Prevalência de anticorpos anti-Rickettsia spp. em cães da cidade de Belo Horizonte, MG / Prevalence of antibodies anti-Rickettsia in dogs from Belo Horizonte, MG, Brazil

A cross-sectional study was conducted to determine the seroprevalence of anti-Rickettsia spp. in dogs from Belo Horizonte, MG. For this purpose, serum samples from 453 dogs were collected during the rabies vaccination campaign and tested by the indirect immunofluorescence assay (IFA) using five antigens: Rickettsia bellii, Rickettsia amblyommii, Rickettsia rickettsii, Rickettsia parkeri, and Rickettsia felis. The endpoint titer reacting with each antigen was determined and serum was considered positive if it reacted at the 1:64 dilution. Serum showing titer for a Rickettsia species at least four-fold higher than that observed for any other Rickettsia species was considered homologous to the first Rickettsia species. Only three (0.66%) dogs reacted positively to at least one Rickettsia species and one serum showed to be homologous to R. rickettsii. These results showed a low prevalence of antibodies anti-Rickettsia spp. in dogs from Belo Horizonte city. However, other serosurvey needs to be performed for surveillance of the endemic status of the disease in the municipal district.(AU)

Purification and functional characterization of two fibrinogenolytic enzymes from Bothrops alternatus venom

Two fibrinogenolytic enzymes, Bothrops alternatus metalloprotease isoform (BaltMP)-I and II, were purified from Bothrops alternatus venom using Diethylaminoethyl (DEAE) Sephacel, Sephadex G-75 and Heparin-Agarose column chromatography. Purified BaltMP-I and II ran as single protein bands on analytical polyacrylamide gel electrophoresis and showed molecular weights of 29000 and 36000, respectively, under reducing conditions in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). BaltMP-II, but not BaltMP-I, displayed blood-clotting activity in bovine plasma, which was about 10-fold higher than that of the crude venom. Both enzymes were proteolytically active against bovine fibrinogen as substrate. When fibrinogen and each enzyme were incubated at 37°C, at a ratio of 1:100 (w/w), BaltMP-II cleaved preferentially the Aalpha -chain and more slowly the Bbeta -chain. The action of BaltMP-I was similar, but lower. None of the proteases degraded the gamma-chain of fibrinogen. The fibrinogenolytic activity of the enzymes was inhibited by 1,10-phenanthroline, suggesting they are metalloproteases. Since both enzymes were found to cause defibrinogenation when intraperitoneally (i.p.) administered to mice, they can be of medical interest as a therapeutic agent in the treatment and prevention of arterial thrombosis.(AU)