Participação de proteínas ligantes de heparina na interação entre Toxoplasma gondii e as células hospedeiras

• Ano de defesa: 2003
• Autor(a) principal: Bonilha, Martha Ribeiro
• Tipo de documento: Dissertação
• Tipo de acesso: Acesso aberto
• Idioma: por
• Instituição de defesa: Universidade Federal de Uberlândia; Brasil; Programa de Pós-graduação em Imunologia e Parasitologia Aplicadas
• Palavras-chave em Português: Toxoplasma gondii; Heparina; Adesão; Invasão; Calgranulina A; Heparin; Adhesion; Invasion; CNPQ::CIENCIAS BIOLOGICAS::IMUNOLOGIA; CNPQ::CIENCIAS BIOLOGICAS::PARASITOLOGIA
• Link de acesso: https://repositorio.ufu.br/handle/123456789/29886; http://doi.org/10.14393/ufu.di.2003.63

Toxoplasma gondii is able to invade virtually any nucleated cell, suggesting that this parasite may bind through a ubiquitous receptor. The aim of this study was to identify heparin—binding proteins involved in T. gondii adhesion to host cells, since heparin/heparan sulfate proteoglycans are putative receptors for the parasite. Tachyzoites from RH strain collected from mouse peritoneal exudate or HFF cells were extracted with 1% Triton—X- 100 at 37°C and the soluble fraction was applied onto a heparin affinity column. Heparin ligands were eluted with NaCl and resolved by SDS-PAGE. Proteins ranging in weight from. 5-100kDa were identified and blotted onto a PVDF membrane. A polypeptide of approximately 5kDa was N-terminal sequenced, revealing 100% homology with mouse calgranulin A, a calcium—binding protein. This protein was not dislocated when parasites were washed with 1M NaCl before lysis, indicating a stable binding to the parasite surface. Our results demonstrated that T. gondii tachyzoites might adsorb host heparin-binding proteins, suggesting that the parasite may utilize such proteins, like calgranulin A, to facilitate adhesion and invasion of the host cells