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At least 19 recordsLinked to original sources
PubMed2000

Classification of Proteus vulgaris biogroup 3 with recognition of Proteus hauseri sp. nov., nom. rev. and unnamed Proteus genomospecies 4, 5 and 6.

Strains traditionally identified as Proteus vulgaris formed three biogroups. Biogroup 1, characterized by negative reactions for indole production, salicin fermentation and aesculin hydrolysis, is now known as Proteus penneri. Biogroup 2, characterized by positive reactions for indole, salicin and aesculin, was shown by DNA hybridization (hydroxyapatite method) to be a genetic species separate from biogroup 1 and from biogroup 3 which is positive for indole production and negative for salicin and aesculin. In this study, 52 strains were examined, of which 36 strains were Proteus vulgaris biogroup 3, which included the current type strain of the species P. vulgaris (ATCC 29905T), and compared to seven strains of Proteus vulgaris biogroup 2 and nine type strains of other species in the genera Proteus, Providencia and Morganella. By DNA hybridization, these 36 strains were separated into four distinct groups, designated as Proteus genomospecies 3, 4, 5 and 6. DNAs within each separate Proteus genomospecies were 74-99% related to each other in 60 degrees C hybridization reactions with < or = 4.5% divergence between related sequences. Proteus genomospecies 3 contained the former P. vulgaris type strain and one other strain and was negative in reactions for salicin fermentation, aesculin hydrolysis and deoxyribonuclease, unlike the reactions associated with strains considered as typical P. vulgaris which are positive in reactions for salicin, aesculin and DNase. Genomospecies 3 can be distinguished from Proteus genomospecies 4, 5 and 6 because it is negative for Jordan's tartrate. Proteus genomospecies 4, containing five strains, was differentiated from Proteus penneri, genomospecies 3 and 6 and most, but not all, strains of genomospecies 5, by its ability to ferment L-rhamnose. Proteus genomospecies 5 and 6, containing 18 and 11 strains, respectively, could not be separated from each other by traditional biochemical tests, by carbon source utilization tests or SDS-PAGE of whole-cell proteins. In an earlier publication, a request was made to the Judicial Commission that the former type strain of P. vulgaris (ATCC 13315) be replaced by P. vulgaris biogroup 2 strain ATCC 29905T, a strain considered more biochemically typical of P. vulgaris strains. This would have the effect of assigning the name P. vulgaris to P. vulgaris biogroup 2. Since this request has been acceded to, the name Proteus hauseri is herein proposed for Proteus vulgaris genomospecies 3. Its type strain is ATCC 700826T. Proteus genomospecies 4, 5 and 6 will remain unnamed until better phenotypic differentiation can be accomplished. All Proteus genomospecies were similar in their antimicrobial susceptibility patterns. Nineteen strains were isolated from urine, four from faeces, two from wounds, nine from other human sources and two from animals.

Anti-Bacterial Agents↗
PubMed2003

Structure of the O-polysaccharide of Proteus penneri 28 and Proteus vulgaris O31 and classification of P. penneri 26 and 28 in Proteus serogroup O31.

The lipopolysaccharides (LPS) of Proteus penneri 28 and Proteus vulgaris O31 (PrK 55/57) were degraded with dilute acetic acid and structurally identical high-molecular-mass O-polysaccharides were isolated by gel-permeation chromatography. Sugar analysis and nuclear magnetic resonance (NMR) spectroscopic studies showed that both polysaccharides contain D-GlcNAc, 2-acetamido-2,6-dideoxy-L-glucose (L-2-acetamido-2,6-dideoxyglucose (N-acetylquinovosamine)) and 2-acetamido-3-O-[(S)-1-carboxyethyl]-2-deoxy-D-glucose (N-acetylisomuramic acid) and have the following structure: [carbohydrate structure: see text] where (S)-1-carboxyethyl [a residue of (S)-lactic acid] (S-Lac) is an ether-linked residue of (S)-lactic acid. The O-polysaccharide studied is structurally similar to that of P. penneri 26, which differs only in the absence of S-Lac from the GlcNAc residue. Based on the O-polysaccharide structures and serological data of the LPS, it was suggested classifying these strains in one Proteus serogroup, O31, as two subgroups: O(31a), 31b for P. penneri 28 and P. vulgaris PrK 55/57 and O31a for P. penneri 26. A serological relatedness of the LPS of Proteus O(31a), 31b and P. penneri 62 was revealed and substantiated by sharing epitope O31b, which is associated with N-acetylisomuramic acid. It was suggested that a cross-reactivity of P. penneri 28 O-antiserum with the LPS of several other P. penneri strains is due to a common epitope(s) on the LPS core.

