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Z Sidorczyk

Publications and source records attributed to Z Sidorczyk.

At least 37 records · Page 2Linked to original sources
PubMed1997

Potential virulence factors of Proteus bacilli.

The object of this review is the genus Proteus, which contains bacteria considered now to belong to the opportunistic pathogens. Widely distributed in nature (in soil, water, and sewage), Proteus species play a significant ecological role. When present in the niches of higher macroorganisms, these species are able to evoke pathological events in different regions of the human body. The invaders (Proteus mirabilis, P. vulgaris, and P. penneri) have numerous factors including fimbriae, flagella, outer membrane proteins, lipopolysaccharide, capsule antigen, urease, immunoglobulin A proteases, hemolysins, amino acid deaminases, and, finally, the most characteristic attribute of Proteus, swarming growth, enabling them to colonize and survive in higher organisms. All these features and factors are described and commented on in detail. The questions important for future investigation of these facultatively pathogenic microorganisms are also discussed.

Bacterial Outer Membrane Proteins↗
PubMed1997

Structural and immunochemical studies on the O-specific polysaccharide of Proteus penneri strain 15.

On the basis of sugar analysis and 1H- and 13C-NMR spectroscopy, it was shown that the O-specific polysaccharide of Proteus penneri strain 15 has a trisaccharide repeating unit, including an acetal-linked pyruvic acid residue, and is structurally identical to the capsular polysaccharide of Proteus vulgaris strain ATCC 49990. Serological studies supported this conclusion and demonstrated the presence in the homological antiserum of both anti-core and anti-O chain antibodies reacting with a lipopolysaccharide (LPS) epitope containing N-acetylglucosamine and galactose residues.

Animals↗
PubMed1997

The influence of iron occurring in the growth medium of Staphylococcus aureus on the bacterial adhesion to collagen.

The aim of this study was to investigate the influence of iron present in the growth medium of Staphylococcus aureus on the bacterial adhesion to collagen. The experiments were extended to determinate the siderophore production and to examine the S. aureus isolates surface hydrophobicity. The addition of iron to metal deficient defined medium causes the change in hydrophobicity of the examined S. aureus strains surfaces from hydrophilic to hydrophobic. The presence of iron in staphylococcal growth medium alters also the adhesion to the surface covered with collagen. Four out of six S. aureus strains adhere to collagen weaker when cells come from iron-rich medium. Majority of tested strains produce markedly less of siderophores in media containing the excess of iron (1 and 10 microM Fe) and there is no staphylococcal siderophore activity in the growth medium with a very high concentration of this compound (120 microM Fe). The obtained results indicate that the iron-stressed conditions influence the staphylococcal adhesion to collagen.

Bacterial Adhesion↗
PubMed1997

[The influence of temperature on culture of Staphylococcus aureus for cell adhesion to collagen].

The aim of this study was the investigation of adhesion of 88 S. aureus clinical isolates to collagen. The experiments were extended to determine the influence of growth temperature on collagen adhesin-collagen interaction. Bacterial adhesion to collagen was estimated by using immunoenzymatic assay at absorbance of 492 nm and compared with standard curves obtained for 8 different densities of each strain. The amount of collagen adhesin was indicated by colour reaction intensity measured by immunoenzymatic assay. Hydrophobicity of S. aureus strains was measured by aggregation in (NH4)2SO4 test. Almost all S. aureus strains isolated from bone and joint infections adhered to collagen whereas only a part of soft tissue infections isolates showed this feature. The comparison of adhesive properties of S. aureus cells cultured at 21 degrees C, 37 degrees C and 42 degrees C did not make it possible to indicate the optimal culture temperature for S. aureus adhesion to collagen. However, the intensive colour reaction of cells cultured at 37 degrees C with anti-collagen adhesin antibodies proves the production of the highest amount of this adhesin under the mentioned conditions. The influence of growth temperature as well as solid and/or liquid medium on the change of S. aureus hydrophobic properties was not observed. The obtained results show that the S. aureus growth temperature can be one of the factors influencing the staphylococci cells adhesion to collagen.

Bacterial Adhesion↗
PubMed1996

Structure of a new N-acetylisomuramic acid-containing O-specific polysaccharide of Proteus penneri strains 19 and 35.

O-Specific polysaccharides, together with oligosaccharide products of their degradation, were isolated by GPC after mild acid delipidation of lipopolysaccharides of Proteus penneri strains 19 and 35. The polysaccharides had the same trisaccharide repeating unit containing one residue each of D-galactose, 2-acetamido-2-deoxy-D-glucose, and 2-acetamido-3-O-[(S)-1-carboxyethyl]-2-deoxy-D-glucose (N-acetylisomuramic acid). On the basis of 1D and 2D 1H and 13C NMR spectroscopy, including 2D correlation spectroscopy (COSY), rotating-frame NOE spectroscopy (ROESY), and H-detected heteronuclear 1H,13C multiple-quantum coherence (HMQC), the following structure of the repeating unit was established: [formula: see text]. The oligosaccharide products formed by cleavage of the glycosidic linkage of GlcNAc represent a chemical trisaccharide repeating unit of the polysaccharide and its oligomer homologs. The ease of hydrolysis of the polysaccharide is associated with the closeness of the glycosyl group and the lactic acid residue in N-acetylisomuramic acid. The polysaccharides studied are structurally related to the O-specific polysaccharides of P. penneri strains 62 and 71 studied by us earlier.

