A monoclonal antibody directed to terminal residue of beta-galactofuranose of a glycolipid antigen isolated from Paracoccidioides brasiliensis; Cross-reactivity with Leishmania major and Trypanosoma cruzi

• Autor(a) principal: Suzuki, Erika [UNIFESP]
• Data de Publicação: 1997
• Outros Autores: Toledo, Marcos Sergio de [UNIFESP], Takahashi, Helio Kiyoshi [UNIFESP], Straus, Anita Hilda [UNIFESP]
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNIFESP
• Texto Completo: http://dx.doi.org/10.1093/glycob/7.4.463; http://repositorio.unifesp.br/handle/11600/25729
• topic: galactofuranose; glycolipid antigen; monoclonal antibody; Paracoccidioides brasiliensis; Leishmania major

A mouse monoclonal antibody, MEST-1, was produced against Band 1 glycolipid antigen of Paracoccidioides brasiliensis, the glycan structure of Band 1 antigen was recently elucidated and the monosaccharides sequence was defined as: Galf beta 1-->6(Manp alpha 1-->3)Manp beta 1-->2Ins. the reactivity of MEST-1 MAb was determined by solid-phase radioimmunoassay and high performance thin layer chromatography immunostaining. Selective oxidation of galactofuranose residues and inhibition assays with different methyl-glycosides, revealed that MAb MEST-1 is directed against the terminal residue of beta-D-gaiactofuranose of Band 1, a phosphoglyceroglycolipid antigen of P.brasiliensis. By indirect immunofluorescence, it was observed that the epitope recognized by MEST-1 is accessible to the antibody in yeast forms of this fungus. Reactivity of MEST-1 with parasites known to express galactofuranose containing glycoconjugates was also analyzed by indirect immunofluorescence. A positive fluorescence was observed with promastigotes of Leishmania major and epimastigotes of Trypanosoma cruzi, GIPL-1 was identified as the antigen recognized by MEST-1 in Leishmania major, indicating that the MAb MEST-1 recognizes terminal galactofuranose residue in either beta 1-->6 or beta 1-->3 linkage to the mannose.