Pacemaker lead infection and vertebral osteomyelitis presumed due to Cardiobacterium hominis.
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Aged↗
Biomedical subjects
A Weintraub
Publications and source records attributed to A Weintraub.
Predoctoral fixed prosthodontics curriculum survey.
PURPOSE: In 1996, a survey of American dental schools was conducted. The purpose of the survey was to determine the curricular structure, techniques taught, and materials used in predoctoral fixed prosthodontics courses. MATERIALS AND METHODS: The survey was mailed to the course directors of predoctoral fixed prosthodontic programs at 53 American dental schools. Of these, 42 schools returned the completed survey, resulting in a response rate of 79%. The mean, median, and the range of responses were computed where applicable. RESULTS: The results from this survey show that the mean student-to-faculty ratio in the preclinical course was 11:1, with a median of 10:1 and a range of 5:1 to 25:1. The mean number of laboratory clock hours was 164, with a median of 148 and a range of 81 to 288. The mean number of lecture hours reported was 42, with a median of 35 and a range of 20 to 80. Fifty-five percent of the schools used the Hanau semiadjustable articulator. The most commonly used provisional technique was the thermoplastic custom external surface form (44%). The finish line of choice for the full metal restoration was the chamfer placed circumferentially (74%). The finish line of choice for the porcelain-fused-to-metal restoration was the shoulder placed facially and the chamfer placed lingually (38%). CONCLUSIONS: Predoctoral fixed prosthodontics education and technical experience varies from school to school, yet a large percentage of schools agree on certain topics.
Curriculum↗
Rapid and sensitive assay for detection of enterotoxigenic Bacteroides fragilis.
Bacteroides fragilis is an obligatory anaerobic, gram-negative bacterium found among the normal intestinal flora of humans. Enterotoxigenic strains of B. fragilis (ETBF) have been associated with diarrheal diseases in humans and animals. The enterotoxin of ETBF induces fluid changes in ligated intestinal segments and cytotoxic response in HT29/C1 cells. By using a pair of monoclonal antibodies (MAbs; MAb C3 and MAb 4H8) specific for the lipopolysaccharide of B. fragilis, an assay based on immunomagnetic separation (IMS) in combination with PCR (IMS-PCR) was developed. After DNA extraction, a 294-bp fragment was amplified. The specificity of the IMS-PCR assay was evaluated by adding previously isolated and confirmed ETBF strains to normal fecal samples. All fecal samples to which ETBF strains were added were positive, showing a 100% specificity. The spiked fecal samples were also used for evaluation of the sensitivity of the assay. The detection limit was found to be approximately 50 CFU/g of feces. By this method 10 clinical fecal samples (5 from patients with diarrhea and 5 from healthy controls) were examined. The results of PCR were in accordance with the results of the HT29/C1 cell assay for all samples. The minimum time to retrieval of the final result by the IMS-PCR method is 36 h. The proposed IMS-PCR assay is rapid and sensitive for the direct detection of ETBF in stool samples.
Animals↗
Structural analysis of the O-antigenic polysaccharide from Vibrio cholerae O10.
The structure of the O-antigenic polysaccharide part of the lipopolysaccharide isolated from Vibrio cholerae O10 has been determined. The main method used has been 1H- and 13C-NMR spectroscopy. Sugar and methylation analyses were also applied to the polysaccharide. The tetrasaccharide repeating unit of the polysaccharide was found to have the following structure: -->3)-alpha-D-ManpNAc-(1-->4)-beta-D-GlcpA-(1-->3)-beta-D-Ga lp-(1-->3)-beta-D-GlcpNAc-(1-->.
Carbohydrate Conformation↗
Structural studies of the O-antigen polysaccharide from Escherichia coli O138.
The structure of the O-antigen polysaccharide from Escherichia coli O138 has been determined. NMR spectroscopy, together with component and methylation analyses, of native and reduced polysaccharide were the principal methods used. The sequence of the sugar residues could be determined by NOESY and heteronuclear multiple bond connectivity (HMBC) NMR experiments. It is concluded that the polysaccharide is composed of tetrasaccharide repeating units with the following structure: [structure: see text].
Carbohydrate Conformation↗
Structural studies on the short-chain lipopolysaccharide of Vibrio cholerae O139 Bengal.