Carbohydrate Conformation↗
PubMed1996

The structure of the O-specific polysaccharide of Proteus penneri 52.

An acidic O-specific polysaccharide isolated from Proteus penneri 52 contains D-galacturonic acid, 2-acetamido-2-deoxy-D-glucose, and 2-acetamido-2-deoxy-D-galactose in the ratio 1:2:2. On the basis of sugar analysis and NMR spectroscopy, which included one-dimensional TOCSY, two-dimensional COSY, heteronuclear 13C, 1H-COSY, and rotating-frame NOE spectroscopy, the following structure of the pentasaccharide repeating unit of the O-specific polysaccharide was established: [sequence: see text] Cross-reactivity of the anti-P-penneri 52 O-serum with other strains of P. penneri isolated in Germany. Poland, USA, and Canada is discussed and a new Proteus serogroup is proposed.

Carbohydrate Conformation↗
PubMed1996

Structure of the O-specific polysaccharide chain and serological characterization of the Proteus penneri 62 lipopolysaccharide compared with the lipopolysaccharides of the P. penneri strains.

The chemical structure of the O-specific polysaccharide chain of Proteus penneri 62 lipopolysaccharide (LPS) containing N-acetylisomuramic acid was established using acid hydrolysis, solvolysis with anhydrous hydrogen fluoride and 1H and 13C NMR spectroscopy. Cross reactivity of the anti-O-serum P. penneri 62 with a number of other strains of the same species isolated in the USA, Canada, Germany and Poland is discussed.

Carbohydrate Sequence↗
PubMed1995

Structure and epitope specificity of the O-specific polysaccharide of Proteus penneri strain 12 (ATCC 33519) containing the amide of D-galacturonic acid with L-threonine.

O-specific polysaccharide was isolated from Proteus penneri strain 12 (ATCC 33519) lipopolysaccharide (LPS) and studied using NMR spectroscopy, including selective spin-decoupling, one-dimensional NOE, two-dimensional homonuclear correlation spectroscopy, 13C,1H heteronuclear correlation spectroscopy and chemical methods (O-deacetylation, Smith degradation, partial acid hydrolysis followed by borohydride reduction and methylation). The amide of D-galacturonic acid with L-threonine [D-GalA(L-Thr)] was identified as a constituent of the polysaccharide and the following structure of the tetrasaccharide repeating unit was established: [formula: see text] where the degree of O-acetylation at either position varies over 20-40%. Serological study with LPS, its degradation products and related synthetic glycoconjugates (2-acrylamidoethyl glycosides of amides of alpha-D-GalA with L-amino acids copolymerised with acrylamide) showed that D-GalA(L-Thr) plays an important role in manifesting the serological specificity of the P. penneri 12 O-antigen. Serological cross reactions between LPSs of P. penneri 12 and Proteus mirabilis S1959, R14/S1959 (transient-like form), O23 and O28 are discussed.

Amides↗
PubMed1994

Effect of lipopolysaccharide (LPS) chain length on interactions of bactericidal/permeability-increasing protein and its bioactive 23-kilodalton NH2-terminal fragment with isolated LPS and intact Proteus mirabilis and Escherichia coli.

The target-specific cytotoxicity for gram-negative bacteria and the endotoxin-neutralizing activity of the 55-kDa bactericidal/Permeability-increasing protein (BPI) and its bioactive 23-kDa NH2-terminal fragment depend on the strong attraction of BPI for the lipid A region of lipopolysaccharides (LPS). We have shown before that smooth gram-negative bacteria with long-chain LPS are more resistant to BPI (especially holo-BPI) than are rough strains. It has been suggested that the high BPI resistance of some gram-negative bacteria, such as Proteus mirabilis, might also reflect the structural diversity of lipid A. To explore this possibility, we compared the antibacterial activity and binding of natural and recombinant holo-BPI and a recombinant NH2-terminal fragment (rBPI-23) to an isogenic rough (Re-LPS chemotype) and a smooth (S-LPS chemotype) strain of P. mirabilis and to LPS isolated from the two strains. Holo-BPI and rBPI-23 were both potently active against the Re strain of P. mirabilis (90% lethal dose, 20 nM). In contrast, the smooth strain was > or = 100 times more resistant to holo-BPI but only 10 times more resistant to rBPI-23. rBPI-23 was also more potent against several Escherichia coli strains from clinical bacteremia isolates. Differences in the antibacterial potency of BPI toward the Re and S strains of P. mirabilis correlated with differences in the binding of holo-BPI and rBPI-23 to these bacteria. In contrast, the binding of biosynthetically (in vitro transcribed and translated) 35S-labeled holo-BPI and NH2-terminal fragment to isolated Re- and S-LPS from P. mirabilis in solution was similar. Moreover, in the Limulus amebocyte lysate assay, holo-BPI and rBPI-23 potently neutralized both forms of LPS with equal effectiveness. Together, these results strongly suggest that BPI recognizes Proteus lipid A and that the relative resistance of (smooth) P. mirabilis to holo-BPI is due to the inhibitory effect of long polysaccharide chains of tightly packed LPS in the envelope.

