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Biomedical subjects

K Jann

Publications and source records attributed to K Jann.

At least 109 records · Page 6Linked to original sources

Crossreactions of Escherichia coli K and O polysaccharides in antipneumococcal and anti-Salmonella sera.

Crossreactions of 24 K polysaccharides and 4 O polysaccharides of E. coli in antisera to 27 pneumococcal types, 3 anti-Salmonella sera, and anti-Klebsiella Kl serum are discussed in relation to structural features of the polysaccharides insofar as these are known. Predictions based on the crossprecipitations are also ventured for several instances in which structures are as yet undetermined.

Animals↗

Biosynthesis of the O9 antigen of Escherichia coli. Synthetic glycosyldiphosphomoraprenols as probes for requirement of mannose acceptors.

Synthetic monosaccharide derivatives (alpha-glucosyl, beta-glucosyl, alpha-mannosyl) and disaccharide derivatives (alpha-mannosyl-1,2-alpha-glucosyl, alpha-mannosyl-1,3-alpha-glucosyl, alpha-mannosyl-1,4-alpha-glucosyl, alpha-mannosyl-1,6-alpha-glucosyl) of diphosphomoraprenol were used as putative mannose acceptors in the biosynthesis of Escherichia coli O9 antigen. Membranes of E. coli O9 derived from the rfe mutant F 1357 were reconstituted with these compounds and then incubated with different concentrations of GDP-[14C]mannose. Of the monosaccharide derivatives tested, only alpha-glucodiphosphomoraprenol was a mannose acceptor and the only disaccharide derivative which accepted mannose was alpha-mannosyl-1,3-alpha-glucosyldiphosphomoraprenol. The alpha-glucosyl derivative accepted only one mannose unit at 4 microM GDP-[14C]mannose, and above 50 microM GDP-[14C]mannose about 25% of the product had a minimum size of about 30 mannose units. The alpha-mannosyl-1,3-alpha-glucosyl derivative was only a mannose acceptor at a GDP-[14C]mannose concentration of 50 microM and higher, and the product had a minimum size of about 30 mannose units. The results are discussed with respect to requirement of mannose acceptors.

Antigens, Bacterial↗

Structure of the amino acid-containing capsular polysaccharide (K54 antigen) from Escherichia coli O6:K54:H10.

The structure of the K54-antigenic polysaccharide (K54 antigen) of Escherichia coli O6:K54:H10 was elucidated by determination of the composition, 1H- and 13C-n.m.r. spectroscopy, periodate oxidation, and a study of the oligosaccharides obtained by partial hydrolysis with acid. The K54 polysaccharide consists of----3)-beta-D-glucosyluronic acid-(1----3)-alpha-L-rhamnosyl-(1----repeating-units. Of the glucuronic acid residues, approximately 85% are substituted in the ratio 9:1 with L-threonine and L-serine amidically linked to the carboxyl group. The K54 polysaccharide has a molecular weight of approximately 160,000, corresponding to approximately 380 repeating-units.

Amino Acids↗

Structure of the fructose-containing K52 capsular polysaccharide of uropathogenic Escherichia coli O4:K52:H-.

The chemical structure of the K52 antigenic capsular polysaccharide (K52 antigen) of Escherichia coli O4:K52:H- was elucidated by composition, nuclear magnetic resonance spectroscopy, methylation, periodate oxidation before and after graded acid hydrolysis and by oligosaccharide analysis. The polysaccharide consists of a backbone of alpha-galactose units interlinked between C1 and C3 by phosphodiester bridges. This poly(alpha-galactosyl-phosphate) is substituted at C2 of each galactose unit by beta-fructofuranose residues. About 80% of the galactose units are O-acetylated at C4 and about 10% of the fructose units are both O-acetylated and O-propionylated at C1. The K52 polysaccharide has an average molecular mass of 34 kDa, thus consisting of approximately 65 fructosyl-galactosyl-phosphate repeating units.

