Late-onset multiple acyl-CoA dehydrogenase deficiency: a frequently missed diagnosis?
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Acyl-CoA Dehydrogenase↗
Biomedical subjects
H Blobel
Publications and source records attributed to H Blobel.
Adherence of Borrelia burgdorferi to granulocytes of different animal species.
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. Binding assays indicated that the adherence occurred between structures on the surface of the borreliae ("binding-sites") and on the membranes of the granulocytes ("receptors"). The "receptors" consisted of 4 fractions (A, B, C, and D) with components differing in molecular weight (MW) and binding activity for proteins on the surface of B. burgdorferi. Fraction A (MW 80000) had the highest binding activity for B. burgdorferi.
Animals↗
Dermonecrotic activity of a cell wall preparation from Fusobacterium necrophorum.
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. A dermonecrotic toxin was isolated from the cell wall preparation with sodium dodecylsulphate and concentrated by precipitation with ethanol. A preparation of the bacterial cytoplasm from Fus. necrophorum induced mainly erythema.
Animals↗
Isolation and characterization of fibronectin-binding sites of Borrelia garinii N34.
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. The binding of fibronectin to the spirochete was specific and saturable. Scatchard plot analysis of the binding data revealed two types of ligands on the spirochetal surface, one with high affinity and one with low affinity for fibronectin. The fibronectin-binding sites were solubilized from the surface of B. garinii N34 by lysozyme treatment. Fast protein liquid chromatography (FPLC) purification of the solubilized binding sites resulted in one band with a high fibronectin-binding activity and a molecular weight of ca. 147,000. FPLC-purified binding sites, fibronectin, and antibodies to fibronectin inhibited the adherence of the spirochete to epithelial cells competitively. These data provide strong support for the hypothesis that fibronectin-binding sites on the surface of B. garinii are involved in the adherence of the spirochete to their respective host cells.
Bacterial Adhesion↗
Inhibitory effects of fibrinogen on phagocytic killing of streptococcal isolates from humans, cattle and horses.
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. Phagocytic killing was determined by a fluorometric microassay using glass adherent polymorphonuclear neutrophils (PMN) from the respective host species, preopsonization with homologous sera led to a dose-dependent increase in phagocytic killing of all streptococcal cultures, preincubation of streptococci with fibrinogen significantly inhibited their phagocytic killing. Fibrinogen had no effect on phagocytic killing of non-fibrinogen binding S. agalactiae cultures. Further characterization studies with S. dysgalactiae and S. pyogenes revealed that a partial inhibition of phagocytic killing could also be achieved by preincubation with monomeric beta-chains of fibrinogen. Digestion of the fibrinogen binding sites on streptococci with proteases resulted in an almost complete loss of the inhibitory effects of fibrinogen on phagocytic killing. It could thus be concluded that by binding fibrinogen animal pathogenic streptococci could evade phagocytic killing in a similar manner as M protein carrying S. pyogenes isolates from human infections.
Animals↗
Isolation of a plasmid from "canine" Staphylococcus epidermidis mediating constitutive resistance to macrolides and lincosamides.
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. A detailed restriction map of pSES 1 could be constructed using the restriction endonucleases Acc I, Bcl I, Cfo I, Cla I, Hind III, Hinf I, Mbo I, Sst I and Taq I. This map allowed structural comparisons of pSES 1 with plasmids from "human" Staphylococcus- and Bacillus-species, also mediating macrolide-lincosamide resistance (MLR). On the basis of its restriction map, pSES 1 proved to be similar to the plasmids pNE 131 from "human" S. epidermidis, pE 194 from "human" S. aureus and pIM 13 from B. subtilis.
Animals↗
Isolation and restriction endonuclease analysis of a tetracycline resistance plasmid from Staphylococcus hyicus.
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. The tetracycline resistance (TET) plasmid, designated pST1, was characterized by restriction endonuclease analysis and a preliminary restriction map was constructed. The pST1 plasmid was demonstrated in 19 (57.6%) of 33 S. hyicus cultures by Southern blot hybridization. It was also detectable by electron microscopy.
Animals↗
Isolation and characterization of hyaluronidases from Streptococcus dysgalactiae, S. zooepidemicus and S. equi.
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. Hyaluronidase could be precipitated from the cell-free culture supernatant with ammonium sulphate and purified by chromatography on DEAE-cellulose, isoelectric focussing and preparative polyacrylamide gel electrophoresis. The isoelectric points of the hyaluronidases from S. dysgalactiae and S. equi were near pH 5, of that from S. zooepidemicus near pH 6. The hyaluronidases from S. dysgalactiae, S. zooepidemicus and S. equi had molecular weights of about 55,000 D. Maximal enzyme activities developed between 40 degrees C and 45 degrees C and pH 5.6 and 5.8. The Michaelis constants ranged from 7.5 x 10(-2) to 8.8 x 10(-2) mg/ml. Hyaluronidase activities were stimulated by Ca++, Mg++, Mn++, Co++, K+, and Li+ and inhibited by Zn++ and Cd++.
Animals↗
Isolations of protein A and protein G from the bacterial surface.
