A monoclonal antibody against blood forms of Trypanosoma cruzi lyses the parasite in vitro and inhibits host cell invasion

Monoclonal antibodies (mAbs) of the IgM isotypes were produced from mice immunized with blood forms of Trypansoma cruzi Y strain. Characterization of the epitope recognized by one of the mAbs, 164C11, as well as the effects of this mAb on complement-mediated lysis and host cell invasion are reported...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology 1995-01, Vol.50 (1), p.57-70
Main Authors: Gomes, Y.M. (Cidade Universitaria, Recife, Brazil.), Abath, F.G.C, Furtado, A.F, Regis, L.N, Nakasawa, M, Montenegro, L.T, Vouldoukis, I, Alfred-Morin, C, Monjour, L
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal - biosynthesis
Antibodies, Monoclonal - pharmacology
ANTICORPS MONOCLONAL
ANTICUERPOS MONOCLONALES
Cells, Cultured
CHIMIE
Complement Activation
Epitopes - immunology
ETAPAS DE DESARROLLO
FACTEUR IMMUNOLOGIQUE
FACTORES INMUNOLOGICOS
Host-Parasite Interactions
Hybridomas - immunology
IMMUNOLOGIE
In Vitro Techniques
INFECCION
INFECTION
INHIBICION
INHIBITION
INMUNOLOGIA
MEMBRANAS CELULARES
MEMBRANE CELLULAIRE
Mice
QUIMICA
RELACIONES HUESPED PARASITO
RELATION HOTE PARASITE
STADE DE DEVELOPPEMENT
TRYPANOSOMA CRUZI
Trypanosoma cruzi - immunology
Trypanosoma cruzi - physiology
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Summary:Monoclonal antibodies (mAbs) of the IgM isotypes were produced from mice immunized with blood forms of Trypansoma cruzi Y strain. Characterization of the epitope recognized by one of the mAbs, 164C11, as well as the effects of this mAb on complement-mediated lysis and host cell invasion are reported. Immunocytochemical analysis showed that the mAb was reactive with various strains of T. cruzi (Y, WSL, and Colombiana) as well as other trypanosomatids. The mAb 164C11 demonstrated a high complement-mediated lytic activity against bloodstream trypomastigotes, being more effective than chronic mouse serum. A protein with an apparent molecular weight of 72 kDa was detected by this mAb on all developmental stages of T. cruzi. Studies using periodate and endoglycosidase treatments suggested that the epitope is not a carbohydrate and seems to be located on the parasite membrane. In addition, preliminary results are presented, suggesting that the 72-kDa protein is involved in adhesion/or internalization of bloodstream trypomastigotes
ISSN:0273-2289
1559-0291
DOI:10.1007/BF02788040