Antigens, Bacterial↗

Abnormal radiofurosemide binding by Tamm Horsfall glycoprotein of diabetic patients.

In the present study, 8 Type 1 diabetic patients with normal creatinine clearance and 8 matched controls were examined. Tamm Horsfall glycoprotein was isolated with the NaCl precipitation procedure. Its purity was checked by gel-electrophoresis, immunodiffusion and isoelectric focussing. Tamm Horsfall glycoprotein of diabetic patients had higher glucose (p less than 0.05) and lower N-acetylneuraminic acid content (p less than 0.01) than controls. 14C-furosemide binding by Tamm Horsfall glycoprotein was examined using an Amicon ultrafiltration system at 0 degree C. In nominally sodium-free medium, furosemide binding by Tamm Horsfall glycoprotein was significantly (p less than 0.01) higher in diabetic patients than in matched controls. The increment of binding capacity with sodium was similar in controls and diabetic patients so that maximal binding capacity in a NaCl system was 1.7 +/- 0.3 in controls and 3.64 +/- 0.5 in diabetic patients (p less than 0.025). Half maximal furosemide binding by Tamm Horsfall glycoprotein occurred at 1.4 +/- 0.2 mmol Na/l in controls and 0.52 +/- 0.12 in diabetic patients (p less than 0.01). Abnormal radiofurosemide binding of Tamm Horsfall glycoprotein of diabetic patients may be the consequence of abnormal postribosomal modification of the glycoprotein which is synthesized in an insulin- and glucose-sensitive nephron segment.

Adult↗

Effect of a lysolecithin analogue on nonspecific resistance to infection of mice.

The effect of racemic 1-octadecyl-2-methoxy-sn-glycero-3 phosphorylcholine (ET-18-OCH3) on the nonspecific resistance of mice to infection with Salmonella typhimurium was investigated. Two S. typhimurium strains with different virulence were studied and no effect was observed in either case at concentrations of ET-18-OCH3 up to 100 micrograms/mouse. However, a concentration of 500 micrograms/mouse caused decreased resistance to S. typhimurium, correlating with a depression of carbon clearance. Treatment of macrophages with ET-18-OCH3 in vitro inhibited phagosome-lysosome fusion, but had no effect on zymosan-induced luminol-dependent chemiluminescence. The relationship between the adjuvant and nonspecific anti-infectious activity of ET-18-OCH3 and other compounds is discussed.

Animals↗

Monoclonal antibodies to enterobacterial common antigen and to Escherichia coli lipopolysaccharide outer core: demonstration of an antigenic determinant shared by enterobacterial common antigen and E. coli K5 capsular polysaccharide.

We established hybridoma cell lines producing monoclonal antibodies against enterobacterial common antigen (ECA) and a substructure of the outer core of different Escherichia coli lipopolysaccharides (LPSs). Anti-ECA antibodies 865 and 898 reacted with ECA in extracts of heated E. coli and with ECA-bound R1 and R4 core-containing LPS preparations, as well as with a purified sample of ECA from Salmonella montevideo. Antibody 865, but not antibody 898, cross-reacted with K5 capsular polysaccharide, suggesting that 4-linked alpha-N-acetylglucosamine is part of an antigenic determinant shared by both K5 polysaccharide and ECA. Anti-LPS antibody 786 recognized an outer core structure common to E. coli K-12, B, R2, and R4 core type LPS, but not to R1 and R3 core type LPS. Its most probable target is the trisaccharide sequence Hexp(1----2)-alpha-D -Glcp(1----3) alpha-D-Glcp----(Hepp) (where Hex is hexose, p is phosphate, Glc is glucose, and Hep is heptose), the first glucose being the immunodominant moiety. These monoclonal antibodies may be used not only for the detection of ECA, K5, and LPS core structures but also for analysis of the molecular forms resolved on polyacrylamide gels (banding patterns) of both ECA and LPS, independently of one another.

