime showed growth-inhibitory activity against Proteus vulgaris at low concentrations but not at high concentrations up to a certain limit. This paradoxical antibacterial activity was not observed with cefoperazone and cefbuperazone. The induction of beta-lactamase by cefmenoxime and the rate of hydrolysis of cefmenoxime in the culture broth were proportional to the initial concentration of this antibiotic. At high initial concentrations, cefmenoxime was rapidly inactivated. On the other hand, neither cefoperazone nor cefbuperazone was inactivated irrespective of concentration. We conclude that cefmenoxime induces beta-lactamase in P. vulgaris, perhaps accounting for its paradoxical antibacterial effect.

Cefmenoxime↗
PubMed2002

Postneurosurgical meningitis due to Proteus penneri with selection of a ceftriaxone-resistant isolate: analysis of chromosomal class A beta-lactamase HugA and its LysR-type regulatory protein HugR.

We report on a case of a postneurosurgical meningitis due to ceftriaxone-susceptible Proteus penneri, with selection of a ceftriaxone-resistant isolate following treatment with ceftriaxone. The isolates presented identical patterns by pulsed-field gel electrophoresis and produced a single beta-lactamase named HugA with an isoelectric point of 6.7. The ceftriaxone-resistant isolate hyperproduced the beta-lactamase (increase in the level of production, about 90-fold). The sequences of the hugA beta-lactamase gene and its regulator, hugR, were identical in both P. penneri strains and had 85.96% homology with those of Proteus vulgaris. The HugA beta-lactamase belongs to molecular class A, and the transcriptional regulator HugR belongs to the LysR family.

Adult↗
PubMed2006

CMY-16, a novel acquired AmpC-type beta-lactamase of the CMY/LAT lineage in multifocal monophyletic isolates of Proteus mirabilis from northern Italy.

We report multifocal detection (four different cities in northern Italy) of Proteus mirabilis isolates resistant to both oxyimino- and 7-alpha-methoxy-cephalosporins and producing a novel acquired AmpC-like beta-lactamase. The enzyme, named CMY-16, is a variant of the CMY/LAT lineage, which differs from the closest homologues, CMY-4 and CMY-12, by a single amino acid substitution (A171S or N363S, respectively) and from CMY-2 by two substitutions (A171S and W221R). Expression of the cloned bla(CMY-16) gene in Escherichia coli decreased susceptibility to penicillins, cephalosporins, and aztreonam. Tazobactam was more effective than clavulanate at antagonizing the enzyme activity. Genotyping, by random amplification of polymorphic DNA and pulsed-field gel electrophoresis of genomic DNA digested with SfiI, showed that isolates were clonally related to each other, although not identical. The bla(CMY-16) gene was not transferable to E. coli by conjugation or transformation. In all isolates, it was chromosomally located and inserted in a conserved genetic environment. PCR mapping experiments revealed that the bla(CMY-16) was flanked by ISEcp1 and the blc gene, similar to other genes of this lineage from plasmids of Salmonella enterica, Klebsiella spp., and E. coli. Overall, these results revealed multifocal spreading of a CMY-16-producing P. mirabilis clone in northern Italy. This finding represents the first report of an acquired AmpC-like beta-lactamase in Proteus mirabilis from Italy and underscores the emergence of similar resistance determinants in the European setting.

Bacterial Proteins↗
PubMed1990

New plate medium for facilitated differentiation of Salmonella spp. from Proteus spp. and other enteric bacteria.

A new agar medium for the differentiation of Salmonella spp. from other members of the family Enterobacteriaceae is described. This medium exploits a novel phenotypic characteristic of Salmonella spp.: the formation of acid from propylene glycol. This characteristic may be used in combination with a chromogenic indicator of beta-galactosidase to differentiate Salmonella spp. from Proteus spp. and the other members of the Enterobacteriaceae. Desoxycholate may be included in the plate medium as an inhibitor of gram-positive organisms. Non-typhi Salmonella spp. yield distinct, bright red colonies on this medium, allowing facilitated identification and unambiguous differentiation from Proteus spp.

Animals↗
PubMed1965

Effects of related anionic detergents on flagellation, motility, swarming, and growth of Proteus.

The effects of a series of sodium alkyl sulfates (C(4) to C(16)) on flagellation, motility, swarming, and growth of Proteus were examined. The concentrations of the various sodium alkyl sulfates completely inhibiting the swarming phenomenon (on solid medium) and motility (in liquid medium) were in the same order of magnitude. The inhibiting effect of the detergents examined increased from sodium hexyl sulfate (inhibitory concentration, 20 to 30 mmoles per liter) to sodium tetradecyl sulfate (inhibitory concentration, 0.1 to 0.5 mmoles per liter). Flagella were produced neither in liquid nor on solid medium at these concentrations as could be observed by electron microscopy. At concentrations where motility was not impaired, intact flagellation could be observed. At a concentration of 0.1 mmole per liter, sodium tetradecyl sulfate completely inhibited the motility of Proteus in the liquid medium employed without impairing growth.

