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J Rollof

Publications and source records attributed to J Rollof.

35 records · Page 2Linked to original sources
PubMed1992

Recurrent pneumonia: a review of 90 adult patients.

Recurrent pneumonia is still an important problem. In this retrospective study we reviewed the records of 90 patients with a history of 3 or more episodes of acute pneumonia. The 90 patients accounted for altogether 347 episodes of acute pneumonia, treated at the Department of Infectious Diseases, Lund. 12 patients died while being treated for pneumonia at the department. Pneumonia alone caused the death in 7 of these 12 patients. In all, 51 of the patients died during the 11-year study period. Death certificates, stating the cause of death, were available in 38 cases, and pneumonia was the direct cause of death in 15 patients. Most of the infections were community-acquired, only 47 were nosocomial, 20/90 patients suffered from disorders associated with immune deficiency, and 70 patients had other predisposing illnesses. We found a larger number of underlying immunoglobulin deficiencies (11 patients of 38 investigated) than previously reported. Of 13 patients without other known, predisposing conditions, hypogammaglobulinemia was found in 3 patients. We suggest that patients with recurrent pneumonia should be thoroughly investigated, in order to find previously unrecognized immune deficiency.

Acute Disease↗
PubMed1992

Severe Pasteurella multocida infections in pregnant women.

We report 2 cases of severe infections due to Pasteurella multocida, both occurring during pregnancy in previously healthy women. Both women had contact with animals (dog and cat) but neither of them had been bitten. Apart from a slight decrease in IgG levels, no immunological defects could be detected. Both women had received oral phenoxymethylpenicillin in the early phase of the disease, but still fell ill with severe infections. One woman had meningitis while the other suffered from cellulitis with deep abscess formation.

Abscess↗
PubMed1990

Are tumor necrosis factor (TNF) or cortisol of value for the diagnosis of acute septicemia?

Early diagnosis is of great importance to improve the prognosis of septicemia. Traditional laboratory tests are either delayed like blood cultures, or unspecific like WBC count or ESR. In this retrospective pilot study we have assayed plasma cortisol, blood sugar and serum tumor necrosis factor (TNF) from patients with verified septicemia. With the approach used in this study none of the tests were able to differentiate between septicemia and other infectious febrile illnesses, or to predict if the causing organism was gram-positive or gram-negative.

Acute Disease↗
PubMed1989

Crystal violet binding, cell surface properties and extracellular enzyme profiles of Staphylococcus aureus producing toxic shock syndrome toxin-1.

Staphylococcus aureus isolated from clinically diagnosed cases of toxic shock syndrome (TSS) showed susceptibility to phage types belonging to both I and III groups (90.5%). Phage typing patterns showed a wide diversity among 87 toxic shock syndrome toxin-1 (TSST-1) positive strains isolated from different non TSS clinical sources. Toxin producing strains isolated from both TSS and non TSS showed a remarkable ability to bind to crystal violet (pattern C/D, 97.2%) incorporated into brain heart infusion agar media at subinhibitory concentrations and these isolates were traced to biotype var. hominis. The cellular fatty acid compositions of TSS and non-TSS strains belonging to the three biotypes S. aureus var. hominis, S. aureus var. bovis and S. aureus var. canis did not differ. TSST-1 producing strains demonstrated a high salt aggregation test value (above 1.5) indicating a low cell surface hydrophobicity. Both TSS and non TSS strains demonstrated a high lipolytic activity. TSST-1 positive strains in general, showed significantly higher lipase activity than strains isolated from septicemia (p less than 0.0001) and superficial (p less than 0.0001) infections. The proteolytic activity is higher among TSS (median value 0.075 U/ml) than to non TSS (median value 0.045 U/ml) strains. There was no correlation with the quantity of toxin production in vitro and to the properties described.

Bacterial Toxins↗
PubMed1989

A comparative study of two lipases from different strains of Staphylococcus aureus.

In order to compare lipases from two different Staphylococcus aureus strains (FN 37 and TEN 5), the enzymes from the respective strains were purified using octyl-Sepharose chromatography and characterized with regard to chemical, immunological and enzymatic properties. Differences in the size of the lipases in their native forms necessitated modifications of the purification process, but after purification identical subunits of about 43 kD were found in SDS-PAGE, and both lipases had an apparent molecular weight of 110 kD when subjected to gel chromatography on Sephadex G-200. Analysis of the amino acid compositions of the lipases showed considerable differences. Serine was the predominant amino acid in the FN 37 lipase, whereas glycine was most abundant in the TEN 5 lipase. Nevertheless, the two lipases were similar when tested with double immune diffusion against an antiserum raised against the TEN 5 lipase, and inactivation of enzyme activities by the antiserum followed the same patterns. Enzymatically, the enzymes were similar with regard to salt inhibition, ion dependency and heat inactivation. The substrate specificities, tested against glyceride substrates, were similar. Thus, the two staphylococcal lipases seem to be similar but not identical.

Amino Acids↗
PubMed1989

In vitro activities of cefcanel and some other cephalosporins against Pasteurella multocida.

Thirty-five strains of Pasteurella multocida from humans and animals were tested for susceptibility to five cephalosporins by a broth dilution method. Cefcanel showed high activity against all isolates (MIC and MBC, less than or equal to 0.64 micrograms/ml). The corresponding figure for cefaclor and cefuroxime was 2.56 micrograms/ml. Cefadroxil and cephalexin were the least active compounds tested.

Animals↗
PubMed1989

Pasteurella multocida occurs in a high frequency in the saliva of pet dogs.

