4.1 Article

Leishmania chagasi heparin-binding protein: Cell localization and participation in L. chagasi infection

Journal

MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Volume 204, Issue 1, Pages 34-43

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2015.12.005

Keywords

Leishmania; Lectins; Heparin; Visceral leishmaniasis

Funding

  1. Fundacao de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG) [9553 - FAPEMIG CBB - APQ-00668-13]
  2. Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
  3. Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [06/2011]

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Visceral leishmaniasis is a fatal human disease caused by the intracellular protozoan parasite Leishmania chagasi that is captured by host cells in a process involving classics receptors mediated phagocytosis. The search for molecules involved in this process is important to design strategies to disease control. In this work, we verified the presence of heparin-binding protein (HBP) in L. chagasi promastigotes forms. HBP is a lectin of the group of ubiquitous proteins, whose main characteristic is to bind to carbohydrates present in glycoproteins or glycolipids, which is poorly studied in Leishmania species. L. chagasi HBP (HBPLc) was purified by affinity chromatography using heparin-agarose column in FPLC automated system. Its localization in the parasite was assessed by immunolabeling and electronic transmission microscopy tests using anti-HBPLc polyclonal antibodies, which showed HBP spread over the parasite outer surface and internally next to the kynetoplast. In addition, we verified that HBPLc participates in the process of parasite infection, since its blocking with heparin generated a partial reduction in the internalization of Leishmania by RAW macrophages in vitro. According to these results, it is believed that, in further in vivo studies, interference on this parasitic protein may provide us prophylactic and therapeutic alternatives against visceral leishmaniasis. (C) 2015 Elsevier B.V. All rights reserved.

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