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PubMed1978

Identification of Proteus morganii and distinction from other Proteus species.

The identification of Proteus morganii in the clinical laboratory is complicated by the differences in incidence of hydrogen sulfide (H2S) production recorded by different sources. Since this quality appeared to be a frequent feature of strains of P. morganii at the author's center, all isolates of this species were studied over a six-month period. During this time, 12 of 21 were found to produce scant H2S in Kligler's iron agar (KIA) and triple-sugar iron (TSI) agar butts. The strains were, in every respect, biotypical, and were easily distinguished from other species of Enterobacteriaceae by biochemical study. They also possessed the features of high resistance to cephalothin and ampicillin and relative sensitivity to tetracycline, unlike strains of Proteus mirabilis. It is concluded that weak H2S production in TSI or KIA medium is a frequent normal characteristic of P. morganii, and its presence should not deter microbiologists from correctly identifying isolates manifesting this quality.

Anti-Bacterial Agents↗
PubMed1999

Requirement of MrpH for mannose-resistant Proteus-like fimbria-mediated hemagglutination by Proteus mirabilis.

Two new genes, mrpH and mrpJ, were identified downstream of mrpG in the mrp gene cluster encoding mannose-resistant Proteus-like (MR/P) fimbriae of uropathogenic Proteus mirabilis. Since the predicted MrpH has 30% amino acid sequence identity to PapG, the Galalpha(1-4)Gal-binding adhesin of Escherichia coli P fimbriae, we hypothesized that mrpH encodes the functional MR/P hemagglutinin. MR/P fimbriae, expressed in E. coli DH5alpha, conferred on bacteria both the ability to cause mannose-resistant hemagglutination and the ability to aggregate to form pellicles on the broth surface. Both a DeltamrpH mutant expressed in E. coli DH5alpha and an isogenic mrpH::aphA mutant of P. mirabilis were unable to produce normal MR/P fimbriae efficiently, suggesting that MrpH was involved in fimbrial assembly. Amino acid residue substitution of the N-terminal cysteine residues (C66S and C128S) of MrpH abolished the receptor-binding activity (hemagglutinating ability) of MrpH but allowed normal fimbrial assembly, supporting the notion that MrpH was the functional MR/P hemagglutinin. Immunogold electron microscopy of P. mirabilis HI4320 revealed that MrpH was located at the tip of MR/P fimbriae, also consistent with its role in receptor binding. The isogenic mrpH::aphA mutant of HI4320 was less able to colonize the urine, bladder, and kidneys in a mouse model of ascending urinary tract infection (P < 0.01), and therefore MR/P fimbriae contribute significantly to bacterial colonization in mice. While there are similarities between P. mirabilis MR/P and E. coli P fimbriae, there are more notable differences: (i) synthesis of the MrpH adhesin is required to initiate fimbrial assembly, (ii) MR/P fimbriae confer an aggregation phenotype, (iii) site-directed mutation of specific residues can abolish receptor binding but allows fimbrial assembly, and (iv) mutation of the adhesin gene abolishes virulence in a mouse model of ascending urinary tract infection.

Adhesins, Bacterial↗
PubMed1984

Unique developmental characteristics of the swarm and short cells of Proteus vulgaris and Proteus mirabilis.

Swarming cells of Proteus mirabilis and Proteus vulgaris could be distinguished from their short-cell counterparts by virtue of their synthesis (or lack of synthesis) of certain enzymes and outer membrane proteins. Urease synthesis was constitutive in swarm cells and uninducible in short cells. In contrast, phenylalanine deaminase was inducible in both short and swarm cells, demonstrating that transcriptional and translational processes were functional. During swarm cell development, the amount of one outer membrane protein (45 kilodaltons) fell and the amounts of two others (50 and 28.3 kilodaltons) rose significantly, the level of cytochrome b decreased, and the synthesis of cytochromes a and d were repressed. Respiratory activities of swarm cells were greatly diminished, suggesting that energy for swarming came from fermentation rather than from respiration. Widespread changes in the pattern of enzyme activities, in cytochrome composition, and in the composition and type of outer membrane proteins suggest that they are due to transcriptional regulation.

