Composição compreendendo frações ou sub-frações de promastigotas ou amastigotas de Leishmania denominadas Fucose Mannose Ligand (fml) e saponina, composição para preparar vacinas bloqueadoras da transmissão de Leishmaniose em humanos e animais compreendendo frações ou sub-frações de promastigotas ou amastigotas de Leishmania (fml) e saponina, uso da composição na preparação de vacinas bloqueadoras para impedir a transmissão de Leishmaniose visceral humana ou animal, uso da composição na preparação de reagentes consistindo na administração de frações ou sub-frações de promastigotas ou amastigotas de Leishmania denominadas Fucose Mannose Ligand (fml) e saponina

28/04/1998: Notificação da homologação da desistência do pedido de patente, apresentada pelo depositante, acarretando o encerramento do processo administrativo.DepositadaA invenção trata de uma composição compreendendo frações ou sub-frações de promastigotas ou amastigotas de Leishmania, denominada "Fucose Mannose Ligand" (FML) e saponina. A invenção compreende, também, o uso da composição para preparar vacina bloqueadora impedindo a transmissão de Leishmaniose em humanos ou animais

The replication of human immunodeficiency virus type 1 in macrophages is enhanced after phagocytosis of apoptotic cells.

Submitted by Ana Maria Fiscina Sampaio ([email protected]) on 2012-09-06T17:39:06Z No. of bitstreams: 1 Lima RG The replication of human ....pdf: 118124 bytes, checksum: a010923612eef7c104e7a3063286d053 (MD5)Made available in DSpace on 2012-09-06T17:39:06Z (GMT). No. of bitstreams: 1 Lima RG The replication of human ....pdf: 118124 bytes, checksum: a010923612eef7c104e7a3063286d053 (MD5) Previous issue date: 2002Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, BrasilFundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, BrasilUniversidade Federal do Rio de Janeiro. Instituto de Microbiologia. Rio de Janeiro, RJ, BrasilFundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, BrasilFundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, BrasilFundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, BrasilClearance of apoptotic cells increases macrophage secretion of antiinflammatory mediators and might modulate viral replication in human immunodeficiency virus (HIV) type 1–infected macrophages. To study this, primary macrophages were infected with HIV-1 and exposed to apoptotic cells. It was found that phagocytosis of apoptotic cells potently enhanced HIV-1 growth. The peptide Arg-Gly-Asp-Ser, which binds to integrin receptors, inhibited the uptake of apoptotic cells and the subsequent enhancement of HIV-1 replication. Viral replication was preceded by increased secretion of transforming growth factor (TGF)–b1 and partially reverted by anti–TGF-b1 antibodies. Moreover, anti–TGF-b1 antibodies inhibited HIV-1 replication in macrophages not exposed to apoptotic cells. A positive correlation was observed between TGFb1 production and HIV-1 growth, and the addition of TGF-b1 amplified HIV-1 replication in macrophages from low TGF-b1 producers. The findings suggest that TGF-b1 favors HIV-1 replication in macrophages and that the clearance of apoptotic cells by HIV-1–infected macrophages contributes to persistent viremia in patients infected with HIV-1

Anti-HIV-1 activity of the Iboga alkaloid congener 18-methoxycoronaridine.

Submitted by Ana Maria Fiscina Sampaio ([email protected]) on 2014-08-05T17:35:17Z No. of bitstreams: 1 Silva EM Anti-HIV....pdf: 197976 bytes, checksum: 572839340f28382b8e5a79474f73930c (MD5)Made available in DSpace on 2014-08-05T17:35:18Z (GMT). No. of bitstreams: 1 Silva EM Anti-HIV....pdf: 197976 bytes, checksum: 572839340f28382b8e5a79474f73930c (MD5) Previous issue date: 2004Fundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Laboratório Avançado de Saúde Pública. Salvador, BA, BrasilUniversidade Federal Fluminense. Laboratório de Virologia Molecular. Departamento de Biologia Celular e Molecular. Rio de Janeiro, RJ, Brasil / Instituto Oswaldo Cruz. Laboratório de Imunologia Clínica. Departamento de Imunologia. Rio de Janeiro, RJ, BrasilUniversidade Federal Fluminense. Laboratório de Virologia Molecular. Departamento de Biologia Celular e Molecular. Rio de Janeiro, RJ, BrasilFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Laboratório Avançado de Saúde Pública. Salvador, BA, Brasil / Escola Bahiana de Medicina e Saúde Pública. Fundação Bahiana para o Desenvolvimento das Ciências. Salvador, BA, BrasilUniversidade Federal do Rio de Janeiro. Instituto de Microbiologia. Departamento de Imunologia. Rio de Janeiro, RJ, BrasilUniversity of Vermont. Department of Chemistry. Burlington, VT, USAInstituto Oswaldo Cruz. Laboratório de Imunologia Clínica. Departamento de Imunologia. Rio de Janeiro, RJ, BrasilThe Iboga alkaloid congener 18-methoxycoronaridine (18-MC) exhibits in vitro leishmanicidal and in vivo anti-addiction properties. In this paper, we describe that 18-MC inhibits HIV-1 infection in human peripheral blood mononuclear cells (PBMCs) and monocyte-derived macrophages. We found that 18-MC inhibits the replication of primary isolates of HIV-1 in a dose-dependent manner, regardless of the preferential chemokine receptor usage of the isolates, at non-cell-toxic concentrations. The antiretroviral activity of 18-MC resulted in EC (50) values of 22.5 +/- 4.7 microM and 23 +/- 4.5 microM for R5 and X4 isolates, respectively, in PBMCs, and a therapeutic index (TI) of 14.5. Similar findings were observed for inhibition of HIV-1 replication in macrophages: EC (50) equal to 12.8 +/- 5 microM and 9.5 +/- 3 microM for an R5 virus after 14 and 21 days of infection, respectively, with TI equal to 25.6 and 34.5. 18-MC moderately inhibits the HIV-1 enzyme reverse transcriptase (IC (50) = 69.4 microM), which at least partially explains its antiretroviral activity

