Methods: A representative sample of the population of the seven islands, formed of 662 people aged between 5 and 75 years (368 females, 294 males), was analyzed. learn more Epidemiological data were obtained by direct survey. The detection of serum IgG antibodies against both microorganisms was based on an indirect immunofluorescence test, considered positive if the titers were >= 1/80.
Results: Of the analyzed population 3.9% had IgG antibodies against R. typhi and 4.4% against R. conorii. Out of these positive samples, only three were positive for both
species. The seroprevalence was similar in both sexes. Positive results were found in all age groups, but a higher rate was noticed in those aged 46 years and older (p < 0.05). R. typhi was found to be more prevalent in rural areas of all islands, as well as in farmers.
Conclusions: Our results confirm the presence of antibodies against the causative AS1842856 chemical structure agents of murine typhus and Mediterranean spotted fever in the Canary Islands. Indirect data suggest that the detection of antibodies to R. conorii might be due to a cross-reaction between these species. (C) 2011 International
Society for Infectious Diseases. Published by Elsevier Ltd. All rights reserved.”
“Superoxide dismutase (SOD) has extensive clinical applications for protecting organisms from toxic oxidation. In this study, selleck products the integrated iron-superoxide dismutase gene (fe-sod) coding sequence of Nostoc
commune stain CHEN was cloned from genomic DNA and compared to sods from other reported algae. These analyses of immunology and phylogenetics indicated that this Fe-SOD is considerably homologous with SODs from lower prokaryotes (Fe-SOD or Mn-SOD) but not those from higher animals (Cu/Zn-SOD). In addition, the N. commune Fe-SOD shows 67 to 93% protein sequence identity to 10 other algal Fe-SODs (or Mn-SODs) and 69 to 93% gene sequence identity. Rare nonsynonymous substitutions imply that algal SODs are being subjected to strong natural selection. Interestingly, the N. commune Fe-SOD enzyme molecule has a compact active center that is highly conserved (38.1% of residues are absolutely conserved), and 2 loose ends localized outside the molecule and inclined to mutate (only 11.5% of residues are absolutely conserved). Based on associative analyses of evolution, structure, and function, this special phenomenon is attributed to function-dependent evolution through negative natural selection. Under strong natural selection, although the mutation is random on the gene level, the exterior region is inclined to mutate on the protein level owing to more nonsynonymous substitutions in the exterior region, which demonstrates the theoretical feasibility of modifying Fe-SOD on its ends to overcome its disadvantages in clinical applications.