Amino Acid Oxidoreductases↗
PubMed1980

Separate O-grouping schemes for serotyping clinical isolates of Proteus vulgaris and Proteus mirabilis.

Antisera were prepared against type strains of the original scheme of B. Perch (Acta Pathol. Microbiol. Scand. 25:703-714, 1948) and against newly defined types to produce separate schemes for O-grouping Proteus vulgaris and Proteus mirabilis. In assessing the schemes for their effectiveness it was found that 82% of 208 P. vulgaris isolates and 88% of 194 P. mirabilis isolates from two hospitals were typable. Only 3.4% of the P. vulgaris isolates agglutinated in P. mirabilis antisera, and 1.5% of the P. mirabilis agglutinated in P. vulgaris antisera, indicating that separation of the schemes would be more advantageous in routine typing. P. mirabilis of groups O3, O6, O10, O29, and O30 were most frequently isolated. Of the P. vulgaris isolates, 25% belonged to newly defined O-groups, and one of these was the largest with 14% of all isolates of this species. The application of serotyping using separate schemes for each species was advocated in epidemiological studies.

Agglutination Tests↗
PubMed2003

Immunochemical studies on the O-antigens of Proteus mirabilis O23 and Proteus vulgaris O23.

Analysis by 1H and 13C nuclear magnetic resonance (NMR) spectroscopy demonstrated that the O-specific polysaccharides of Proteus mirabilis PrK 42/57 and P. vulgaris PrK 43/57 are structurally similar to that of P. vulgaris PrK 44/57 and different from the polysaccharide of P. mirabilis PrK 41/57 studied earlier. The lipopolysaccharides of these strains were tested using enzyme immunosorbent assay, passive hemolysis and Western blot with O-antisera against P. mirabilis 42/57 and P. vulgaris 43/57 and 44/57, as well as with cross-absorbed O-antisera. The chemical and serological data revealed the basis for combining the four strains into Proteus serogroup O23 and division of this serogroup to three subgroups, one for P. vulgaris 43/57 and 44/57 and two others for P. mirabilis 41/57 and 42/57.

Animals↗
PubMed1986

Cell invasiveness of Proteus mirabilis and Proteus vulgaris strains.

Cell penetration ability of haemolytic and non haemolytic Proteus rods was compared. Among four Proteus strains all were able to invade the tested cells (Vero 135, HeLa, L-929 and human blood lymphocytes) but the expression of this feature by haemolytic strains was markedly higher. The survival and multiplication of intracellular bacteria, especially in the case of fresh human blood lymphocytes may be of importance for the development of infection in higher organisms.

Animals↗
PubMed2004

Structure of the O-polysaccharide of Proteus mirabilis CCUG 10701 (OB) classified into a new Proteus serogroup, O74.

An acidic O-polysaccharide was isolated by mild acid degradation of the lipopolysaccharide of Proteus mirabilis CCUG 10701 (OB) and studied by chemical analyses and (1)H and (13)C NMR spectroscopy. The following structure of the tetrasaccharide repeating unit of the polysaccharide was established: --> 3)-beta-D-GlcpNAc6Ac-(1 --> 2)-beta-D-GalpA4Ac-(1--> 3)-alpha-D-GalpNAc-(1 --> 4)-alpha-D-GalpA-(1 -->, where the degree of O-acetylation at position 6 of GlcNAc is approximately 50% and at position 4 of beta-GalA approximately 60%. Based on the unique structure of the O-polysaccharide and serological data, it is proposed to classify P. mirabilis CCUG 10701 (OB) into a new Proteus serogroup, O74.

Acetylation↗
PubMed2005

Structure and serological studies of the O-polysaccharide of Proteus penneri 75 Epitopes and subgroups of Proteus serogroup O73.