Bacterial Typing Techniques↗
PubMed1974

Bacteriophage typing of Proteus mirabilis, Proteus vulgaris, and Proteus morganii.

A bacteriphage typing scheme for differentiating Proteus isolated from clinical specimens was developed. Twenty-one distinct patterns of lysis were seen when 15 bacteriophages isolated on 8 Proteus mirabilis, 1 P. vulgaris, and 1 P. morganii were used to type 162 of 189 (85.7%) P. mirabilis and P. vulgaris isolates. Seven phages isolated on 3 P. morganii were used to type 13 of 19 (68.4%) P. morganii isolates. Overall, 84.1% of the 208 isolates were lysed by at least 1 phage at routine test dilution (RTD) or 1,000 x RTD. Fifty isolates, retyped several weeks after the initial testing, showed no changes in lytic patterns. The phages retained their titers after storage at 4 C for several months. A computer analysis of the data showed that there was no relationship between the source of the isolate and bacteriophage type. This bacteriophage typing system may provide epidemiological information on strains involved in human infections.

Bacteriological Techniques↗
PubMed1982

Identification of Proteus penneri sp. nov., formerly known as Proteus vulgaris indole negative or as Proteus vulgaris biogroup 1.

The name Proteus penneri sp. nov. is proposed for a group of organisms previously called Proteus vulgaris indole negative or P. vulgaris biogroup 1. All of these strains were salicin negative, esculin negative, and chloramphenicol resistant (zone size, less than 14 mm). DNA relatedness studies indicated that when DNA from P. penneri strain 1808-73 was labeled and tested against unlabeled DNA from 13 other P penneri strains, a highly related group was formed (88 to 99% relatedness at 60 degrees C and 67 to 99% relatedness at 75 degrees C). Strain 1808-73 (ATCC 33519) is proposed as the type strain of P. penneri. In this study, two distinct groups of indole-positive P. vulgaris strains were also apparent. The first group (defined as P. vulgaris biogroup 2) was indole positive, salicin positive, and esculin positive, and the second group (defined as P. vulgaris biogroup 3) was indole positive, salicin negative, and esculin negative. The current type strain of P. vulgaris (ATCC 13315) belongs to biogroup 3. The DNA from P. penneri strains was not highly related to labeled DNA from the type strain of P. vulgaris (14 to 30% relatedness at 75 degrees C) or from P. vulgaris strain PR 1 (ATCC 29905), which belongs to biogroup 2 (27 to 33% relatedness at 75 degrees C). Strains of biogroup 2 were sensitive to chloramphenicol (zone size, greater than 19mm), and 10 of these strains formed a highly related group by DNA hybridization when DNA from PR 1 was labeled (64 to 100% relatedness at 60 degrees C and 70 to 100% relatedness at 75 degrees C), but they were not highly relatedness to the type strain of P. vulgaris (51 to 68% relatedness at 60 degrees C and 14 to 44% relatedness at 75 degrees C). Further DNA relatedness studies are needed on strains of biogroup 3 before a definitive taxonomic proposal can be made for these two indole-positive biogroups.

Anti-Bacterial Agents↗
PubMed2002

Structural and serological characterization of the lipopolysaccharide from Proteus penneri 20 and classification of the cross-reacting Proteus penneri strains 10, 16, 18, 20, 32 and 45 in Proteus serogroup O17.