Antimicrobial Cationic Peptides↗
PubMed1994

Structural and immunochemical studies on O-specific polysaccharide of Proteus penneri strain 14.

The complete structure of the O-antigen of Proteus penneri strain 14, containing D-alanine and L-alanine was established using methylation, solvolysis with anhydrous hydrogen fluoride, partial acid hydrolysis, 1H- and 13C-NMR spectroscopy. The role of partial structures of the pentasaccharide repeating unit in manifesting serological specificity and cross-reactivity of this strain with some other bacteria is discussed.

Alanine↗
PubMed1993

Analysis of antibiotic resistance determinants in Proteus penneri.

The plasmid profiles of 65 strains of Proteus penneri were analyzed to determine whether resistance was determined chromosomally or by plasmids. Only seven strains harboured one to three plasmids, although these strains exhibited resistance to a wide range of antibiotics. Markers for ampicillin and tetracycline resistance could be transferred to Escherichia coli by transformation. Plasmids carried resistance to chloramphenicol in two strains and resistance to sulfonamides in one strain. The result showed that resistance is determined chromosomally rather than by plasmids, however the possibility that these bacteria may acquire resistance plasmids which change their antibiotic susceptibility pattern cannot be excluded.

Chloramphenicol Resistance↗
PubMed1993

[Further types of core lipopolysaccharides in Proteus].

Comparative analysis of the chemical composition of 11 core oligosaccharides isolated from lipopolysaccharides of the wild (S) and phenotypically rough (R) strains Proteus mirabilis (nine) and Proteus vulgaris (two) allowed to recognize three new types Proteus core, classified as IV, V, VI. All of them contained D-galactose and D-galactosamine in addition to common core constituents: D-glucose, D-galacturonic acid, L-glycero-D-manno-heptose, KDO, EtN described for Proteus core types I, II, III (6, 7, 8). D-glucosamine was characteristic for Proteus core type VI whereas D-glycero-D-manno-heptose for types V and VI.

Oligosaccharides↗
PubMed1993

[Selected properties of strains of a new species of Proteus penneri from the second American collection].

The second collection of the novel species Proteus penneri consists of 25 strains from which only two have shown rough from properties in the tests differentiating S and R variants of bacteria. The migration pattern of their lipopolysaccharides in gel electrophoresis was leader-like, typical for smooth organisms. 13 out of 25 lipopolysaccharide preparations showed strong-reactivity with anti-0 sera in semi-quantitative precipitation test. Serological similarity between the strains within species Proteus penneri is discussed.

Electrophoresis, Agar Gel↗
PubMed1993

[Isolation and certain biological and immunologic properties of Proteus penneri strains from the European collection].

The American Collection of 45 Proteus penneri strains was supplemented by 22 strains isolated in Poland and Germany. All strains exhibited typical smooth forms of bacteria. Susceptibility to antibiotics was determined and compared with the other P. penneri strains. 0-antigenic relatedness and serological similarity between strains in the whole Proteus penneri collection were discussed.

Drug Resistance, Microbial↗
PubMed1993

[Immunochemical studies of O-specific polysaccharide of Proteus penneri 42 lipopolysaccharide].

O-specific polysaccharide was obtained an mild acid degradation of Proteus penneri strain 42 lipopolysaccharide and found to contain D-glucose, D-galacturonic acid and 2-acetamido-2-deoxy-D-glucose in molar ratio 2:1:1. Methylation analysis showed that the polysaccharide is linear, one of the glucose residue is substituted at position 2, the second one and the residue of galacturonic acid at position 4, and the 2-acetamido-2-deoxy-D-glucose residue at position 3. On the basis of non-destructive NMR analysis the following structure of repeat unit of the O-specific polysaccharide was established and confirmed independently by methylation analysis: -2)-beta-D-Glc-(1-->4)-beta-D-Glc-(1-->3)-beta-D-GlcNAc-(1-->4)-al fa-D-GalA-(1--> The serological investigation with application of P. penneri strain 42 anti O-serum has shown the activity of homologous preparations of LPS and PS, as well as cross-reactions with heterologous lipopolysaccharides from other Proteus strains.

Immunochemistry↗