A Vibrio cholerae O139 strain, MO10-T4, lacking capsular polysaccharide, produces a short-chain lipopolysaccharide (LPS), similar to enterobacterial SR strains. It was studied by acidic and alkaline degradation, dephosphorylation, sugar and methylation analysis, high-performance anion-exchange chromatography, one- and two-dimensional 1H-, 13C-, and 31P-NMR spectroscopy, and electrospray ionization mass spectrometry. The following structure was proposed for the core region of the LPS: [structure: see text] where PEtn stands for 2-aminoethyl phosphate, Fru for fructose, Hep for L-glycero-D-manno-heptose, and Kdo for 3-deoxy-D-manno-octulosonic acid; unless otherwise stated, the monosaccharide residues are D and present in the pyranose form. An O-acetyl group is present on a secondary position, tentatively O4 of the alpha-linked glucosyl group. Some LPS species contain an additional putative fructose residue whose location remains unknown. An O139-negative mutant strain, Bengal-2R, derived from V. cholerae O139, has also been investigated and shown to produce an O-antigen-lacking LPS similar to those from enterobacterial R strains, some of the LPS species containing the same core region as the strain MO10-T4 LPS and the other lacking the lateral heptose residue. The carbohydrate backbone core structure is the same for the V. cholerae O139 and V. cholerae O1 LPS, thus confirming the close relation between these bacteria; however, the 2-aminoethyl phosphate, the O-acetyl group, and the second fructose residue have not been reported for the O1 LPS. In the V. cholerae O139 strain MO10-T4 LPS, a short O-side chain is attached at position 3 of the 7-substituted heptose residue and has the same structure as one repeating unit of the V. cholerae O139 capsular polysaccharide. Some details of the structure proposed are at variance with those recently published for another V. cholerae O139 strain [Cox, A. D., Brisson, J.-R., Varma, V. & Perry, M. B. (1996) Carbohydr. Res. 290, 43-58; Cox, A. D. & Perry, M. B. (1996) Carbohydr. Res. 290, 59-65.]
Lipopolysaccharides↗
Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage.
The tailspike protein of Salmonella phage P22 is a viral adhesion protein with both receptor binding and destroying activities. It recognises the O-antigenic repeating units of cell surface lipopolysaccharide of serogroup A, B and D1 as receptor, but also inactivates its receptor by endoglycosidase (endorhamnosidase) activity. In the final step of bacteriophage P22 assembly six homotrimeric tailspike molecules are non-covalently attached to the DNA injection apparatus, mediated by their N-terminal, head-binding domains. We report the crystal structure of the head-binding domain of P22 tailspike protein at 2.3 A resolution, solved with a recombinant telluromethionine derivative and non-crystallographic symmetry averaging. The trimeric dome-like structure is formed by two perpendicular beta-sheets of five and three strands, respectively in each subunit and caps a three-helix bundle observed in the structure of the C-terminal receptor binding and cleaving fragment, reported here after full refinement at 1.56 A resolution. In the central part of the receptor binding fragment, three parallel beta-helices of 13 complete turns are associated side-by-side, while the three polypeptide strands merge into a single domain towards their C termini, with close interdigitation at the junction to the beta-helix part. Complex structures with receptor fragments from S. typhimurium, S. enteritidis and S. typhi253Ty determined at 1.8 A resolution are described in detail. Insertions into the beta-helix form the O-antigen binding groove, which also harbours the active site residues Asp392, Asp395 and Glu359. In the intact structure of the tailspike protein, head-binding and receptor-binding parts are probably linked by a flexible hinge whose function may be either to deal with shearing forces on the exposed, 150 A long tailspikes or to allow them to bend during the infection process.
Amino Acid Sequence↗
Structural analysis of the O-antigenic polysaccharide from the enteropathogenic Escherichia coli O142.
The polysaccharide part of the lipopolysaccharide obtained from the enteropathogenic Escherichia coli O142 has been isolated, and its structure determined. Together with 1H-NMR and 13C-NMR spectroscopy, sugar and methylation analyses show that the polysaccharide is composed of repeating pentasaccharide units. Sequential information on the O-polysaccharide was obtained by two-dimensional NMR techniques, namely heteronuclear-multiple-bond-connectivity and NOESY experiments. The repeating unit of the O-polysaccharide of E. coli strain O142 has the following structure: [structure: see text].
Carbohydrate Sequence↗
Structure determination of the O-antigenic polysaccharide from the enterotoxigenic Escherichia coli (ETEC) O101.
The O-antigenic polysaccharide of the lipopolysaccharide from the enterotoxigenic Escherichia coli O101 has been investigated. The composition and sequence of the repeating units was established by sugar and methylation analysis together with 1H and 13C NMR spectroscopy. The sequence was corroborated using the computer program CASPER. The structure of the repeating unit of the polysaccharide from E. coli O101 is as follows: -->6)-alpha-D-GlcpNAc-1-->4-alpha-D-GalpNAc-(1-->.
Carbohydrate Conformation↗
Identification of Bacteroides fragilis by co-agglutination, using a specific monoclonal antibody.
A monoclonal antibody, mAbC3 (IgG(2b)), specific for the Bacteroides fragilis lipopolysaccharide (LPS) was produced and found to react with a common epitope in most strains within the species. mAbC3 was adsorbed to Staphylococcus aureus Cowan I strain and used in a co-agglutination assay for identification of B. fragilis. Almost 98% of the B. fragilis strains were positive in co-agglutination. Among the 283 non-B. fragilis only two strains showed false positive reaction. These results show that the mAbC3 has a high specificity and can be used for the rapid identification of the B. fragilis species.
Journal Article↗
Rapid detection of Vibrio cholerae O139 Bengal from stool specimens by PCR.