Interplay between parasite cysteine proteases and the host kinin system modulates microvascular leakage and macrophage infection by promastigotes of the Leishmania donovani complex.

Submitted by Ana Maria Fiscina Sampaio ([email protected]) on 2014-09-18T14:22:56Z No. of bitstreams: 1 Svensjo, Erik- Interplay between parasite........pdf: 540364 bytes, checksum: be1082889aacb96e0eaada59cccfb538 (MD5)Approved for entry into archive by Ana Maria Fiscina Sampaio ([email protected]) on 2014-09-18T14:23:09Z (GMT) No. of bitstreams: 1 Svensjo, Erik- Interplay between parasite........pdf: 540364 bytes, checksum: be1082889aacb96e0eaada59cccfb538 (MD5)Made available in DSpace on 2014-09-18T16:18:30Z (GMT). No. of bitstreams: 1 Svensjo, Erik- Interplay between parasite........pdf: 540364 bytes, checksum: be1082889aacb96e0eaada59cccfb538 (MD5) Previous issue date: 2006Fundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, BrasilUniversidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Rio de Janeiro, RJ, BrasilFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, BrasilFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, BrasilFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, BrasilFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, BrasilUniversidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. Rio de Janeiro, RJ, BrasilUniversidade Federal do Estado de São Paulo. UNIFESP. Escola Paulista de Medicina. Departamento de Biofísica. São Paulo, SP, BrasilUniversidade Federal do Estado de São Paulo. UNIFESP. Escola Paulista de Medicina. Departamento de Biofísica. São Paulo, SP, BrasilUniversity of Frankfurt Medical School. Institute for Biochemistry II. Frankfurt, GermanyFundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, BrasilKinins, the vasoactive peptides proteolytically liberated from kininogens, were recently recognized as signals alerting the innate immune system. Here we demonstrate that Leishmania donovani and Leishmania chagasi, two etiological agents of visceral leishmaniasis (VL), activate the kinin system. Intravital microscopy in the hamster cheek pouch showed that topically applied promastigotes induced macromolecular leakage (FITC-dextran) through postcapillary venules. Peaking at 15 min, the parasite-induced leakage was drastically enhanced by captopril (Cap), an inhibitor of angiotensin-converting enzyme (ACE), a kinin-degrading metallopeptidase. The enhanced microvascular responses were cancelled by HOE-140, an antagonist of the B2 bradykinin receptor (B2R), or by pre-treatment of promastigotes with the irreversible cysteine proteinase inhibitor N-methylpiperazine-urea-Phe-homoPhe-vinylsulfone-benzene (N-Pip-hF-VSPh). In agreement with the above-mentioned data, the promastigotes vigorously induced edema in the paw of Cap-treated J129 mice, but not Cap-B2R–/– mice. Analysis of parasite-induced breakdown of high molecular weight kininogens (HK), combined with active site-affinity-labeling with biotin- N-Pip-hF-VSPh, identified 35–40 kDa proteins as kinin-releasing cysteine peptidases.We then checked if macrophage infectivity was influenced by interplay between these kinin-releasing parasite proteases, kininogens, and kinin-degrading peptidases (i.e. ACE). Our studies revealed that full-fledged B2R engagement resulted in vigorous increase of L. chagasi uptake by resident macrophages. Evidence that inflammatory macrophages treated with HOE-140 became highly susceptible to amastigote outgrowth, assessed 72 h after initial macrophage interaction, further suggests that the kinin/B2R activation pathway may critically modulate inflammation and innate immunity in visceral leishmaniasis