Antibodies, Monoclonal↗

Biosynthesis of the 09 antigen of Escherichia coli. Core structure of rfe mutant as indication of assembly mechanism.

The chemical structure of the outer (hexose) regions of the core oligosaccharide from Escherichia coli 09 with the complete R1 core, and from a R1-derived rfe mutant were analyzed using compositional analysis, methylation and gas chromatography/mass spectrometry. It was found that, in contrast to the branched outer region of the R1 core, the outer region of the core from the rfe mutant lacked terminal glucose and was linear. These results are in agreement with recent findings on the biosynthesis of the 09 antigen. They suggest a cotransfer of glucose with the 09-specific mannan to a 'pre-core' lacking terminal glucose, as the assembly (translocation) step in the 09 antigen synthesis. Thus it is suggested that the initiation of O-chain synthesis (by the formation of an acceptor glucolipid ) and the termination of core synthesis are closely correlated. In conjunction with previous biochemical data, the analytical results presented here indicate a novel core synthesis.

Antigens, Bacterial↗

Structural studies of the O-specific side chain of the lipopolysaccharide from Escherichia coli O:7.

The structure of the O-specific side-chain of the lipopolysaccharide from Escherichia coli O:7 has been investigated, using n.m.r. spectroscopy, methylation analysis, partial hydrolysis, and Smith degradation as the principal methods. It is concluded that the polysaccharide is constructed of repeating pentasaccharide units having the structure (formula; see text) where D-QuipNAc stands for 4-acetamido-4,6-dideoxy-D-glucopyranose. The 13C-n.m.r. spectrum of the polysaccharide has been interpreted completely.

Carbohydrate Conformation↗

Escherichia coli O18ac antigen: structure of the O-specific polysaccharide moiety.

The O-specific polysaccharide moiety (O18ac polysaccharide) of the O18ac antigen (lipopolysaccharide) from Escherichia coli 2980 (O18ac:K5:Fim+:H-) was isolated in pure form by degradation of the lipopolysaccharide and chromatography on Sephadex G-50. The primary structure of the O18ac polysaccharide was elucidated by composition, fragmentation procedures, methylation analysis, and nuclear magnetic resonance spectroscopy. The polysaccharide consists of repeating units of the pentasaccharide: (formula; see text) which are joined in the polymer by alpha-1,2 linkages.

Antigens, Bacterial↗

Cell-wall lipopolysaccharide of the urinary-tract-infective Escherichia coli 04:K12:H-. Structure of the polysaccharide chain.

The O-specific polysaccharide moiety (04 polysaccharide) of the 04 antigen (lipopolysaccharide) from Escherichia coli 04:K12:H- was isolated in pure form by degradation of the lipopolysaccharide and chromatography on Sephadex G-50. The primary structure of the 04 polysaccharide was elucidated by composition, Smith degradation, nuclear magnetic resonance spectroscopy, methylation and oligosaccharide analysis. Oligosaccharides were obtained by deaminating fragmentation of partially and completely de-N-acetylated polysaccharides. The polysaccharide consists of repeating units of the pentasaccharide (formula; see text) which are joined in the polymer through alpha-1, 4-linkages. The 04 polysaccharide has a mean molecular mass of 13800 Da and consists of the core oligosaccharide and about 14 pentasaccharide repeating units.

Carbohydrate Conformation↗

Structure of the 3-deoxy-D-manno-octulosonic acid-(KDO)-containing capsular polysaccharide (K14 antigen) from Escherichia coli 06:K14:H31.

