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Fc‐binding molecules specific for human IgG1 and IgG3 are present in Echinococcus granulosus protoscoleces
Author(s) -
BAZ ADRIANA,
CAROL HERNÁN,
MARCO MARTA,
CASABÓ LUCÍA,
JONES FRANCES,
DUNNE DAVID,
NIETO ALBERTO
Publication year - 1998
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1046/j.1365-3024.1998.00147.x
Subject(s) - biology , echinococcus granulosus , monoclonal antibody , viral tegument , immunoglobulin e , antigen , microbiology and biotechnology , affinity chromatography , antibody , sepharose , subclass , parasite hosting , immunology , biochemistry , virology , enzyme , zoology , world wide web , computer science
In this work we describe the presence of Fc‐binding activity on the suckers and tegument of E. granulosus protoscoleces. A fraction (PSA‐Fc + ) from protoscolex somatic antigens was isolated by affinity chromatography on human Fc‐γ1‐Sepharose. Analysis by SDS‐PAGE of PSA‐Fc + showed that it contained two major components. Using mouse F(ab′)2‐human Fc chimaeric monoclonal antibodies we verified that PSA‐Fc + bound mainly to human Fc‐γ1 and Fc‐γ3 isotypes. In addition, one of the components of PSA‐Fc + showed proteolytic activity. Both, Fc‐binding and proteolytic activities localized on the protoscolex surface, may play a relevant role in the host‐parasite interaction .