O-specific polysaccharide (O-antigen) of the lipopolysaccharide of Proteus penneri 20 was studied using sugar analysis along with various one- and two-dimensional NMR spectroscopy techniques. The following structure of the polysaccharide was established: [formula: see text] It has the same carbohydrate backbone structure as that described earlier for P. penneri 16, in which the positions of the O-acetyl groups have not been determined. P. penneri 20 O-antiserum showed a strong cross-reactivity with the lipopolysaccharides of P. penneri 10, 16, 18, 32, 45 and P. mirabilis O17. These data enable classifying these strains together with P. penneri 20 in one Proteus serogroup, O17.

Acetylation↗
PubMed2002

[Investigation of hydrophobicity of Proteus vulgaris strains and ability of Proteus vulgaris and Proteus penneri strains to penetrate bladder membrane HCV T-29 cells ].

Proteus bacilli play a particularly important role in urinary tract infections (UTI). Fimbriae and adherence ability and hemolysins production (HpmA, HlyA) are one of the factors of pathogenicity of these bacteria. In this paper we describe the invasion of HCV T-29 transitional bladder urothelial cells carcinoma strains of P. penneri, as well as P. vulgaris strains belonging to different serogroups. The cytotoxic effect was observed at 8 hour of incubation of the tested cells with P. vulgaris O21 and the same effect (complete lysis) at 6 hours by P. vulgaris O4 (this strain manifests maximal activity in the production of HlyA hemolysin). P. penneri strains, produce different types of fimbriae, expressed similar bacterial invasiveness. The hydrophobic properties of 25 P. vulgaris strains were also tested and only 3 strains occur to have hydrophobic cell surface.

Carcinoma, Transitional Cell↗
PubMed1983

Some biological features of Proteus bacilli. 2. Haemolytic activities of Proteus mirabilis and Proteus vulgaris strains.

The haemolytic activities of Proteus mirabilis and P. vulgaris strains were studied under different conditions. No filterable alpha haemolysin could be detected in P. mirabilis uropathogens provided from patients with urinary tract infections. Together with the results presented in the accompanying paper, in which three clinical isolates with temporary ability to produce a soluble haemolysin were described, the occurrence of alpha haemolytic P. mirabilis isolates did not exceed 3%. Cell bound beta haemolysin is present in nearly 35% of P. mirabilis urinary strains. Another kind of haemolytic activity was observed when P. mirabilis and P. vulgaris strains were grown in liquid media supplemented with erythrocytes. During the logarithmic growth phase nearly 100% of P. mirabilis and P. vulgaris strains of various origin haemolyzed 100-50% of erythrocytes. Except for Serratia, the other representatives of Enterobacteriaceae did not demonstrate such activity in the same conditions. The preliminary characteristics of this phenomenon is given.

Animals↗
PubMed2002

Principles for the surgical management of patients with Proteus syndrome and patients with overgrowth not meeting Proteus criteria.

BACKGROUND: Proteus syndrome is a rare, sporadic disorder consisting of disproportionate overgrowth of multiple tissues, vascular malformations, and connective tissue or epidermal nevi. Patients with Proteus syndrome present with diverse and variable phenotypes because of the syndrome's mosaic pattern of distribution. METHODS: Eighty patients with Proteus syndrome, satisfying published diagnostic criteria, and 51 patients with overgrowth not meeting Proteus criteria were identified from the literature. Three additional patients, one patient with Proteus syndrome and 2 patients with overgrowth, were treated at the author's institutions and are discussed in detail. All nonorthopedic and noncutaneous surgical interventions were reviewed. RESULTS: Fourteen genitourinary, 9 gastrointestinal, and 5 otolaryngologic operations were performed on patients with Proteus syndrome. Six genitourinary, 5 gastrointestinal, and 2 otolaryngologic operations were performed on patients with overgrowth not meeting Proteus criteria. Eight patients with Proteus syndrome and 4 patients with overgrowth experienced thoracic manifestations, generally diffuse cystic pulmonary lesions, but only 1 of 12 underwent surgical treatment. CONCLUSIONS: Patients with visceral manifestations of either Proteus syndrome or overgrowth not meeting Proteus criteria should be treated in a similar manner. Lesions involving the ovaries and testes, because of the high incidence of neoplasm, should be managed aggressively. Gastrointestinal and renal lesions may be managed conservatively with frequent follow-up to minimize abdominal explorations. All patients undergoing surgery should have a thorough preoperative assessment of their airway and pulmonary reserve because of the relatively high frequency of tonsillar hypertrophy and pulmonary cystic involvement.