In a previous study using pure bacterial cultures in a PCR assay, a primer pair corresponding to a unique chromosomal region of Vibrio cholerae O139 Bengal generated an amplicon from only V. cholerae O139 Bengal. PCR with the same primer pair was used to screen 180 diarrheal stool specimens. All the 67 V. cholerae O139 culture-positive stool specimens were positive by PCR, and the remaining specimens, which contained either other recognized enteric pathogens or no pathogens, were all negative by PCR.
Cholera↗
Penicillin at birth can help prevent early-onset group B streptococcal disease.
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Humans↗
Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.
The O-antigenic repeating units of lipopolysaccharides from Salmonella serogroups A, B, and D1 serve as receptors for the phage P22 tailspike protein, which also has receptor destroying endoglycosidase (endorhamnosidase) activity, integrating the functions of both hemagglutinin and neuraminidase in influenza virus. Crystal structures of the tailspike protein in complex with oligosaccharides, comprising two O-antigenic repeating units from Salmonella typhimurium, Salmonella enteritidis, and Salmonella typhi 253Ty were determined at 1.8 A resolution. The active-site topology with Asp-392, Asp-395, and Glu-359 as catalytic residues was identified. Kinetics of binding and cleavage suggest a role of the receptor destroying endorhamnosidase activity primarily for detachment of newly assembled phages.
Bacteriophage P22↗
Structure determination of the O-antigen polysaccharide from the enteroinvasive Escherichia coli (EIEC) O143 by component analysis and NMR spectroscopy.
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Carbohydrate Conformation↗
Structural studies of the enteroinvasive Escherichia coli (EIEC) O28 O-antigenic polysaccharide.
The structure of the O-specific side-chain of the lipopolysaccharide from Escherichia coli O28 has been investigated. NMR spectroscopy has been the main method used, complemented with sugar and methylation analyses. The polysaccharide contains one equivalent of O-acetyl groups per repeating unit. Selective cleavage of the O-deacetylated polymer was performed by treatment with aqueous hydrofluoric acid, and resulted in a trisaccharide-glycerol. The polysaccharide thus is of the teichoic acid type and composed of repeating units in which the trisaccharide-glycerol residues are joined by phosphodiester linkages. The O-antigen polysaccharide has the following structure. [sequence: see text] The absolute configuration of the glycerol moiety as R, )i.e., D-glycerol 1-phosphate) was determined by a new method based on TEMPO oxidation of the polysaccharide, followed by GLC analysis of the (+)-2-butyl ester of the resulting glyceric acid.
Carbohydrate Conformation↗
Structural analysis of the O-antigenic polysaccharide from the enteropathogenic Escherichia coli O125.
The structure of the polysaccharide part of the lipopolysaccharide obtained from the enteropathogenic Escherichia coli O125 has been investigated. Methylation analysis, 1H-NMR spectroscopy and 13C-NMR spectroscopy revealed that the polysaccharide is composed of repeating hexasaccharide units. Smith degradation of the native O-polysaccharide resulted in a polysaccharide with four sugar residues in the repeating unit. Information on the sequence of the native O-polysaccharide and the Smith-degraded product was obtained by two-dimensional techniques, namely heteronuclear-multiple-bond-connectivity and NOESY experiments. The structure of the repeating unit of the O-polysaccharide of E. coli strain O125, which has two adjacent branch-point residues, is [sequence: see text].
Carbohydrate Conformation↗
Structure of the O-specific polysaccharide of an Aeromonas trota strain cross-reactive with Vibrio cholerae O139 Bengal.
The O-specific polysaccharide of an Aeromonas trota strain was isolated by hydrolysis of the lipopolysaccharide at pH 4.5 followed by gel-permeation chromatography and found to consist of hexasaccharide repeating units containing D-galactose, L-rhamnose, 3,6-dideoxy-L-xylo-hexose (colitose, Col), 2-acetamido-2-deoxy-D-glucose and 2-acetamido-2-deoxy-D-galactose in the ratios 1:1:2:1:1. Partial hydrolysis of the polysaccharide with 48% hydrofluoric acid resulted in selective removal of colitose to give a modified polysaccharide containing the other four sugar constituents. On the basis of methylation analysis and NMR spectroscopic studies of the initial and modified, colitose-free polysaccharide, it was concluded that the repeating unit of the O-specific polysaccharide has the following structure [sequence: see text] The known cross-reactivity between the strain studied and Vibrio cholerae O139 Bengal is substantiated by the presence of a common colitose-containing epitope shared by the O-specific polysaccharide of A. trota and the capsular polysaccharide of V. cholerae, which is thought to carry determinants of O-specificity.
Aeromonas↗
Structural studies of the Escherichia coli O26 O-antigen polysaccharide.
The structure of the O-specific side chain of the E. coli O26 lipopolysaccharide has been investigated. Based on sugar and methylation analyses, and 2D NMR spectroscopy employing HMBC experiments, it is concluded that the polysaccharide is composed of trisaccharide repeating units having the following structure. -->3)-alpha-L-Rhap-(1-->4)-alpha-L-FucpNAc-(1-->3)-beta-D-Gl cpNAc-(1-->
Acetylglucosamine↗