Carbon Isotopes↗
PubMed1968

Synergistic antibacterial activity of ampicillin-cloxacillin mixtures against Proteus morganii.

Synergistic antibacterial effects of mixtures of ampicillin and cloxacillin and induced penicillinases were investigated in 48 strains of Proteus. The serial tube dilution method was used to determine the minimal inhibitory concentration of ampicillin, cloxacillin, and 2:1 and 1:1 mixtures of ampicillin and cloxacillin. Production of penicillinases was determined by the cellulose acetate membrane method, with ampicillin, cloxacillin, mixtures of ampicillin and cloxacillin, penicillin G, and cephalothin as inducing agents and as substrates for penicillinase. Synergism occurred against P. morganii, but against no other species. The 1:1 ampicillin-cloxacillin combination was synergistic against 13 of 17 P. morganii strains; the 2:1 combination was synergistic against only 9 strains. Penicillinases, demonstrated in all species except P. mirabilis, hydrolyzed penicillin G and cephalothin. Although only P. vulgaris hydrolyzed ampicillin, no species of Proteus hydrolyzed cloxacillin or the ampicillin-cloxacillin mixtures. Penicillinases were, however, induced by ampicillin, cloxacillin, and the mixtures. There was no relationship between production of penicillinase and synergism with mixtures of ampicillin and cloxacillin.

Ampicillin↗
PubMed1986

Identification and characterization of a uroepithelial cell adhesin from a uropathogenic isolate of Proteus mirabilis.

Proteus mirabilis is a frequent cause of urinary tract infections in rehabilitation hospitals and among persons with structural abnormalities of the urinary tract. Adherence to uroepithelial tissues may be an important virulence determinant in these infections because most Proteus strains adhere to desquamated uroepithelial cells. To identify the adherence factor responsible for this phenomenon, we sheared outer membrane material from 35SO4-radiolabeled bacteria and allowed it to bind to uroepithelial cells. Following sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the major adherence element was a protein with an apparent molecular weight of 17,500 and was provisionally designated as the uroepithelial cell adhesin. This adhesin was purified by heat shock and gel filtration on Sepharose CL-4B. After purification, the adhesin was seen assembled as long, flexible rods by electron microscopy. The N-terminal amino acid sequence of the subunit had limited homology with that of the K99 fimbriae of Escherichia coli.

Amino Acid Sequence↗
PubMed1987

Genetic and biochemical diversity of ureases of Proteus, Providencia, and Morganella species isolated from urinary tract infection.

Bacterial urease, particularly from Proteus mirabilis, has been implicated as a contributing factor in the formation of urinary and kidney stones, obstruction of urinary catheters, and pyelonephritis. Weekly urine specimens (n = 1,135) from 32 patients, residing at two chronic-care facilities, with urinary catheters in place for greater than or equal to 30 days yielded 5,088 phenotypically and serotypically diverse bacterial isolates at greater than or equal to 10(5) CFU/ml. A total of 86% of specimens contained at least one urease-positive species, and 46% of 3,939 gram-negative bacilli were urease positive. For investigation of genetic relatedness of urease determinants, whole-cell DNA from 50 urease-positive isolates each of Providencia stuartii, Providencia rettgeri, P. mirabilis, Proteus vulgaris, and Morganella morganii were hybridized with a urease gene probe derived from within the urease operon of Providencia stuartii BE2467. The percentage of strains hybridizing with the gene probe was 98 for Providencia stuartii, 100 for Providencia rettgeri, 70 for P. mirabilis, 2 for M. morganii, and 0 for P. vulgaris. Electrophoretic mobilities of ureases from representative isolates revealed nine different patterns among the five species. The urease gene probe hybridized with fragments of HindIII-digested chromosomal DNA from all isolates except M. morganii. Fragment sizes differed between species. Molecular sizes of the enzymes, determined by Sephacryl S-300 chromatography, were found to be 280 kilodaltons (kDa) (P. mirabilis), 323 to 337 kDa (Providencia stuartii, Providencia rettgeri, P. mirabilis, P. vulgaris), 620 kDa (providencia rettgeri), and greater than 700 kDa (M. morganii, Providencia rettgeri). Kms ranged from 0.7 mM urea for M. morganii to 60 mM urea for a P. mirabilis isolate. In general, P. mirabilis ureases demonstrated lower affinities for substrate but hydrolyzed urea at rates 6- to 25-fold faster than did enzymes from other species, which may explain the frequent association of this species with stone formation.

Aged↗
PubMed1993

Proteus mirabilis fimbriae: N-terminal amino acid sequence of a major fimbrial subunit and nucleotide sequences of the genes from two strains.