Pasteurella multocida is a frequent cause of infection after animal bites. In contrast to earlier reports, P. multocida appeared to be as common among dogs as among cats. We found 17 (81%) of 21 pet dogs to harbour P. multocida in their saliva. At normal contact, the risk of transmission from dogs to humans seems to be negligible. Only 1/27 dogs owners was found to harbour the organism. None of 13 cat owners or 23 persons without animal contacts harboured P. multocida.

Animals↗
PubMed1988

Interference of Staphylococcus aureus lipase with human granulocyte function.

The influence of purified Staphylococcus aureus lipase on granulocyte function and morphology was studied. The lipase itself was strongly chemotactic; in addition preincubation of granulocytes with low concentrations of lipase enhanced the directed movement, as assayed in the agarose system. Higher concentrations of lipase, in contrast, gave a progressive reduction of granulocyte chemotaxis; at 12 micrograms lipase per ml, cells were almost immobilized. Phagocytic killing of Staphylococcus aureus by granulocytes preincubated with lipase was reduced in a dose-dependent manner. At 12 micrograms lipase per ml almost no staphylococcal killing occurred. This was mainly accounted for by a reduction of bacterial uptake, but some decrease in intragranulocytic killing was also noted. These functional alterations, which can all be ascribed to an interference with membrane functions, were associated with marked changes of the granulocyte surface structure, which was denuded and lacked normal microvilli. The effects of lipase were partly retained after heat inactivation of lipase activity, indicating that the effects of staphylococcal lipase on granulocyte function are not due to enzymatic activity alone. These effects of lipase may be an important virulence factor and contribute to the preferential location of lipase-producing Staphylococcus aureus strains at deep sites of infection.

Chemotaxis, Leukocyte↗
PubMed1988

The Tween 80 reaction does not correlate to triglyceride lipase production of Staphylococcus aureus.

This comparison of Tween 80 reaction with triglyceride lipase production comprises 357 Staphylococcus aureus strains from various clinical sources. Tween 80 is a water-soluble substrate, and thus estimates esterase activity. Lipase production was assayed using water-insoluble substrates (radiolabelled triglyceride emulsions). Only a minor proportion of Tween 80-positive strains had significant triglyceride lipase production (greater than 5 mU/10(9) bacteria). The discrepancy between the two methods was most pronounced in subgroups of samples with low frequency of lipase production, e.g. from isolates from superficial locations such as nasal mucosa and impetigo. Owing to its low specificity, the Tween 80 reaction therefore seems unsuitable as a marker for lipase activity in clinical isolates of Staphylococcus aureus.

Bacteriophage Typing↗
PubMed1987

Purification and characterization of a lipase from Staphylococcus aureus.

An extracellular lipase from Staphylococcus aureus (strain FN 37) was purified to homogeneity. A cell-free culture broth was subjected to ammonium sulphate precipitation, and the lipase was isolated from the resuspended pellet by adsorption chromatography on octyl-Sepharose. The purification was 957-fold, and the recovery of the octyl-Sepharose chromatography was about 100%. The specific activity of the purified lipase was 546 mU of lipase activity per micrograms protein. The purity of the final product was documented by SDS-polyacrylamide gel electrophoresis in which a homogeneous protein band of 43 kDa was found. In gel chromatography on Sephadex G-200 the lipase eluted as a homogeneous peak with an apparent molecular mass of 110 kDa, suggesting that the lipase may exist as an oligomer in physiological media. Analysis of the amino-acid composition revealed a predominance of polar, non-charged amino acids, with serine accounting for 24 mol% of the amino-acid residues.

Amino Acids↗
PubMed1987

Positional specificity and substrate preference of purified Staphylococcus aureus lipase.

We have studied the substrate preference and specificity, including positional specificity, of a lipase purified from Staphylococcus aureus (strain FN 37). This extracellular bacterial enzyme is relatively insensitive to product inhibition, and hydrolyzes tri-, di- and monooleoylglycerol in emulsified and micellar form at similar rates and without marked substrate preference. The lipase lacks positional specificity, and the hydrolysis of triacylglycerol proceeds rapidly to free fatty acid and glycerol without accumulation of intermediary products.

Blood↗
PubMed1987

Lipolytic activity of Staphylococcus aureus strains from disseminated and localized infections.

Lipase production of 425 S. aureus strains isolated from patients with different clinical diagnoses and healthy carriers were measured by a specific method, using emulsified trioleoylglycerol substrate. Strains isolated from patients with septicemia showed significantly higher lipase activity than osteomyelitis strains (p = 0.011), impetigo strains (p = 0.002) and strains isolated from healthy relatives of patients with recurrent furunculosis (p = 0.019). Recurrent furunculosis and pyomyositis strains had significantly higher (p = 0.002 and 0.032, respectively) lipase activity than septicemia strains. S. aureus strains isolated from patients with a significant antibody response in an antilipase ELISA did not show a higher lipase activity in culture supernatants than strains from patients without a significant antibody response. The lipase activity was significantly higher in strains isolated from deep or subcutaneous infections, i.e., septicemia, pyomyositis, osteomyelitis, aerobic and anaerobic furunculosis, than in strains from superficial infections, i.e. impetigo, or from nasal mucosa.

Furunculosis↗
PubMed1984

A simple turbidimetric method for specific measurement of Staphylococcus aureus lipase activity.

We have developed a simple semiquantitative method for measuring Staphylococcus aureus lipase activity. Enzymatic activity is measured as the decrease in spectrophotometric absorbancy in a lipid emulsion after incubation with the sample. The sensitivity, precision and accuracy are adequate for routine purposes. The assay is rapid and simple and does not require advanced technical equipment.

Lipase↗