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Pierwszorzędowa struktura antygenów O bakterii rodzaju Salmonella

Gajdus J., Głośnicka R., Szafranek J.

Wiadomości Chemiczne

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2006

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[Z] 60, 9-10

621-653

EN

Salmonella spp. are pathogenic Gram-negative bacteria that belong to Enterobacteriaceae family with lipopolysaccharide (LPS) as a constituent of cell wall. This is an integral component of the outer membrane of the wall. Salmonella smooth (S) forms produce LPS, which is composed of three parts, chemically bonded together viz. polysaccharide O-antigen, oligosaccharide core region and lipid A. Antigens O (O-PS) together with H flagella antigens are the foundation of serological classification of these bacteria. O-chain, which is built with up to 50 oligosaccharide repeating units, is one of the products of mild acidic hydrolysis of LPS. Due to the fact that polysaccharide antigens are the sites of specific antibody complexing, any difference in primary and secondary structures of O-antigens reflect serological specificity of bacteria. Taking this fact into consideration, we can distinguish about 2541 Salmonella serotypes with O and H antigenic formulas defined [4]. In this review we present 55 chemical structures of O-antigenic repeating units of Salmonella strains including their heterogeneity structures. The structures can have 22 different monosaccharide residues usually in 3 to 6 sugar repeating units. We describe here selected chemical and spectroscopic (MS, NMR) methods for primary structure examination of these bacterial O-PS. Enzymatic and immunochemical methods are also described. Cross-reactions of Salmonella spp. with any other bacteria or blood group A, B, 0 antigens are explained on the molecular level. Thus, structural assignments of somatic antigens of Salmonella spp. allow us to understand the molecular level of the classification system of these bacteria.

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Structure of the Polysaccharide O-Antigen of Salmonella Aberdeen (O : 11)

Szafranek J., Kaczyńska M., Kaczyński Z., Gajdus J., Czerwicka M., Dziadziuszko H., Głośnicka R.

Polish Journal of Chemistry

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2003

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Vol. 77 / nr 9

1135-1140

EN

O-specific polysaccharide (OPS) of Salmonella Aberdeen was obtained from bacterial cell mass by water-phenol extraction procedure of lipopolysaccharide (LPS) followed by its mild acid hydrolysis and gel filtration of soluble carbohydrate material. Rhamnose, galactose, N-acetyl-glucosamine and mannose were detected and their linkages were established. Sugar configurations, D or L, were determined for (S)-(+)-2-butyl glycosides on an achiral capillary column. The structure of OPS was determined by analysis of spectra of 1H and 13C NMR and homonuclear and heteronuclear correlations spectra. Anomeric configurations were tentatively assigned by chromium trioxide oxidation and later proved by anomeric proton chemical shifts, H1-H2 coupling constants and proton coupled 13C spectra. Sugar sequences were established from comparisons of specific carbon shifts with those from literature, two-dimensional nuclear Overhauser effect spectroscopy (NOESY) and heteronuclear multiple-bond correlation experiments (HMBC). The repeating unit of S. Aberdeen OPS has the structure: _3)-_-D-GlcpNAc-(1_3)-[ _-D-Manp-(1_4)-]_-D-Galp-(1_4)-_-L-Rhap-(1_

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Cyclic Analogue of Human Heat Shock Protein 70(29-42) Fragment. Synthesis, Conformational Studies and Evaluation of Its Immunogenicity

Karawajczyk B., Wirkus-Romanowska I., Wysocki J., Rolka K., Maćkiewicz Z., Głośnicka R., Kupryszewski G.

Polish Journal of Chemistry

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2001

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Vol. 75, nr 2

265-273

EN

The cyclic hexadecapeptide containing human heat shock protein 70(29-42) fragment cyclized by the disulfide bridge between two L-cysteine residues introduced at the N- and C-termini was synthesized by the solid phase method. It was established that the cyclic analogue, contrary to its linear counterpart, had much lower ability to generate immune response in rabbits. Conformational studies of cyclic peptide performed using 1D and 2D 1H-NMR spectroscopy in conjunction with theoretical conformational analysis revealed that the cyclization constrained the 3D structure of this peptide, reflected by the observed rate of cis/trans isomerization of Arg9-Thr10 peptide bond and the presence of Gly7-Asn8 peptide bond in cis geometry.We, therefore, postulate that the conformational flexibility in the case of Human Heat Shock Protein fragments is a key element for their immunogenicity.

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Synthesis of human heat shock protein 70 (29-42) fragment and evaluation of its immunogenicity

Karawajczyk B., Wysocki J., Kunikowska D., Maćkiewicz Z., Głośnicka R., Korzeniowski A., Górski J., Kupryszewski G.

Polish Journal of Chemistry

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1998

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Vol. 72, nr 6

1017-1020

EN

The 29-42 fragment of human heat shock protein 70 (hsp 70) was synthesized by the solid phase method. As determined by enzyme-linked immunosorbent assay (ELISA), the synthetic hsp 70(29-42) peptide generated relatively strong immune response in immunized rabbits. Antibody titers were comparable with anti hsp 70 antibody serum level that was induced by immunization with recombinant protein (hsp 70). It was established that antibodies directed against hsp 70(29-42) peptide could be applied in ELISA for detecting hsp 70 in body fluids and tissues.

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Synthesis of hepatitic C virus protein fragments and evaluation of their immunogenicity

Karawajczyk B., Maćkiewicz Z., Kunikowska D., Dziadziuszko H., Dera-Tomaszewska B., Głośnicka R., Kupryszewski G.

Polish Journal of Chemistry

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1998

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Vol. 72, nr 1

84-88

EN

Three polypeptide fragments of Hepatitis C virus protein (130-140)C, (133-142)C and (1406-1415)NS3 were synthesized using the solid-phase method. The immunogenicity of the peptides was tested on rabbits. All the peptides studied revealed homoral and cell response.

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Synthesis of flagellin fragments and studies of their interactions with antibodies. Part 1

Klugmann K., Kunikowska D., Głośnicka R., Maćkiewcz Z.

Polish Journal of Chemistry

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1998

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Vol. 72, nr 9

2093-2097

EN

Three polypeptide fragments of flagellin protein were synthesized using the solid-phase method. The immunogenicity of the peptides was tested. All the peptides exhibit high immunonological activity.