• Newman Shah a publié une note il y a 6 jours et 1 heure

    Author contributionsAcknowledgementsWe gratefully acknowledge Myriam Siffert (Institute of Pathology, Vetsuisse Faculty, University of Bern) and Vreni Balmer (Institute of Parasitology) for their excellent technical assistance. David Arranz Solís was supported by a fellowship from the Spanish Ministry of Economy and Competitiveness (MINECO), as part of the training researcher staff programme (FPI, grant number BES-2011-043433) and a mobility grant for pre-doctoral short stays in R+D centres (EEBB-I-14-08002). This work was supported by the AGL2010-22191/GAN grant from the Spanish Ministry of Economy and Competitiveness (MINECO) and the Swiss National Science Foundation (SNSF; grant number 310030_146162).IntroductionThe disease caused by Trypanosoma vivax results in losses to livestock in Africa and in Central and South America (Osório et al., 2008). Although this disease is transmitted by tsetse flies in Africa, in the Americas it is transmitted mechanically by hematophagous dipterans, such as Tabanus sp., Stomoxys calcitrans and Haematobia irritans (Oliveira et al., 2009), as well as by fomites (Silva et al., 1997). During the course of trypanosomiasis, the parasitemia levels fluctuate and there may even be aparasitemic intervals, which can make diagnosis through parasitological methods harder. Serological tests are routinely used in diagnosing trypanosomiasis in cattle, although they do not indicate whether the infection is active or not (Nantulya 1990). Molecular methods such as the conventional dna ligase and loop-mediated isothermal amplification of DNA (LAMP) (Laohasinnarong et al., 2011) are excellent indicators of the presence of T. vivax DNA in the bloodstream of these animals. However, these methods are unable to indicate severity of disease or the phase of infection that the host is in.On the other hand, serum proteinograms are a diagnostic tool capable of predicting prognoses, thereby indicating the phase of infection and response to treatment of different illnesses (Murata et al., 2004). Acute-phase proteins (APPs) are glycoproteins produced by the liver through cytokine stimulation and, since they are related to the severity of disease and extent of tissue damage, their quantification can supply information on the diagnosis and prognosis of a given illness (Ceciliani et al., 2012). In a general manner, APPs can be classified as positive if they increase proportionally to tissue damage after an inflammatory process becomes established (Murata et al., 2004). In ruminants, the major APPs are serum amyloid A, haptoglobin, lipopolysaccharide-binding proteins and α1-acid glycoprotein (Ceciliani et al., 2012). According to Almeida et al. (2012) and Costa et al. (2010), the electrophoresis profile of serum proteins from animals that are naturally infected by Trypanosoma sp. indicates that APPs can aid in diagnosing this hemoprotozoon and providing better understanding of the host-parasite relationship, even in the chronic phase of infection.The aim of this study was to evaluate serum proteinograms of 429 cattle that were naturally infected by T. vivax, in order to investigate the APPs that act as markers of T. vivax infection and their behavior during host infection.Material and methodsResultsThe mean absorbances of the 429 serum samples tested were grouped into ELISA levels, which ranged from 0 to 9. The mean absorbances for the positive and negative control serum samples were 0.885±0.428 and 0.131±0.030, respectively. The 429 samples that were positive in the ELISA test were also positive through IFAT, titrated at dilutions of 1:40 to 1:1,280Thus, a total of 429 serum proteinograms from naturally infected animals (NIF) were performed and compared with 50 samples from control animals (C). In the serum proteinograms, IgA, transferrin, albumin, antitrypsin, IgG, haptoglobin and acid glycoprotein were evaluated. Proteins bands at 120, 95, 88, 37, 23 and 20.5KDa were observed and showed significant differences (p<0.05) between the NIF and C groups, and were identified by means of tandem mass spectrometry.

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