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...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
BMC
2005-01-01
|
| Series: | Biological Research |
| Subjects: | |
| Online Access: | http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602005000200008 |
| _version_ | 1819034365798121472 |
|---|---|
| author | LORENA AGUILAR GALIA RAMÍREZ CAROLINA VALCK MARÍA C MOLINA ÁLVARO ROJAS WILHELM SCHWAEBLE VIVIANA FERREIRA ARTURO FERREIRA |
| author_facet | LORENA AGUILAR GALIA RAMÍREZ CAROLINA VALCK MARÍA C MOLINA ÁLVARO ROJAS WILHELM SCHWAEBLE VIVIANA FERREIRA ARTURO FERREIRA |
| author_sort | LORENA AGUILAR |
| collection | DOAJ |
| 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 |
| first_indexed | 2024-12-21T07:32:35Z |
| format | Article |
| id | doaj.art-90f6d4a03eab48a899cd7ebc79203653 |
| institution | Directory Open Access Journal |
| issn | 0716-9760 0717-6287 |
| language | English |
| last_indexed | 2024-12-21T07:32:35Z |
| publishDate | 2005-01-01 |
| publisher | BMC |
| record_format | Article |
| series | Biological Research |
| spelling | doaj.art-90f6d4a03eab48a899cd7ebc792036532022-12-21T19:11:32ZengBMCBiological Research0716-97600717-62872005-01-01382-3187195F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complementLORENA AGUILARGALIA RAMÍREZCAROLINA VALCKMARÍA C MOLINAÁLVARO ROJASWILHELM SCHWAEBLEVIVIANA FERREIRAARTURO FERREIRATrypanosoma 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 processhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602005000200008calreticulinC1qF(ab')2 antibody fragmentsTrypanosoma cruzi |
| spellingShingle | LORENA AGUILAR GALIA RAMÍREZ CAROLINA VALCK MARÍA C MOLINA ÁLVARO ROJAS WILHELM SCHWAEBLE VIVIANA FERREIRA ARTURO FERREIRA F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement Biological Research calreticulin C1q F(ab')2 antibody fragments Trypanosoma cruzi |
| title | 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_short | 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 |
| topic | calreticulin C1q F(ab')2 antibody fragments Trypanosoma cruzi |
| url | http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602005000200008 |
| work_keys_str_mv | AT lorenaaguilar fab2antibodyfragmentsagainsttrypanosomacruzicalreticulininhibititsinteractionwiththefirstcomponentofhumancomplement AT galiaramirez fab2antibodyfragmentsagainsttrypanosomacruzicalreticulininhibititsinteractionwiththefirstcomponentofhumancomplement AT carolinavalck fab2antibodyfragmentsagainsttrypanosomacruzicalreticulininhibititsinteractionwiththefirstcomponentofhumancomplement AT mariacmolina fab2antibodyfragmentsagainsttrypanosomacruzicalreticulininhibititsinteractionwiththefirstcomponentofhumancomplement AT alvarorojas fab2antibodyfragmentsagainsttrypanosomacruzicalreticulininhibititsinteractionwiththefirstcomponentofhumancomplement AT wilhelmschwaeble fab2antibodyfragmentsagainsttrypanosomacruzicalreticulininhibititsinteractionwiththefirstcomponentofhumancomplement AT vivianaferreira fab2antibodyfragmentsagainsttrypanosomacruzicalreticulininhibititsinteractionwiththefirstcomponentofhumancomplement AT arturoferreira fab2antibodyfragmentsagainsttrypanosomacruzicalreticulininhibititsinteractionwiththefirstcomponentofhumancomplement |