Structure of the acidic O-specific polysaccharide from Proteus vulgaris O39 containing 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-non-2-ulosonic acid.

The O-specific polysaccharide of Proteus vulgaris O39 was found to contain a new acidic component of Proteus lipopolysaccharides, 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-non-2-ulosonic acid (di-N-acetylpseudaminic acid, Pse5Ac7Ac). The following structure of the polysaccharide was determined by NMR spectroscopy, including 2D 1H,(1)H COSY, TOCSY, ROESY, and 1H,(13)C HMQC experiments, along with selective cleavage of the polysaccharide by solvolysis with anhydrous trifluoromethanesulfonic (triflic) acid: -->8)-beta-Psep5Ac7Ac-(2-->3)-alpha-L-FucpNAc-(1-->3)-alpha-D-GlcpNAc-(1--> The structure established is unique among the O-specific polysaccharides, which is in accordance with classification of the strain studied into a separate Proteus serogroup.

[Tests for studying invasive properties of selected Proteus mirabilis strains]. / Badanie wlasciwosci inwazyjnych wybranych szczepów Proteus mirabilis.

Proteus mirabilis is an important pathogen of the urinary tract infections (UTI). Lipopolysaccharide (LPS, endotoxin) is one of the pathogenic factors of pathogenicity of these bacteria. In this paper we described the invasion of L929 mouse fibroblasts by P. mirabilis strains, classified into the O10, O23, O30, O43 serogroups. The maximal invasiveness was observed between 4-6 hours of incubation of the tested cells with bacteria. The cytotoxic effect slightly increased with the incubation time, probably as a result of the production of HpmA hemolysin. Incubation of L929 fibroblasts with LPS led to decrease of bacterial invasiveness. We observed that with the time of incubation of L929 cells with LPS (2-22 h), the invasiveness decreased (longer incubation time with LPS--weaker penetration).

Structure of a new acidic O-antigen of Proteus vulgaris O22 containing O-acetylated 3-acetamido-3,6-dideoxy-D-glucose.

The acidic O-specific polysaccharide of Proteus vulgaris O22 was studied using 1H and 13C NMR spectroscopy, including 2D COSY, TOCSY, NOESY, and H-detected 1H, 13C heteronuclear multiple-quantum coherence (HMQC) experiments, and the following structure for the branched pentasaccharide repeating unit was established: [sequence: see text] where Qui3NAc is 3-acetamido-3,6-dideoxyglucose, O-acetylation of QuiNAc at position 4 is stoichiometric and at position 2 nonstoichiometric. Serological relationships of P. vulgaris O22 with some other Proteus strains were substantiated on the level of the O-antigen structures.

[The influence of temperature on culture of Staphylococcus aureus for cell adhesion to collagen]. / Wplyw temperatury hodowli Staphylococcus aureus na przyleganie komórek do kolagenu.

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.

[Characterization of hemolytic activity of Proteus penneri]. / Charakterystyka aktywnosci hemolitycznej Proteus penneri.

Bacteria belonging to the genus Proteus synthesise two kinds of hemolysins HpmA and HlyA which represent "RTX proteins". In previous papers we described the production of an extracellular HlyA hemolysin by some P. penneri strains. Now we are reporting on the synthesis by P. penneri, typical for P. mirabilis HpmA hemolysin. There were identified two P. penneri strains 5 and 37 in which both hpmA and hlyA regions are present. In two other strains P. penneri 13 and 44 only hlyA region was found, whereas in strain P. penneri 42 operon hpmA was identified. The production of HpmA hemolysin was revealed in the cases of P. penneri 5, 42 and P. mirabilis 03 and 1959. The dynamics of HlyA hemolysin synthesis by P. penneri 44 was also investigated and its highest activity was observed during logarithmic phase of growth of bacterial culture. HlyA hemolysin was isolated from culture filtrate by precipitation with polyethylene glycol 4000. The invasiveness of HpmA+ and/or HlyA+ P. penneri strains was also checked by use of mouse L929 fibroblasts. Both kinds of strains were able to penetrate tested cells. The invasion of L929 fibroblasts by strains producing HlyA hemolysin is accompanied by cytotoxic effect.

Some biological features of proteus bacilli. 3. Comparison of haemolytic activity of Proteus and Serratia strains.

The haemolytic activity of Proteus mirabilis and P. vulgaris bacilli exhibited in young broth cultures was compared with the ability of Serratia marcescens strains to haemolyze human and sheep erythrocytes in the same conditions.