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PubMed2006

Perioperative respiratory complications caused by cystic lung malformation in Proteus syndrome.

A 7-year-old girl with Proteus syndrome, complicated with severe kyphoscoliosis and cystic lung malformation, developed respiratory complications during and after posterior spinal fusion under general anesthesia. We speculated that low oxygenation while in the prone position contributed to ventilation perfusion mismatch owing to the cystic lung malformation that existed predominantly in the right lung, and that postoperative respiratory failure was caused by initially increased bronchial mucous secretions and secondary persistent bacterial pneumonia. Cystic lung malformation rather than reduced respiratory function, although both can be a cause of mucous clearance impairment, should be considered as one of the predictive factors for perioperative respiratory failure in Proteus syndrome.

Child↗
PubMed1975

Membrane ATPase of Proteus L-forms. Solubilization and molecular properties.

The Mg2+ -dependent ATPase (EC 3.6.I.3) of Proteus L-form membrane has been solubilized according to various procedures (Tris - HCL shock-wash with or without MG2+, EDTA, Triton X-100). The best results were obtained by the same 33mM Tris-HCL (pH 7.5) shock-wash without MG2+ used for ATPase of protoplasts from Streptococcus faecalis. The solubilized enzyme after 105 000 times g centrifugation was purified on acrylamide/agarose. The molecular weight was established to be 360 000 by gel filtration and by sedimentation coefficient (12.5 S). Polyacrylamide disc-gel electrophoresis in sodium dodecylsulphate revealed two classes or subunit of mol. wt. 64 000 (alpha) and 58 000 (beta), associated in ratio 1:1. We propose a formula alpha-3beta-3 for the native ATPase of Proteus L-forms. Structural similarities to ATPase of various origins are discussed.

Adenosine Triphosphatases↗
PubMed1993

Macrodactyly in Proteus syndrome.

A case of Proteus syndrome in a 13-year-old boy with macrodactyly, hemihypertrophy, exostosis of the skull, epidermal naevi, palmar and plantar masses, and scoliosis is reported. Macrodactyly involving the left thumb was treated surgically. The usual findings in macrodactyly, hypertrophy of the digital nerves and proliferation of subcutaneous fat, were not observed in this case. Macrodactyly associated with Proteus syndrome should be distinguished from other forms of macrodactyly because of its poor prognosis and high rate of recurrence.

Adolescent↗
PubMed1992

Proteus syndrome.

Proteus syndrome is a rare congenital disorder that is characterized by a wide variety of deformities including macrodactyly. Skin and soft tissue lesions are common; they may increase in size as the child develops and may assume tremendous proportions. The syndrome is often mistaken for other more commonly recognized conditions such as neurofibromatosis. Unlike neurofibromatosis, the soft tissue masses in Proteus syndrome are not nerve tumors but, rather, are hamartomas composed primarily of lipomatous tissue. The hand surgeon should be aware of this condition when evaluating a child with macrodactyly.

Diagnosis, Differential↗
PubMed1995

[Hamartomatous dysplasias with hemihypertrophy. 2 cases including one with Proteus syndrome].

BACKGROUND: Hamartomatous dysplasias with hemihypertrophy are a part of several congenital diseases, sometimes difficult to classify when their symptomatology is relatively poor. CASE REPORTS: Case 1. A girl, 11 year-old, suffered from gigantism of the feet, left hemihypertrophy of the limbs, scoliosis and kyphosis. X-rays showed frontal hyperostose, bony and soft tissues overgrowth involving the left limbs and pelvis with hip dislocation and coxa valga. The vertebrae were hypertrophic and dysplastic. No tumor could be found. Case 2. A girl, 18 year-old, suffered from left hemihypertrophy of limbs and face associated with homolateral cutaneous hemangioma. X-rays showed enlargement of bone and soft tissue. No tumor or venous abnormalities were observed. CONCLUSION: A diagnosis of Proteus syndrome was made in the first patient while the second patient was considered to have Klippel-Trenaunay syndrome even though hemangiomatous involvement has been seen in Proteus syndrome.

Adolescent↗
PubMed2004

Structure of the neutral O-polysaccharide and biological activities of the lipopolysaccharide of Proteus mirabilis O20.