The chemical structure of the K14-antigenic polysaccharide (K14 antigen) of Escherichia coli 06:K14:H31 was elucidated by determination of the composition, 1H- and 13C-n.m.r. spectroscopy, periodate oxidation, and study of the oligosaccharides obtained by partial hydrolysis. The polysaccharide consists of [O-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-(1 leads to 5)-O-(3-deoxy-beta-D-manno-octulopyranosylonic acid)-(2 leads to 6)] repeating units, approximately 60% of the octonic acid units being O-acetylated and approximately 10% O-propionylated at O-8. The sequence of acetylated and propionylated residues is not known. The serologically-specific part of the K14 antigen residues in the polysaccharide part.

Bacterial Capsules↗

Cell-wall lipopolysaccharide of Escherichia coli 0114:H2. Structure of the polysaccharide chain.

The O-specific polysaccharide of the 0114 antigen (lipopolysaccharide) of Escherichia coli 0114 and oligosaccharides obtained from it by Smith degradation and hydrogen fluoride solvolysis were analyzed, using proton and 13C nuclear magnetic resonance spectroscopy and methylation. The results indicated that the 0114 polysaccharide has the tetrasaccharide repeating unit alpha-N-acetylglucosamine(1 leads to 4) beta-3,6-dideoxy-3-(N-acetyl-L-seryl)aminoglucose(1 leads to 3) beta-ribofuranose(1 leads to 4)galactose. In the polysaccharide the repeating units are joined through beta 1 leads to 3-galactosyl linkages. This structure is compared with that of the serologically cross-reacting Shigella boydii 08 antigen and the serological similarity is discussed.

Cell Wall↗

Structure of the 2-keto-3-deoxy-D-manno-octonic-acid-containing capsular polysaccharide (K12 antigen) of the urinary-tract-infective Escherichia coli O4:K12:H-.

The primary structure of the K12 antigenic capsular polysaccharide (K12 antigen) of Escherichia coli O4:K12:H- was elucidated by composition, nuclear magnetic resonance spectroscopy, methylation, periodate oxidation and oligosaccharide analysis. The polysaccharide consists of repeating trisaccharide alpha-rhamnosyl-1,2-alpha-rhamnosyl-1,5-dOclA units (dOclA = 2-keto-3-deoxy-D-manno-octonic acid) which are joined through beta-2,3-linkages. About 50% of the dOclA units are O-acetylated at C7 or C8. The sequence of acetylated and non-acetylated dOclA residues is not known. As had been reported before, the polysaccharide is linked to a phosphatidic acid at the reducing end (dOclA) via a phosphodiester bridge. The serologically specific part of the K12 antigen is its polysaccharide moiety.

Antigens↗

Structure of the Escherichia coli K2 capsular antigen. Stereochemical configuration of the glycerophosphate and distribution of galactopyranosyl and galactofuranosyl residues.

The Escherichia coli K2 capsular antigen is known to be composed of alpha-D-galactopyranosyl(1--2)glycerophosphate and alpha-D-galactofuranosyl(1--2)glycerophosphate units which are connected by phosphodiester bonds to C-4 of the galactopyranosyl and C-5 or C-6 of the galactofuranosyl moieties. In the present study the glycerophosphates were released by two different procedures and shown to have the sn-glycero-3-phosphate stereochemical configuration. In the first, the chain was fragmented by Smith degradation to glycerophosphothreitol from which the glycerophosphate was released by alkali hydrolysis. The structure-dependent low recovery of alpha-glycerophosphate (less than 10%) initiated the development of another degradative sequence which consisted of periodate oxidation, beta elimination, hydrazinolysis, and alkaline treatment. This way, approximately 90% of the glycerophosphate was released as sn-glycero-3-phosphate. beta elimination revealed in addition that most of the galactofuranosyl residues carry the phosphodiester bond at position 5. Separation by gel permeation chromatography and analysis of the fragments obtained by beta elimination showed that pyranosidic and furanosidic galactosyl residues alternate in the same chain and suggested the sequences Galf(p)GroP-(GalpGroP)n-Galf- and -GalfGroP-(GalpGroP)n-Galf-, where n is 6, 4, and 3, respectively.

Antigens↗