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. aureus by lysozyme, mutanolysine, hydroxylammoniumchloride, hot acid extraction or lysostaphin and subsequently purified by affinity chromatography on human IgG-sepharose. The purified protein A preparation had molecular weights between 29,000 and 63,000 D and inhibited binding of 125I-labeled human IgG to S. aureus Cowan I. Protein G could be solubilized from strain 26540 of the G-streptococci with lysozyme or hot acid extraction and purified by affinity chromatography on human IgG-sepharose. The purified protein G revealed a molecular weight of 67,000 D and inhibited binding of human IgG to the G-streptococci.
Bacterial Proteins↗
Common antibiotic resistance plasmids in Staphylococcus aureus and Staphylococcus epidermidis from human and canine infections.
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 4.45 kB tetracycline resistance (TetR-) plasmid pST 3 could be isolated. Detailed restriction maps of pSC 4 and pST 3 were constructed by double restriction endonuclease digests. The restriction maps revealed extensive structural homologies between pSC 4 from "canine" S. epidermidis and the CmR-plasmid pC 221 from "human" S. aureus as well as between pST 3 from "canine" S. epidermidis and the TetR-plasmid pT 181 from "human" S. aureus. These data suggested that an exchange of small plasmids between S. epidermidis and S. aureus might be possible.
Animals↗
A new streptomycin-resistance plasmid from Staphylococcus hyicus and its structural relationship to other staphylococcal resistance plasmids.
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. This plasmid was further characterised by restriction endonuclease analysis and a preliminary restriction map was constructed. The plasmid from S. hyicus that conferred streptomycin resistance was designated as pSAI-1. It showed some structural homology with the streptomycin-chloramphenicol resistance plasmid pSK68 from S. aureus of human origin. The MIC of streptomycin in resistance mediated by pSAI-1 was about 10 times higher than the MICs in resistance mediated by Smr plasmids from human S. aureus strains.
Animals↗
Plasmid-encoded resistance to macrolides and lincosamides in Staphylococcus hyicus.
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. The plasmid from porcine Staph. hyicus was designated as pSE2. It differed on the basis of its restriction map from the macrolid/lincosamid resistance (MLR-)-plasmids of other staphylococcal species from infections of humans. Furthermore, the pSE2 plasmid encoded two proteins of approximately 20.5 and 30 kDa.
Animals↗
Detection of a novel chloramphenicol resistance plasmid from "equine" Staphylococcus sciuri.
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. On the basis of restriction endonuclease analyses a detailed restriction map of pSC3 could be constructed. This allowed structural comparisons of pSC3 with Cm-plasmids of other staphylococcal species from infections of humans and animals and identification of pSC3 as a member of the pC 221-family of staphylococcal Cm-plasmids. The pSC3-plasmid encoded an inducible chloramphenicol acetyltransferase as confirmed by enzymatic assays. This enzyme could be demonstrated in cell-free lysates of Cm-induced pSC3-transformants.
Animals↗
Role of alpha 2-macroglobulin in phagocytosis of group A and C streptococci.
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. equi from equine infections bound only a complex of alpha 2M with trypsin (alpha 2M-T). Preincubation of S. pyogenes with native alpha 2M substantially enhanced their phagocytosis by human polymorphonuclear neutrophils (PMN) whereas preincubation with alpha 2M-T was without any effect. On the other hand, incubation of S. dysgalactiae and S. equi with alpha 2M-T markedly reduced their phagocytosis by PMN from the respective host species. Native alpha 2M did not affect the phagocytosis of these streptococci. Digestion of the streptococcal binding sites for alpha 2M and alpha 2M-T pronase abolished the enhancement of phagocytosis of S. pyogenes by native alpha 2M as well as the inhibition of phagocytosis of S. dysgalactiae and S. equi by alpha 2M-T. Thus, binding of alpha 2M or its complexes appeared to play a role in streptococcal pathogenicity.
Animals↗
Role of complement S protein (vitronectin) in adherence of Streptococcus dysgalactiae to bovine epithelial cells.
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. The S protein-binding sites were saturable and highly sensitive to trypsin. The binding of bovine S protein to S dysgalactiae isolates was specific and could not be inhibited by other plasma proteins, such as fibronectin, albumin, fibrinogen, alpha 2-macroglobulin, or IgG. Similarly, streptococcal binding of bovine S protein was not influenced by the synthetic peptide Gly-Arg-Gly-Asp-Ser, which constituted the host cell attachment sequence of S protein. In adherence experiments, prior binding of bovine S protein to S dysgalactiae enhanced streptococcal adherence to bovine epithelial cells. The enhancing effects by bovine S protein were abolished when the respective binding sites on the streptococci were digested by trypsin. Thus, bovine S protein could be an important mediator of adherence of S dysgalactiae to bovine epithelial cells.
Animals↗
[Plasmid-encoded antibiotic resistance in Staphylococcus hyicus].
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. This led to the construction of a specific restriction map for each of the 4 plasmids. On the basis of their restriction maps, these 4 antibiotic resistance plasmids from "porcine" S. hyicus-cultures were compared with the respective resistance plasmids of other staphylococcal species from infections of humans and animals.
Animals↗
[Isolation of Streptococcus pyogenes fibronectin receptors by affinity chromatography and high pressure liquid chromatography].
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Blotting, Western↗
Isolation and interspecies-transfer of a plasmid from Pasteurella multocida encoding for streptomycin resistance.
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.
Animals↗