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1

Activation Limulus amebocyte by endotoxins

100%
Kaca W.
Postępy Higieny i Medycyny Doświadczalnej
|
1996
|
vol. 50
|
issue 5
447-457
EN
Limulus amebocyte lysate (LAL) test is commonly used for the detection of trace amounts of endotoxins (lipopolysaccharides, LPS). The mechanisms, LPS structural requirements and limitations of LAL tests are presented.
2

Neutrophile activation by bacterial endotoxins

63%
Klink M., Kaca W.
Postępy Higieny i Medycyny Doświadczalnej
|
1996
|
vol. 50
|
issue 4
333-350
EN
The endotoxin (lipopolysaccharide, LPS), major component of Gram-negative bacteria cell wall, activate numerous types of cells, neutrophile included. The chemical compositions of polysaccharide (O-specific polysaccharide and core oligosaccharide) and hydrophobic lipid A parts of LPS are presented. The bindings of LPSs to neutrophiles resulted in signal transduction and neutrophiles activation. Neutrophiles, under LPS stimulation, generate oxygen radicals, nitric oxide and other components of inflammatory processes.
3

Serological studies of cross-reactions between strains of Proteus mirabilis OXK (PrO 10/52) and Proteus mirabilis S1959

51%
Swierzko A., Cedzynski M., Ziolkowski A., Kaca W.
Postępy Higieny i Medycyny Doświadczalnej
|
1996
|
vol. 50
|
issue 5
507-509
EN
Strong cross-reactions are described between Proteus mirabilis strains having the same structures of repeating units of their O-specific polysaccharides. These strains are used in routine diagnosis of ricketsiae.
4

Structure and serological characterization of an N-[(R)-1-carboxyethyl]-L- -lysine-containing the O-chain of the lipopolysaccharide of Proteus mirabilis O13

39%
Swierzko A. A., Cedzynski M., Ziolkowski A., Senchenkova S. N., Perepelov A. V., Knierel Y. A., Kaca W.
Archivum Immunologiae et Therapiae Experimentalis
|
2001
|
vol. 49
|
issue 2
163-170
EN
In this paper we present the structure and describe serological properties of the O-specific polysaccharide of Proteus mirabilis O13 lipopolysaccharide, which contains a unique component, an amide of D-galacturonic acid (D-GalA) with an unusual amino acid N-[(R)-1-carboxyethyl]-L-lysine (alaninolysine, AlaLys). Selective chemical degradations of either GalA or AlaLys resulted in the loss of the serological reactivity of the polysaccharide with anti-O serum against P. mirabilis O13. Neither synthetic stereoisomers of AlaLys nor the isolated amide of GalA with AlaLys inhibited the reaction of the O-antiserum with the homologous lipopolysaccharide. The O-antiserum did not cross-react with the lipopolysaccharide of Providencia alcalifaciens O23 containing an amide of D-glucuronic acid with AlaLys. These data showed that both uronic acid and amino acid components of the amide play an important role in manifesting the P. mirabilis O13-specificity, but the full specific epitope also includes also another OPS component(s). A cross-reactivity of anti-O13 serum with some other P. mirabilis strains was observed and attributed to a common heat-stable antigen(s) different from the lipopolysaccharide.
5

Immunochemical studies on the O-antigens of Proteus mirabilis O23 and Proteus vulgaris O23

39%
Rozalski A., Perepelov A. V., Bartodziejska B., Senchenkova S. N., Babicka D., Kaca W., Knirel Y. A.
Archivum Immunologiae et Therapiae Experimentalis
|
2003
|
vol. 51
|
issue 1
69-73
EN
Analysis by 1H and 13C nuclear magnetic resonance (NMR) spectroscopy demonstrated that the O-specific polysaccharides of P. mirabilis PrK 42/57 and P. vulgaris PrK 43/57 are structurally similar to that of P. vulgaris PrK 44/57 and different from the polysaccharide of P. mirabilis PrK 41/57 studied earlier. The lipopolysaccharides of these strains were tested using enzyme immunosorbent assay, passive hemolysis and Western blot with O-antisera against P. mirabilis 42/57 and P. vulgaris 43/57 and 44/57, as well as with cross-absorbed O-antisera. The chemical and serological data revealed the basis for combining the four strains into Proteus serogroup O23 and division of this serogroup to three subgroups, one for P. vulgaris 43/57 and 44/57 and two others for P. mirabilis 41/57 and 42/57.
6

Structures and serology of the O-antigens of Proteus strains classified into serogroup O17 and former serogroup O35

33%
Torzewska A., Grabowski S., Kondakova A. N., Toukach F. V., Senchenkova S. N., Shashkov A. S., Arbatsky N. P., Knirel Y. A., Rozalski A., Kaca W.
Archivum Immunologiae et Therapiae Experimentalis
|
2006
|
vol. 54
|
issue 4
277-282
EN
Introduction: Bacteria of the genus Proteus are facultative pathogens which commonly cause urinary tract infections. Based on the serological specificity of the O-chain polysaccharide of the lipopolysaccharide (O-polysaccharide, O-antigen), strains of P. mirabilis and P. vulgaris have been classified into 60 serogroups. Studies on the chemical structure and serological specificity of the O-antigens aim at the elucidation of the molecular basis and improvement of the serological classification of these bacteria. Materials and Methods: The O-polysaccharide was prepared by acetic acid degradation of the lipopolysaccharide isolated from dried bacterial mass of each strain by hot phenol/water extraction. 1H- and 13C-NMR spectroscopy was used for structural studies. Serological studies were performed with rabbit O-antisera using enzyme immunosorbent assay, passive hemolysis test, and the inhibition of reactions in these assays as well DOC-PAGE and Western blot. Results: Four Proteus strains belonging to serogroups O17 and O35 were found to possess similar O-polysaccharide structures, in particular having the same carbohydrate backbone built up of tetrasaccharide repeating units. However, they differ in the presence or absence of additional substituents, such as phosphoethanolamine in P. mirabilis O17 and glucose in P. penneri O17, as well as in the pattern and degree of O-acetylation of various monosaccharide residues. Serological studies also showed close relationships between the O-antigens studied. Conclusions: Based on these data it is proposed to reclassify strain P. mirabilis PrK 61/57, formerly representing the O35 serogroup, into the serogroup O17 in the Kauffman-Perch classification system of Proteus.
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