The O-specific polysaccharide of the lipopolysaccharide of Proteus penneri strain 75 consists of tetrasaccharide-ribitol phosphate repeating units and resembles ribitol teichoic acids of Gram-positive bacteria. The following structure of the polysaccharide was elucidated by chemical methods and 1H and 13C NMR spectroscopy: [structure in text] where Rib-ol is ribitol. Serological studies with polyclonal antisera showed that the same structure of the O-polysaccharide occurred in two strains: P. penneri 75 and 128. A similar structure has been established earlier for the O-polysaccharide of P. penneri 103 [Drzewiecka, D., et al., Carbohydr. Res. 337 (2002) 1535-1540]. On the basis of complex serological investigations with use of two polyclonal P. penneri 75 and 103 O-antisera, five strains could be classified into Proteus O73 serogroup: P. penneri 48, 75, 90, 103 and 128, two of which (P. penneri 75 and 128) should be subdivided into subgroup 73a, 73b and three others (P. penneri 48, 90 and 103) into subgroup 73a, 73c. Epitopes responsible for the cross-reactivity of P. penneri O73 strains and a related strain of P. mirabilis O20 were tentatively defined.

Animals↗
PubMed2001

Association of germline mutation in the PTEN tumour suppressor gene and Proteus and Proteus-like syndromes.

The molecular aetiology of Proteus syndrome (PS) remains elusive. Germline mutations in PTEN cause Cowden syndrome and Bannayan-Riley-Ruvalcaba syndrome, which are hereditary hamartoma syndromes. Some features-eg, macrocephaly, lipomatosis, and vascular malformations-can be seen in all three syndromes. We examined PTEN in patients with PS and undefined Proteus-like syndromes (PS-like) and identified de-novo germline mutations in two of nine patients with PS and three of five patients with PS-like. Germline PTEN mutation analysis should be done in individuals with PS and PS-like because of its association with increased risk of cancer development and potential of germline-mutation transmission.

Genes, Tumor Suppressor↗
PubMed2002

Structural and serological relatedness of the O-antigens of Proteus penneri 1 and 4 from a novel Proteus serogroup O72.

O-specific polysaccharides (O-antigens) of the lipopolysaccharides (LPS) of Proteus penneri strains 1 and 4 were studied using sugar analysis, (1)H and (13)C NMR spectroscopy, including 2D COSY, H-detected (1)H,(13)C HMQC, and rotating-frame NOE spectroscopy (ROESY). The following structures of the tetrasaccharide (strain 1) and pentasaccharide (strain 4) repeating units of the polysaccharides were established: [reaction: see text]. In the polysaccharide of P. penneri strain 4, glycosylation with the lateral Glc residue (75%) and O-acetylation of the lateral GalNAc residue (55%) are nonstoichiometric. This polysaccharide contains also other, minor O-acetyl groups, whose positions were not determined. The structural similarity of the O-specific polysaccharides was consistent with the close serological relatedness of the LPS, which was demonstrated by immunochemical studies with O-antisera against P. penneri 1 and 4. Based on these data, it was proposed to classify P. penneri strains 1 and 4 into a new Proteus serogroup, O72, as two subgroups, O72a and O72a,b, respectively. Serological cross-reactivity of P. penneri 1 O-antiserum with the LPS of P. penneri 40 and 41 was substantiated by the presence of an epitope(s) on the LPS core region shared by all P. penneri strains studied.

Animals↗
PubMed1998

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.

Acetylglucosamine↗
PubMed1980

Purification and some properties of beta-lactamases from Proteus rettgeri and Proteus inconstans.

Two beta-lactamases were isolated from strains of Proteus species and purified, one from a strain of P. rettgeri and the other from a strain of P. inconstans. Each enzyme preparation gave a single protein band on polyacrylamide gel electrophoresis. Molecular weights of P. rettgeri and P. inconstans enzymes were found to be 42,000 and 43,000, and their isoelectric points pH 8.7 and 8.6, respectively. The two enzymes presented typical cephalosporinase profiles. Cefmetazole (CS-1170) and cefoxitin, both cephamycin antibiotics, not only resisted hydrolysis by both of the enzymes, but also inhibited their activities competitively. Rabbit antiserum against purified P. rettgeri enzyme inhibited the activity of both purified and crude enzyme preparations from other strains of P. rettgeri so far tested. None of the beta-lactamases produced by other species of Proteus including P. inconstans was inhibited by the antiserum, thus showing that the purified cephalosporinase was of the species-specific types. The enzymological properties of the preparations were compared with those of beta-lactamases derived from other gram-negative enteric bacteria.