Adolescent↗
PubMed1990

[Proteus peritonitis-bacteremia in mice--a model for studying postvaccinal Proteus immunity].

The dynamics of the formation of postvaccinal immunity after immunization with preparations obtained with the use of hydroxylamine (HA) preparations from Proteus strains of different O serogroups, Salmonella minnesota Re-mutant and the common antimicrobial antigen isolated from Escherichia coli 14 has been studied on mice with Proteus peritonitis-bacteremia used as a model. The study has revealed that intraperitoneal immunization with Proteus HA preparations stimulates the phagocytic activity of peritoneal mononuclear cells in mice and induces an increase in the titers of specific O antibodies. Proteus antigens ensure the formation of anti-Proteus immunity, preventing the death of the animals from peritonitis-bacteremia. The protection of mice from such infection resulting from the injection of the common antigens of gram-negative bacteria is considerably less. These data are indicative of the possibility of using Proteus peritonitis-bacteremia as a model for the study of the protective potency of Proteus vaccines.

Animals↗
PubMed1994

Anti-Proteus antibodies and Proteus organisms in rheumatoid arthritis: a clinical study.

We have studied anti-Proteus antibodies (APA), isolation of Proteus, and their relation to various measures of RA disease activity. Seventy RA patients with a CRP > 10 mg/l had higher APA titres than 17 RA patients with CRP < or = 10 mg/l (P = 0.006), and 36 non-RA controls (P = 0.003). However, in a cross-sectional study of the RA group, there was no correlation between APA and a number of clinical and laboratory measures of disease activity, including the CRP and Stoke RA activity index. A longitudinal study showed no correlation between changes in these measures of disease activity and change in APA titre. We were unable to isolate Proteus in the urine or faeces of RA patients more frequently than controls, and the isolation of Proteus did not correlate with serum APA titres. Urinary APA was present in equal frequencies in RA and non-RA patients. NSAIDs, DMARDs and steroids did not appear to influence APA titres in the RA group. These results suggest that APA may act as an acute phase protein, distinct from CRP, but not correlating with RA disease activity in its broadest context. The fact that the antibody we are measuring binds to Proteus may be irrelevant, and the study does not support a role for Proteus in RA.

Adult↗
PubMed1996

Comparison of serological reactions of Rickettsiae-infected patients and rabbit anti-Proteus OX antibodies with Proteus OX2, OX19 and OXK lipopolysaccharides.

The reactivity of anti-Rickettsiae human antibodies with Proteus OX cells is used as a presumptive rickettsial diseases diagnostic test Weil-Felix reaction. In presented studies we compare the reactivity of human anti-Rickettsiae and rabbit anti-Proteus antibodies with series of Proteus OX2, OX19 and OXK lipopolysaccharides (LPS). Polyclonal rabbit anti-OX2, anti-OX19 and anti-OXK sera reacted only with the homologous LPS--OX2, OX19 and OXK, respectively. The antibodies of Japanese spotted fever patients were less specific and reacted with OX2 as well as OX19 LPS. The antibodies of scrub typhus patients recognized Proteus OXK LPS, only. The serological reactions of O-antigen of P. mirabilis S1959 indicated that this, previously serologically not classified, strain may belong to the OXK group. Bacteria, used in the studies, came from the American, Japanese and European strain collections. The series of OX2, OX19 and OXK LPS, isolated from these Proteus strains, presented pattern of electrophoretic mobility and serological reactivities specific for each of OX-group types.

