Publications by authors named "Blobel H"

Adherence of 4 Borrelia (B.) burgdorferi strains (z7/22, z7/27, z7/41, PBi) to polymorphonuclear granulocytes from different domestic animals (horses, cattle, sheep, dogs) was investigated. All 4 strains adhered to the granulocytes.

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Adherence of bacteria to host cell membranes is one of the initial steps of microbial pathogenicity. Numerous studies have suggested that fibronectin promotes this interaction in some bacterial species. In this study, we have examined the ability of Borrelia garinii to bind fibronectin.

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A cell wall preparation of Fusobacterium necrophorum induced haemorrhagic necrosis in the skins of guinea pigs and rabbits. Effects in mice and rats were weak or absent. The toxic activity of the cell wall preparation was not reduced by heat treatment.

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The effects of fibrinogen on phagocytic killing of Streptococcus dysgalactiae from cattle and S. equi from horses were studied in comparison to that of S. pyogenes from humans.

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A small plasmid of 2.35 kb, isolated from a porcine Staphylococcus hyicus-culture, was found to be responsible for constitutive resistance to macrolide/lincosamide antibiotics. This plasmid-encoded property could be established by interspecific transformation experiments.

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A small chloramphenicol resistance (Cm) plasmid of 4.65 kB could be detected in an "equine" Staphylococcus sciuri-culture. This plasmid, designated as pSC3, was identified by interspecific protoplast transformation.

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A total of 33 Staphylococcus hyicus-cultures from piglets with exudative epidermatitis were analyzed for the presence of antibiotic resistance plasmids. Four small plasmids encoding resistances to chloramphenicol, macrolide-lincosamide-antibiotics, streptomycin or tetracyclines could be identified in plasmid-curing and plasmid-transformation experiments. For further characterization these plasmids were digested with restriction endonucleases.

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A plasmid of 4.550 kb, conferring resistance to tetracycline, was demonstrated in Staphylococcus hyicus cultures from piglets with exudative epidermidis. The plasmid-encoded properties were determined both by curing and interspecific protoplast transformation experiments.

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The plasmids of a multiresistant "canine" Staphylococcus epidermidis-culture were investigated. Two small plasmids, the 4.55 kB chloramphenicol resistance (CmR-) plasmid pSC4 and the 4.

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Ten tested cultures each of Staphylococcus aureus (S. aureus) and of Streptococcus belonging to serological group G bound human IgG to a high extent. Protein A could be solubilized from strain Cowan I of S.

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Binding of alpha 2-macroglobulin (alpha 2M) to streptococci and its effects on phagocytosis were investigated. Two types of streptococcal binding sites for alpha 2M were observed: Streptococcus pyogenes from human infections interacted only with native alpha 2M whereas S. dysgalactiae from bovine and S.

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A small plasmid of 4.4 kb encoding resistance to streptomycin (Smr) was detected in a multiresistant Staphylococcus hyicus culture from a piglet with exudative epidermitis. The plasmid-encoded properties were determined by interspecies protoplast transformation experiments.

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The binding of bovine complement S protein (vitronectin) to Streptococcus dysgalactiae isolates from cattle with mastitis and the S protein's role in streptococcal adherence to bovine epithelial cells were investigated. All 25 clinical isolates of S dysgalactiae interacted with bovine S protein. None of the other streptococcal species tested bound to bovine S protein.

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10 out of 10 cultures each of Streptococcus dysgalactiae and S. zooepidemicus and 6 out of 10 cultures of S. equi tested for hyaluronidase produced this enzyme.

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A small plasmid of 2.5 kB mediating constitutive resistance to macrolide-lincosamide-(ML)antibiotics could be detected in a "canine" Staphylococcus epidermidis-culture. This plasmid, designated as pSES 1, was identified by interspecies protoplast transformation into Staphylococcus aureus RN 4220.

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A small plasmid of 3.95 kb, encoding resistance to chloramphenicol (Cm) was detected in three of 33 Staphylococcus hyicus strains. The plasmid in each of the three strains was indistinguishable by Southern-blot hybridization and restriction enzyme analysis.

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Staphylococcus hyicus-cultures, isolated from piglets and cattle with skin lesions were investigated for their plasmid content and their resistance to antimicrobial agents and heavy metals. Several plasmids of different sizes could be detected in most of the 32 "porcine" S. hyicus-isolates, whereas none of the 20 "bovine" S.

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All tested cultures of Streptococcus uberis produced free hyaluronidase. Hyaluronidase could be isolated by ammonium sulfate precipitation and was further purified by chromatography on DEAE-cellulose, gelfiltration on ultragel ACA44 and isoelectric focusing. The purification factor was estimated to be 1689.

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Pasteurella haemolytica-cultures, isolated from cattle with respiratory diseases, were investigated for their biotype, serotype, antimicrobial resistance and plasmid content. A plasmid encoding a beta-lactamase could be demonstrated in 9 of 19 Pasteurella haemolytica-cultures. These 9 cultures, all belonging to biotype A and serotype 1, were resistant to ampicillin, carbenicillin, penicillin G and ticarcillin.

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A plasmid encoding streptomycin-resistance could be detected in 13 of 32 Pasteurella multocida-cultures isolated from cattle and swine. The plasmid of these cultures proved to be similar upon Southern blot hybridization. It could be transformed into Escherichia coli 490A, where it also expressed streptomycin resistance.

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The role of S protein in the adherence of group A and G streptococci to human umbilical vein endothelial cells cultivated in 96-well microdilution plates was studied by utilizing fluorescein-labeled streptococci. The assay proved suitable for quantitative determination of bacterial adherence to cultured endothelial cells for all tested strains of streptococci. Only bacterial strains with significant S protein binding but weak fibronectin binding were included in these studies.

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Adherence of Streptococcus dysgalactiae isolates from cattle and S equi isolates from horses to their respective host epithelial cells was compared with the adherence of S pyogenes to human epithelial cells. The adherence was quantitatively determined by use of fluorescein-labeled streptococci. All 3 streptococcal species adhered selectively to their respective host cells.

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All 24 cultures of Streptococcus canis examined bound 125I-labelled human albumin, IgG and fibrinogen; but neither IgA nor haptoglobin. Binding of human albumin was time-dependent, saturable and reversible by the addition of unlabelled albumin. The binding of 125I-labelled human albumin could be inhibited completely by unlabelled albumin preparations from humans, mice and dogs, and partly by bovine albumin.

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