Amino Acids↗
PubMed1997

Proteus mirabilis mannose-resistant, Proteus-like fimbriae: MrpG is located at the fimbrial tip and is required for fimbrial assembly.

The mannose-resistant, Proteus-like (MR/P) fimbria, responsible for mannose-resistant hemagglutination, is a virulence factor for uropathogenic Proteus mirabilis. Based on known fimbrial gene organization, we postulated that MrpG, a putative minor subunit of the MR/P fimbria, functions as an adhesin responsible for hemagglutination, while MrpA serves as the major structural subunit for the filamentous structure. To test this hypothesis, an mrpG mutant was constructed by allelic-exchange mutagenesis and verified by PCR and Southern blotting. The mrpG mutant was found to be negative for hemagglutination, while wild-type strain H14320 and the complemented mutant were positive. Western blots with antiserum raised against an overexpressed MrpG'-His6 fusion protein showed that MrpG was present in the fimbrial preparations of both the wild-type strain and the complemented mutant but absent in that of the mrpG mutant. The mrpG mutant was significantly less virulent in a CBA mouse model of ascending urinary tract infection. Western blots with antiserum to whole MR/P fimbriae showed that MrpA protein was also missing from the fimbrial preparation of the mrpG mutant. Using immunogold electron microscopy, we found that the normal MR/P-fimbrial structure was absent in the mrpG mutant, suggesting that MrpG is essential for initiation of normal fimbrial formation. In the wild-type strain, MrpG protein was localized to the tips of the fimbriae or at the surface of the cell when antiserum raised against overexpressed MrpG was used. Given the tip localization, MrpG may be required for initiation of assembly of MR/P fimbriae but does not appear to be the fimbrial adhesin.

Adhesins, Bacterial↗
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↗
PubMed1983

Some biological features of Proteus bacilli. 1. Comparison of Proteus mirabilis strains provided from various sources.

Some properties which may contribute to the pathogenicity of Proteus mirabilis were compared in urinary isolates and in strains provided from soil and from culture collection. Clinical isolates revealed the higher expression of all the features examined in this report: swarming growth, haemagglutination, adherence to human uroepithelial cells, urease activity and haemolytic activity. Noteworthy is the higher mean value of adherence to the uroepithelial cells in clinical strains. Three P. mirabilis urinary isolates were detected which produce an as yet unreported filterable haemolysin. However, the loss of this ability within a few months seems to suggest the temporary presence of a plasmid rapidly eliminated by the Proteus strains.

Adhesiveness↗
PubMed1994

A new phage typing scheme for Proteus mirabilis and Proteus vulgaris strains. 1. Morphological analysis.

A new bacteriophage typing set, composed of 22 phages, was established as a tool for differentiation of Proteus strains. All the phages were tailed and included 4 morphological types (A1, A2, B1 and C1). They were classified into the families Myoviridae, Siphoviridae and Podoviridae. From the set, 19 phages had double-stranded DNA and 3 were single-stranded DNA phages.

Bacteriophage Typing↗
PubMed2001

The structure of the carbohydrate backbone of the core-lipid A region of the lipopolysaccharide from Proteus penneri strain 40: new Proteus strains containing open-chain acetal-linked N-acetylgalactosamine in the core part of the LPS.

Analysis of the core part of the LPS from several strains of Proteus revealed that P. penneri strains 2, 11, 19, 107, and P. vulgaris serotypes 04 and 08 have the same structure with a new type of linkage between monosaccharidesan open-chain acetal--that was previously determined for P. vulgaris OX2 and P. penneri 17. The LPS from P. penneri strain 40 contains the same structure substituted with one additional monosaccharide: [molecular structure: see text] where (1S)-GalaNAc1 is a residue of N-acetyl-D-galactosamine in the open-chain form. It is connected as a cyclic acetal to positions 4 and 6 of the galactosamine residue having a free amino group. All other sugars are in the pyranose form.

Acetals↗