Animals↗
PubMed2000

Structural and serological studies of the related O-specific polysaccharides of Proteus vulgaris O21 and Proteus mirabilis O48 having oligosaccharide-phosphate repeating units.

The O-specific polysaccharide chains (O-antigens) of the lipopolysaccharides (LPSs) of Proteus mirabilis O48 and Proteus vulgaris O21 were found to have tetrasaccharide and pentasaccharide repeating units, respectively, interlinked by a glycosidic phosphate. Polysaccharides and an oligosaccharide were derived from the LPSs by various degradation procedures and studied by 1H and 13C NMR spectroscopy, including 2D COSY, TOCSY, NOESY, H-detected 1H,13C and 1H,31P HMQC experiments. The following related structures of the repeating units of the O-antigens were established (top: Proteus mirabilis O48; bottom: Proteus vulgaris O21) The O-specific polysaccharide of P. vulgaris O21 has the same structure as that of Hafnia allvei 744 and PCM 1194 [Petersson C., Jachymek, W., Klonowska, A., Lugowski, C., Niedziela, T. & Kenne, L. (1997) Eur. J. Biochem., 245, 668-675], except that the GlcN residue carries the N-acetyl rather than the N-[(R)-3-hydroxybutyryl] group. Serological investigations confirmed the close relatedness of the Proteus and Hafnia O-antigens studied.

Animals↗
PubMed2003

Structure of the O-polysaccharide leads to classification of Proteus penneri 31 in Proteus serogroup O19.

O-polysaccharide was obtained by mild acid degradation of the lipopolysaccharide (LPS) of Proteus penneri strain 31. Sugar and methylation analyses along with NMR spectroscopic studies, including 2D 1H,1H COSY, TOCSY, ROESY, 1H,13C and 1H,31P HMQC experiments, demonstrated the following structure of the polysaccharide: [carbohydrate structure: see text] where FucNAc is 2-acetamido-2,6-dideoxygalactose and EtnP is 2-aminoethyl phosphate. The polysaccharide studied has the same carbohydrate backbone as the O-polysaccharide of Proteus vulgaris O19. Based on this finding and close serological relatedness of the LPS of the two strains, it is proposed to classify P. penneri 31 in Proteus serogroup O19 as an additional subgroup. In contrast, D-GlcNAc6PEtn and alpha-L-FucNAc-(1-->3)-D-GlcNAc shared with a number of other Proteus O-polysaccharides could not provide any significant cross-reactivity of the corresponding LPS with rabbit polyclonal O-antiserum against P. penneri 31.

Animals↗
PubMed1991

Cytotoxicity of the HpmA hemolysin and urease of Proteus mirabilis and Proteus vulgaris against cultured human renal proximal tubular epithelial cells.

Proteus mirabilis, a common agent of nosocomially acquired and catheter-associated bacteriuria, can cause acute pyelonephritis. In ascending infections, bacteria colonize the bladder and ascend the ureters to the proximal tubules of the kidney. We postulate that Proteus species uses the HpmA hemolysin and urease to elicit tissue damage that allows entry of these bacteria into the kidney. To study this interaction, strains of Proteus mirabilis and P. vulgaris and their isogenic hemolysin-negative (hpmA) or isogenic urease-negative (ureC) constructs were overlaid onto cultures of human renal proximal tubular epithelial cells (HRPTEC) isolated from kidneys obtained by immediate autopsy. Cytotoxicity was measured by release of soluble lactate dehydrogenase (LDH). Two strains of P. mirabilis inoculated at 10(6) CFU caused a release of 80% of total LDH after 6 h, whereas pyelonephritogenic hemolytic Escherichia coli CFT073 released only 25% at 6 h (P less than 0.012). Ten P. mirabilis isolates and five P. vulgaris isolates were all hemolytic and cytotoxic and produced urease which was induced by urea. The HpmA hemolysin is apparently responsible for the majority of cytotoxicity in vitro since the hemolysin-negative (hpmA) mutants of P. mirabilis and P. vulgaris were significantly less cytotoxic than wild-type strains. P. mirabilis WPM111 (hemolysin negative) was used to test the effect of urease-catalyzed urea hydrolysis on HRPTEC viability. In the presence of 50 mM urea, WPM111 caused the release of 42% of LDH versus 1% at 6 h in the absence of substrate (P = 0.003). We conclude that the HpmA hemolysin of Proteus species acts as a potent cytotoxin against HRPTEC. In addition, urease apparently contributes to this process when substrate urea is available.

