F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement

Trypanosoma cruzi calreticulin (TcCRT), described in our laboratory, retains several important functional features from its vertebrate homologues. We have shown that recombinant TcCRT inhibits the human complement system when it binds to the collagenous portion of C1q. The generation of classical pa...

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Autores principales:	AGUILAR,LORENA, RAMÍREZ,GALIA, VALCK,CAROLINA, MOLINA,MARÍA C, ROJAS,ÁLVARO, SCHWAEBLE,WILHELM, FERREIRA,VIVIANA, FERREIRA,ARTURO
Lenguaje:	English
Publicado:	Sociedad de Biología de Chile 2005
Materias:	calreticulin C1q F(ab')2 antibody fragments Trypanosoma cruzi
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602005000200008
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spelling	oai:scielo:S0716-976020050002000082007-01-04F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complementAGUILAR,LORENARAMÍREZ,GALIAVALCK,CAROLINAMOLINA,MARÍA CROJAS,ÁLVAROSCHWAEBLE,WILHELMFERREIRA,VIVIANAFERREIRA,ARTURO calreticulin C1q F(ab')2 antibody fragments Trypanosoma cruzi Trypanosoma cruzi calreticulin (TcCRT), described in our laboratory, retains several important functional features from its vertebrate homologues. We have shown that recombinant TcCRT inhibits the human complement system when it binds to the collagenous portion of C1q. The generation of classical pathway convertases and membrane attack complexes is thus strongly inhibited. In most T. cruzi-infected individuals, TcCRT is immunogenic and mediates the generation of specific antibodies. By reverting the C1q / TcCRT interaction, a parasite immune evasion strategy, these antibodies contribute to the host / parasite equilibrium. In an in vitro correlate of this situation, we show that the C1q / TcCRT interaction is inhibited by F(ab')2 polyclonal anti-TcCRT IgG fragments. It is therefore feasible that in infected humans anti-TcCRT antibodies participate in reverting an important parasite strategy aimed at inhibiting the classical complement pathway. Thus, membrane-bound TcCRT interacts with the collagenous portion C1q, and this C1q is recognized by the CD91-bound host cell CRT, thus facilitating parasite internalization. Based on our in vitro results, it could be proposed that the in vivo interaction between TcCRT and vertebrate C1q could be inhibited by F(ab')2 fragments anti-rTcCRT or against its S functional domain, thus interfering with the internalization processinfo:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.38 n.2-3 20052005-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602005000200008en10.4067/S0716-97602005000200008
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	calreticulin C1q F(ab')2 antibody fragments Trypanosoma cruzi
spellingShingle	calreticulin C1q F(ab')2 antibody fragments Trypanosoma cruzi AGUILAR,LORENA RAMÍREZ,GALIA VALCK,CAROLINA MOLINA,MARÍA C ROJAS,ÁLVARO SCHWAEBLE,WILHELM FERREIRA,VIVIANA FERREIRA,ARTURO F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement
description	Trypanosoma cruzi calreticulin (TcCRT), described in our laboratory, retains several important functional features from its vertebrate homologues. We have shown that recombinant TcCRT inhibits the human complement system when it binds to the collagenous portion of C1q. The generation of classical pathway convertases and membrane attack complexes is thus strongly inhibited. In most T. cruzi-infected individuals, TcCRT is immunogenic and mediates the generation of specific antibodies. By reverting the C1q / TcCRT interaction, a parasite immune evasion strategy, these antibodies contribute to the host / parasite equilibrium. In an in vitro correlate of this situation, we show that the C1q / TcCRT interaction is inhibited by F(ab')2 polyclonal anti-TcCRT IgG fragments. It is therefore feasible that in infected humans anti-TcCRT antibodies participate in reverting an important parasite strategy aimed at inhibiting the classical complement pathway. Thus, membrane-bound TcCRT interacts with the collagenous portion C1q, and this C1q is recognized by the CD91-bound host cell CRT, thus facilitating parasite internalization. Based on our in vitro results, it could be proposed that the in vivo interaction between TcCRT and vertebrate C1q could be inhibited by F(ab')2 fragments anti-rTcCRT or against its S functional domain, thus interfering with the internalization process
author	AGUILAR,LORENA RAMÍREZ,GALIA VALCK,CAROLINA MOLINA,MARÍA C ROJAS,ÁLVARO SCHWAEBLE,WILHELM FERREIRA,VIVIANA FERREIRA,ARTURO
author_facet	AGUILAR,LORENA RAMÍREZ,GALIA VALCK,CAROLINA MOLINA,MARÍA C ROJAS,ÁLVARO SCHWAEBLE,WILHELM FERREIRA,VIVIANA FERREIRA,ARTURO
author_sort	AGUILAR,LORENA
title	F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement
title_short	F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement
title_full	F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement
title_fullStr	F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement
title_full_unstemmed	F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement
title_sort	f(ab')2 antibody fragments against trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement
publisher	Sociedad de Biología de Chile
publishDate	2005
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602005000200008
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F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement

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