Mild acid degradation of the lipopolysaccharide (LPS) of Proteus mirabilis O20 resulted in depolymerisation of the O-polysaccharide to give a repeating-unit pentasaccharide. A polysaccharide was obtained by O-deacylation of the LPS followed by nitrous acid deamination. The derived pentasaccharide and polysaccharide were studied by NMR spectroscopy, including 2D 1H,1H COSY, TOCSY, ROESY, 1H,13C HMQC and HMQC-TOSCY experiments, along with chemical methods, and the following structure of the repeating unit of the O-polysaccharide was established: [Carbohydrate structure: see text]. As opposite to most other P. mirabilis O-polysaccharides studied, that of P. mirabilis O20 is neutral. A week serological cross-reactivity was observed between anti-P. mirabilis O20 serum and LPS of a number of Proteus serogroups with known O-polysaccharide structure. The ability of LPS of P. mirabilis O20 to activate the serine protease cascade was tested in Limulus amoebocyte lysate and in human blood plasma and compared with that of P. mirabilis O14a,14c having an acidic O-polysaccharide. The LPS of P. mirabilis O20 was found to be less active in both assays than the LPS of P. mirabilis O14a,14c and, therefore, the structurally variable O-polysaccharide may influenced the biological activity of the conserved lipid A moiety of the LPS.

Animals↗
PubMed2005

Structure of the O-polysaccharide and serological studies of the lipopolysaccharide of Proteus mirabilis 2002.

The structure of the O-polysaccharide of the lipopolysaccharide of Proteus mirabilis 2002 was elucidated by chemical methods and 1H and 13C NMR spectroscopy. It was found that the polysaccharide consists of branched pentasaccharide repeating units having the following structure: [structure in text]. The O-polysaccharide of P. mirabilis 2002 has a common tetrasaccharide fragment with that of P. mirabilis 52/57 from serogroup O29, and the lipopolysaccharides of the two strains are serologically related. Therefore, based on the structural and serological data, we propose to classify P. mirabilis 2002 into the Proteus O29 serogroup as a subgroup O29a,29b.

Animals↗
PubMed2006

Structure of the O-polysaccharide of Proteus mirabilis CCUG 10705 (OF) containing an amide of D-galacturonic acid with L-alanine.

The structure of the O-polysaccharide of Proteus mirabilis CCUG 10705 (OF) was determined by chemical analyses along with one- and two-dimensional (1)H and (13)C NMR spectroscopy. The polysaccharide was found to contain an amide of D-galacturonic acid with L-alanine and based on the uniqueness of the O-polysaccharide structure and serological data, it was suggested to classify P. mirabilis OF into a new separate Proteus serogroup, O74. A weak cross-reactivity of P. mirabilis OF and P. mirabilis O5 was observed and accounted for by a similarity of their O-repeating units. The following structure of the polysaccharide of P. mirabilis OF was established: [chemical structure: see text]

Acetylation↗
PubMed2004

Craniofacial hyperostoses in Proteus syndrome -- a case report.

OBJECTIVE: Description of a patient with a rare syndrome leading to the partial overgrowth of craniofacial bones. CASE REPORT: In a 17-year-old female patient with severe hyperostoses of the craniofacial bones asymmetric overgrowth of the right upper and left lower limbs, linear hyperpigmentation of the right arm and a history of regional lipomatosis were found. These manifestations were suggestive of Proteus syndrome. The management of the craniofacial involvement is described and a literature overview presented. CONCLUSION: Proteus syndrome is a rare overgrowth syndrome probably related to a somatic mutation that involves craniofacial structures in about 30% of patients. Early diagnosis is required for adequate interdisciplinary treatment.

Adolescent↗
PubMed2001

Structure of the O-specific polysaccharide of Proteus vulgaris O4 containing a new component of bacterial polysaccharides, 4,6-dideoxy-4.