Bacterial Proteins↗
PubMed1964

TRANSFER OF EPISOMIC ELEMENTS TO PROTEUS. II. NATURE OF LAC+ PROTEUS STRAINS ISOLATED FROM CLINICAL SPECIMENS.

Falkow, Stanley (Walter Reed Army Institute of Research, Washington, D.C.), J. A. Wohlhieter, R. V. Citarella, and L. S. Baron. Transfer of episomic elements to Proteus. II. Nature of lac(+)Proteus strains isolated from clinical specimens. J. Bacteriol. 88:1598-1601. 1964.-Strains of Proteus mirabilis exhibiting the unusual property of utilizing lactose (lac(+)) have been reported in clinical material. A genetic examination discloses that the lac(+) determinants in these Proteus strains are associated with an infectious element, P, which is distinct from the sex factor of Escherichia coli K-12. The composite genetic element, P-lac, is readily transmissible to other enteric species and possesses properties which conform to those of an episomic element of the transfer variety. CsCl density-gradient studies of deoxyribonucleic acid (DNA) extracted from lac(+)P. mirabilis indicate that the P-lac(+) element did not arise in this species, but was acquired from an organism possessing a markedly different DNA base composition.

Amino Acids↗
PubMed2003

Structure of the O-polysaccharide of a serologically separate strain of Proteus mirabilis, TG 332, from a new proposed Proteus serogroup O50.

The O-polysaccharide was obtained by mild acid degradation of the lipopolysaccharide of Proteus mirabilis TG 332 strain. The following structure of the O-polysaccharide was determined by chemical methods along with NMR spectroscopy, including 2D COSY, TOCSY, ROESY and 1H, 13C HMQC experiments: [see equation in text]. The O-polysaccharide studied has a unique structure among Proteus O-antigens. Accordingly, P. mirabilis TG 332 is serologically separate, and we propose to classify this strain into a new Proteus serogroup, O50. The nature of minor epitopes that provide a cross-reactivity of P. mirabilis TG 332 O-antiserum with the LPS of P. mirabilis O30 and Proteus penneri 34 (O60) is discussed.

Animals↗
PubMed2003

Structure of the O-polysaccharide from Proteus myxofaciens. Classification of the bacterium into a new Proteus-O-serogroup.

The O-polysaccharide (O-antigen) was obtained from the lipopolysaccharide of Proteus myxofaciens, a Proteus strain producing copious amounts of slime, which was isolated from the gypsy moth larvae. The structure of the polysaccharide was studied by chemical analysis and 1H and 13C NMR spectroscopy, including 2D COSY, TOCSY, ROESY and H-detected 1H,13C HMQC experiments. It was found that the polysaccharide contains an amide of glucuronic acid (GlcA) with an unusual alpha-linked amino acid, Nepsilon-[(R)-1-carboxyethyl]-l-lysine (2S,8R-alaninolysine, 2S,8R-AlaLys), and has a linear tetrasaccharide repeating unit of the following structure: This structure is unique among known bacterial polysaccharide structures. On the basis of these and serological data, it is proposed that P. myxofaciens be classified into a new Proteus serogroup, O60, of which this strain is the single representative. Structural and serological relatedness of P. myxofaciens to other AlaLys-containing O-antigens of Proteus and Providencia is discussed.

Amides↗