Proteus mirabilis, a common cause of urinary tract infection in hospitalized and catheterized patients, produces mannose-resistant/klebsiella-like (MR/K) and mannose-resistant/proteus-like (MR/P) hemagglutinins. The gene encoding the major structural subunit of a fimbria, possibly MR/K, was identified in two strains. A degenerate oligonucleotide probe based on the N terminus of the Proteus uroepithelial cell adhesin and antiserum raised against the denatured polypeptide were used to screen a cosmid gene bank of strain HU1069. A cosmid clone that reacted with the probe and antiserum was identified, and a fimbria-like open reading frame was determined by nucleotide sequencing. The predicted N-terminal amino acid sequence of the processed polypeptide, ENETPAPKVSSTKGEIQLKG (residues 23 to 42), did not match the uroepithelial cell adhesin N terminus but, rather, matched exactly the N-terminal amino acid sequence of a polypeptide with an apparent molecular size of 19.5 kDa isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of a fimbrial preparation from strain HI4320 expressing MR/K hemagglutinin. By using an oligonucleotide from the HU1069 open reading frame, the fimbrial gene was isolated and sequenced from a cosmid gene bank clone of strain HI4320. A 552-bp open reading frame predicts a 184-amino-acid polypeptide including a 22-amino-acid hydrophobic leader sequence. The unprocessed polypeptide is predicted to be 18,921 Da; the processed polypeptide is predicted to be 16,749 Da. The predicted amino acid sequence of the polypeptide encoded by the gene, designated pmfA, displayed 36% exact matches with the mannose-resistant fimbrial subunit encoded by smfA of Serratia marcescens but only 15% exact matches with the predicted sequence encoded by mrkA of Klebsiella pneumoniae.

Amino Acid Sequence↗
PubMed1994

Effect of lipopolysaccharide (LPS) chain length on interactions of bactericidal/permeability-increasing protein and its bioactive 23-kilodalton NH2-terminal fragment with isolated LPS and intact Proteus mirabilis and Escherichia coli.

The target-specific cytotoxicity for gram-negative bacteria and the endotoxin-neutralizing activity of the 55-kDa bactericidal/Permeability-increasing protein (BPI) and its bioactive 23-kDa NH2-terminal fragment depend on the strong attraction of BPI for the lipid A region of lipopolysaccharides (LPS). We have shown before that smooth gram-negative bacteria with long-chain LPS are more resistant to BPI (especially holo-BPI) than are rough strains. It has been suggested that the high BPI resistance of some gram-negative bacteria, such as Proteus mirabilis, might also reflect the structural diversity of lipid A. To explore this possibility, we compared the antibacterial activity and binding of natural and recombinant holo-BPI and a recombinant NH2-terminal fragment (rBPI-23) to an isogenic rough (Re-LPS chemotype) and a smooth (S-LPS chemotype) strain of P. mirabilis and to LPS isolated from the two strains. Holo-BPI and rBPI-23 were both potently active against the Re strain of P. mirabilis (90% lethal dose, 20 nM). In contrast, the smooth strain was > or = 100 times more resistant to holo-BPI but only 10 times more resistant to rBPI-23. rBPI-23 was also more potent against several Escherichia coli strains from clinical bacteremia isolates. Differences in the antibacterial potency of BPI toward the Re and S strains of P. mirabilis correlated with differences in the binding of holo-BPI and rBPI-23 to these bacteria. In contrast, the binding of biosynthetically (in vitro transcribed and translated) 35S-labeled holo-BPI and NH2-terminal fragment to isolated Re- and S-LPS from P. mirabilis in solution was similar. Moreover, in the Limulus amebocyte lysate assay, holo-BPI and rBPI-23 potently neutralized both forms of LPS with equal effectiveness. Together, these results strongly suggest that BPI recognizes Proteus lipid A and that the relative resistance of (smooth) P. mirabilis to holo-BPI is due to the inhibitory effect of long polysaccharide chains of tightly packed LPS in the envelope.

Antimicrobial Cationic Peptides↗
PubMed1994

Internalization of Proteus mirabilis by human renal epithelial cells.

Proteus mirabilis, a common agent of bacteriuria in humans, causes acute pyelonephritis and bacteremia. Renal epithelium provides a barrier between luminal organisms and the renal interstitium. We have hypothesized that P. mirabilis may be internalized into renal epithelium. To test this hypothesis, we added suspensions of three P. mirabilis strains (10(8) CFU) to confluent monolayers of primary cultures of human renal proximal tubular epithelial cells (HRPTEC) and, after 3 h, found the bacteria internalized within membrane-bound vacuoles by light and electron microscopy. Internalization of bacteria by HRPTEC was corroborated by using the gentamicin protection assay. Cytolysis of HRPTEC by the HpmA hemolysin, however, was a confounding factor in this assay, and therefore a hemolysin-negative hpmA mutant was used in subsequent experiments. The nonhemolytic mutant WPM111 did not disrupt the monolayer and was recovered in numbers that were 10- to 100-fold higher than those of the hemolytic parent BA6163. Cytochalasin D (20 micrograms/ml) inhibited internalization of Salmonella typhimurium but not that of P. mirabilis, suggesting that the latter species enters HRPTEC by a mechanism that is not dependent on actin polymerization. We suggest that HpmA hemolysin-mediated cytotoxicity and internalization of bacteria by HRPTEC may play a role in the development of Proteus pyelonephritis.

Cells, Cultured↗