The immunomodulator glatiramer acetate influences spinal motoneuron plasticity during the course of multiple sclerosis in an animal model

The immunomodulador glatiramer acetate (GA) has been shown to significantly reduce the severity of symptoms during the course of multiple sclerosis and in its animal model - experimental autoimmune encephalomyelitis (EAE). Since GA may influence the response of non-neuronal cells in the spinal cord, it is possible that, to some extent, this drug affects the synaptic changes induced during the exacerbation of EAE. In the present study, we investigated whether GA has a positive influence on the loss of inputs to the motoneurons during the course of EAE in rats. Lewis rats were subjected to EAE associated with GA or placebo treatment. The animals were sacrificed after 15 days of treatment and the spinal cords processed for immunohistochemical analysis and transmission electron microscopy. A correlation between the synaptic changes and glial activation was obtained by performing labeling of synaptophysin and glial fibrillary acidic protein using immunohistochemical analysis. Ultrastructural analysis of the terminals apposed to alpha motoneurons was also performed by electron transmission microscopy. Interestingly, although the GA treatment preserved synaptophysin labeling, it did not significantly reduce the glial reaction, indicating that inflammatory activity was still present. Also, ultrastructural analysis showed that GA treatment significantly prevented retraction of both F and S type terminals compared to placebo. The present results indicate that the immunomodulator GA has an influence on the stability of nerve terminals in the spinal cord, which in turn may contribute to its neuroprotective effects during the course of multiple sclerosis.17918

Effect of surgical treatment on the cellular immune response of gastric cancer patients

Patients with gastric cancer have a variety of immunological abnormalities. In the present study the lymphocytes and their subsets were determined in the peripheral blood of patients with gastric cancer (N = 41) both before and after surgical treatment. The percent of helper/inducer CD4 T cells (43.6 ± 8.9) was not different after tumor resection (43.6 ± 8.2). The percent of the cytotoxic CD8+ T cell population decreased significantly, whether patients were treated surgically (27.2 ± 5.8%, N = 20) or not (27.3 ± 7.3%, N = 20) compared to individuals with inflammatory disease (30.9 ± 7.5%) or to healthy individuals (33.2 ± 7.6%). The CD4/CD8 ratio consequently increased in the group of cancer patients. The peripheral blood lymphocytes of gastric cancer patients showed reduced responsiveness to mitogens. The defective blastogenic response of the lymphocytes was not associated with the production of transforming growth factor beta (TGF-ß) since the patients with cancer had reduced production of TGF-ß1 (269 ± 239 pg/ml, N = 20) in comparison to the normal individuals (884 ± 175 pg/ml, N = 20). These results indicate that the immune response of gastric cancer patients was not significantly modified by surgical treatment when evaluated four weeks after surgery and that the immunosuppression observed was not due to an increase in TGF-ß1 production by peripheral leukocytes.33934

The efficacy of recombinant protein lbk39 for the diagnosis of leishmaniosis in dogs

Visceral leishmaniosis is one of the most important zoonotic diseases on the planet and dogs are the main reservoir of canine visceral leishmaniosis (CVL) in endemic areas. They play an important role in human infection because in dogs the disease appears long time after infection, and they can move uncontrollably, contributing to disperse the parasite. To take the decision to treat the animals or for euthanasia, in an elimination programme, in order to reduce the parasitic load, it is necessary to diagnose correctly, having more effective tools. Our group has developed a new recombinant antigen-based kinesin-related gene of Leishmania braziliensis (Lbk39), which shows 59% amino acid identity to the L. infantum homologue. The Lbk39 gene was synthesized, inserted into the pLEXSY-sat2 vector and transfected into L. tarentolae cells by electroporation. The recombinant protein was secreted in the culture with a C-terminal histidine marker, purified, generating a product at 337.68 μg mL-1. A total of 152 sera from dog's endemic and non-endemic areas were used, being 78 positives and 75 negatives. The antigen Lbk39 showed 100% sensitivity and 96.1% specificity. We compared this antigen with other antigens such as total extract of the parasite, TRDPP, and our data indicate that Lbk39 has potential application in the diagnosis of CVL through antibody detection. Copyright © The Author(s), 2020. Published by Cambridge University Press

Protective Immunity Induced By A Trypanosoma Cruzi Soluble Extract Antigen In Experimental Chagas' Disease. Role Of Interferon γ

CBA/J mice can be protected against lethal infection with Trypanosoma cruzi by treatment using T. cruzi soluble extract antigen (TCSE). In vivo administration of TCSE (400 μg/mouse) into naive mice increased the cellular proliferative response to Con A and elevated the levels of IFN-γ. The production of IFN-γ was extremely important in controlling the replication of the parasite since the protective activity of TCSE was completely abrogated by in vivo treatment with an anti IFN-γ neutralizing antibody. These results suggest that depending on the level, cytokine production results in the control of replication of the parasite in experimental Chagas' disease.291112Kierszenbaum, F., Cuna, W.R., Beltz, L.A., Sztein, M.B., (1990) J. Immunol., 143, pp. 275-279Kierszenbau, F., Sztein, M.B., Beltz, L.A., (1989) Immunology Today, 10, pp. 129-131Cunningham, D.S., Kuhn, R.E., (1980) J. Parasitol., 66, pp. 16-27Harel-Bellan, A., Joskowicz, M., Dradelizi, D., Eisen, H., (1983) Proc. Natl. Acad. Science USA, 80, pp. 3466-3469Silva, J.S., Twardzik, D.R., Reed, S.G., (1991) J. Exp. Med., 174, pp. 539-545Bermudez, L.E., (1993) J. Immunol., 150, pp. 1838-1845Reed, S.G., Phil, D.L., Grabstein, K.H., (1989) J. Immunol., 142, pp. 2067-2071Plata, F., Wietzerbin, J., Pons, F.G., Falcoff, E., Eisen, H., (1984) Eur. J. Immunol, 14, pp. 930-935Reed, S.G., (1988) J. Immunol., 140, pp. 4342-4347Torrico, F., Heremans, H., Rivera, M.T., Marck, E.V., Billiau, A., Carlier, Y., (1991) J. Immunol., 146, pp. 3626-3632Al-Sabbagh, A., Garcia, C.A.A.C., Diaz-Bardales, B.M., Zaccarias, C., Sakurada, J.K., Santos, L.M.B., (1998) Exp. Parasitol., 89, pp. 304-311Minoprio, P.M., Eisen, H., Forni, L., D'Imperio Lima, M.R., Joskowics, M., Coutinho, A., (1986) J. Immunol., 24, pp. 661-668Tamashiro, W.M.S.C., Repka, D., Sakurada, J.K., Camargo, I.J.B., Araujo, P.M.F., Atta, A.M., Rangel, H.A., (1983) Z. Parasitenkd., 69, pp. 425-434Scott, M.T., Snary, D., (1979) Nature, 282, pp. 73-74Segura, E.L., Paulone, I., Cerisola, J., Gonzalez-Capra, S.M., (1976) J. Parasitol., 62, pp. 131-133Wirth, J.J., Kiersenbaum, F., Sonnenfeld, G., Zlotnik, A., (1985) Infection and Immunity, 49, pp. 61-66Taibi, A., Espinoza, A.G., Ouaissi, A., (1995) Immunol. Letters, 48, pp. 193-200Scott, P., Natovitz, P., Coffman, R.L., Pearce, E., Sher, A., (1988) J. Exp. Med., 168, pp. 1675-168