A high-molecular-mass O-specific polysaccharide was obtained by mild acid degradation of Proteus vulgaris O4 lipopolysaccharide followed by GPC. The polysaccharide was studied by chemical methods along with 1H and 13C NMR spectroscopy, including two-dimensional COSY, TOCSY, NOESY, H-detected 1H,13C HMQC, and 1H,13C HMBC experiments. Solvolysis of the polysaccharide with trifluoromethanesulfonic (triflic) acid resulted in a GlcpA-(1 --> 3)-GlcNAc disaccharide and a novel amino sugar derivative, 4,6-dideoxy-4-[N-[(R)-3-hydroxybutyryl]-L-alanyl]amino-D-glucose [Qui4N(HbAla)]. On the basis of the data obtained, the following structure of the tetrasaccharide repeating unit of the O-specific polysaccharide was established: --> 4)-beta-D-GlcpA-(1 --> 3)-beta-D-GlcpNAc-(1 --> 2)-beta-D-Quip4N(HbAla)-(1 --> 3)-alpha-D-Galp-(1 -->. This structure is unique among the O-specific polysaccharides, which is in accordance with classification of the strain studied in a separate Proteus serogroup.

Animals↗
PubMed2002

Structure of the core part of the lipopolysaccharides from Proteus penneri strains 7, 8, 14, 15, and 21.

The core-lipid A region of the lipopolysaccharides from Proteus penneri strains 7, 8, 14, 15, and 21 was studied using NMR spectroscopy, ESI MS, and chemical analysis after alkaline deacylation, deamination, and mild-acid hydrolysis of the lipopolysaccharides. The following general structure of the major core oligosaccharides is proposed: [abstract: see text] where all sugars are in the pyranose form and have the D configuration unless otherwise stated, Hep and DDHep=L-glycero- and D-glycero-D-manno-heptose, respectively, K=H, and Q=H in strain 8 or alpha-Glc in strains 7, 14, 15, and 21. In addition, several minor structural variants are present, including those lacking Ara4N in strains 7 and 15 and having the alpha-GlcN residue N-acylated to a various degree with glycine in strains 7, 8, 14, and 21. In strain 14, there are also core oligosaccharides with K=amide of beta-D-GalpA with putrescine, spermidine, or 4-azaheptane-1,7-diamine; remarkably, these structural variants lack either the PEtN group or the alpha-Hep-(1-->2)-alpha-DDHep disaccharide fragment at alpha-D-GalpA. While structural features of the inner core part are shared by Proteus strains studied earlier, the outermost Q-(1-->4)-alpha-GalNAc-(1-->2)-alpha-DDHep-(1-->6)-alpha-GlcN oligosaccharide unit has not been hitherto reported.

Carbohydrate Conformation↗
PubMed2003

Structure of the O-specific polysaccharide of Proteus vulgaris O45 containing 3-acetamido-3,6-dideoxy-D-galactose.

An O-specific polysaccharide was isolated by mild acid degradation of the lipopolysaccharide of Proteus vulgaris O45 and studied by sugar and methylation analyses along with 1H and 13C NMR spectroscopy, including 2D COSY, TOCSY, ROESY, H-detected 1H,13C HSQC and HMBC experiments. The following structure of the pentasaccharide repeating unit of the polysaccharide was established:-->6)-alpha-D-GlcpNAc-(1-->4)-alpha-D-GalpNAc-(1-->4)-alpha-D-GalpA-(1-->3)-beta-D-GlcpNAc-(1-->2)-beta-D-Fucp3NAc4Ac-(1-->where Fuc3NAc4Ac is 3-acetamido-4-O-acetyl-3,6-dideoxygalactose. A cross-reactivity of anti-P. vulgaris O45 serum was observed with several other Proteus lipopolysaccharides, which contains Fuc3N derivatives.

Acetylgalactosamine↗
PubMed1996

Structural and serological studies of the O-specific polysaccharide of the bacterium Proteus mirabilis O10 containing L-altruronic acid, a new component of O-antigens.

An acidic O-specific polysaccharide from the lipopolysaccharide of Proteus mirabilis O10 contains 2-acetamido-2-deoxy-D-glucose, 2-acetamido-2-deoxy-D-galactose, D-galacturonic acid, and L-altruronic acid, the last-named sugar having not been found hitherto in O-antigens. Structure of a branched tetrasaccharide repeating unit of the polysaccharide was established by 1H and 13C NMR spectroscopy, including two-dimensional COSY and rotating-frame NOE spectroscopy. The lateral L-altruronic acid residue plays the immunodominant role in manifestation of the O10 specificity of Proteus, whereas a disaccharide fragment of the main chain in common with the O-specific polysaccharide of P. mirabilis O43 provides the one-way serological cross-reactivity between anti-O10 serum and O43-antigen.

