ABSTRACT
INTRODUCTION: Living with dogs leads one to consider the necessity of identifying canine infections found in the people with whom the dogs live. OBJECTIVE: Dogs which were clinically and serologically positive with the infections Ehirlichia canis, Anaplasma phagocytophilum, Borrelia burgdorferi, and Dirofilaria Immitis were sought. People with the same infections were also identified. MATERIAL AND METHODS: From a population of 80 dogs identified in the villages of San Bartolo Coyotepec and San Agustín Etla (suburbs peripheral to the city of Oaxaca, Mexico), 27 dogs were selected for study, all of which had adenomegaly, hepatomegaly, splenomegaly, and fevers of at least 43° C. Using enzyme immunoassay in this population of dogs and their closest human contacts, antibodies for Ehirlichia canis, Anaplasma phagocytophilum, Borrelia burgdorferi, and the antigen for Dirofilaria immitis were sought. Positive results in humans were confirmed by polymerase chain reaction (PCR). RESULTS: Ten dogs with the clinical signs mentioned above tested positive for antibodies to Ehrlichia canis; two cases tested positive for Anaplasma phagocytophilum; one case tested positive for Dirofilaria Immitis. From human contact, one person tested positive for Ehirlichia canis; this case was confirmed by DNA amplification by means of PCR. CONCLUSION: It is necessary to identify the population of sick dogs in order to reduce related infections in people.
Subject(s)
Disease Reservoirs/veterinary , Ehrlichiosis/diagnosis , Occupational Diseases/diagnosis , Adult , Anaplasma phagocytophilum/immunology , Animals , Borrelia burgdorferi/immunology , Dirofilaria immitis/immunology , Disease Reservoirs/microbiology , Disease Reservoirs/parasitology , Dogs , Ehrlichia canis/immunology , Female , Humans , Tick Bites/complications , ZoonosesABSTRACT
The peptide NH(2)-DTEDQEDQVDPR-COOH is released during activation of protein C zymogen. We measured the effect of a synthetic peptide with an amino acid sequence similar to that of the natural peptide on platelets from healthy individuals using platelet aggregometry. We found that this synthetic peptide inhibits platelet aggregation induced by thrombin; furthermore, it diminishes mobilization of intraplatelet calcium. Molecular docking showed weak interaction between the synthetic peptide and thrombin. Our findings suggest that this synthetic peptide may interact with a receptor located on the platelet cell membrane.