Antibodies, Bacterial↗
PubMed1985

Antibodies to proteus in rheumatoid arthritis.

Antibodies to proteus species were measured in patients with rheumatoid arthritis (RA) and ankylosing spondylitis (AS) and in healthy controls by a Coombs agglutination method. The titres to Proteus mirabilis were higher in 30 RA patients being treated with gold than in 24 patients with active AS (p less than 0.001), 28 patients with inactive AS (p less than 0.001), and 41 healthy control subjects (p less than 0.001). Control studies with Klebsiella pneumoniae var oxytoca showed high antibody titres only in active AS patients.

Adult↗
PubMed1998

Proteus syndrome. A case report of a hamartomatous syndrome with severe mandibular hemihypertrophy.

Proteus syndrome is a rare congenital hamartomatous malformation that is characterized by a wide range of deformities, including craniofacial deformities. Skin and skeletal developmental malformations are common and may assume tremendous proportions. The syndrome is often mistaken for other, more commonly recognized conditions, including neurofibromatosis. The soft-tissue masses in Proteus syndrome are not nerve tumors but are usually hamartomatous proliferations. The case report describes its varied manifestations, which include significant craniofacial dysmorphism, and discusses the differential diagnosis and management.

Adult↗
PubMed2003

[Proteus syndrome: report of two cases].

Proteus syndrome is a complex disorder, consisting of mesodermal and skeletal malformations as well as hamartomatous overgrowth. It is characterized by highly variable presentation and mosaic-pattern lesions. The two cases described herein illustrate the wide polymorphism of this syndrome. The second case also had a pubic fracture, which we have not previously seen reported in the medical literature on Proteus syndrome.

Abnormalities, Multiple↗
PubMed2002

Tryptophan indole-lyase from Proteus vulgaris: kinetic and spectral properties.

An efficient method for purification of recombinant tryptophanase from Proteus vulgaris was developed. Catalytic properties of the enzyme in reactions with L-tryptophan and some other substrates as well as competitive inhibition by various amino acids in the reaction with S-o-nitrophenyl-L-cysteine were studied. Absorption and circular dichroism spectra of holotryptophanase and its complexes with characteristic inhibitors modeling the structure of the principal reaction intermediates were examined. Kinetic and spectral properties of two tryptophanases which markedly differ in their primary structures are compared. It was found that although the spectral properties of the holoenzymes and their complexes with amino acid inhibitors are different, the principal kinetic properties of the enzymes from Proteus vulgaris and Escherichia coli are analogous. This indicates structural similarity of their active sites.

Binding Sites↗
PubMed2006

[A young patient with portal and mesenteric vein thrombosis and Proteus syndrome].

In the 26th year of life a young woman suffered a portal and mesenteric thrombosis followed by portal hypertension with splenomegaly, esophageal varices and pancytopenia. After splenorenal shunt surgery and splenectomy hematologic parameters resolved rapidly. Also, she was suffering of Proteus syndrome, which is an extremely rare and sporadic hamartomatous disorder characterized by a variety of cutaneous and subcutaneous tumors including vascular malformations, several types of nevi, partial gigantism of the hands and/or feet and cystic visceral affections. It has been demonstrated that concurrence of several prothrombotic risk factors occur relatively often in patients with portal vein thrombosis. An extensive investigation of thrombophilic factors revealed reproduced high anti-beta2-glycoprotein I antibody titers together with mildly increased homocysteine levels. Other coagulation parameters were normal or negative. The presence of myeloproliferative moglobinuria was ruled out. Together with the history of recurrent superficial thrombophlebitis and portal vein thrombosis in the absence of other underlying diseases allowed for diagnosis of primary antiphospholipid syndrome being aggravated by hyperhomocysteinemia and vascular malformations caused by Proteus syndrome. Because of combined risk factors for further thrombembolisms permanent oral anticoagulant therapy was initiated.

Adult↗