Show simple item record

dc.contributor.authorCazorla, Silvia I
dc.contributor.authorFrank, Fernanda M
dc.contributor.authorBecker, Pablo D
dc.contributor.authorArnaiz, María
dc.contributor.authorMirkin, Gerardo A
dc.contributor.authorCorral, Ricardo S
dc.contributor.authorGuzmán, Carlos A
dc.contributor.authorMalchiodi, Emilio L
dc.date.accessioned2011-01-14T11:31:08Z
dc.date.available2011-01-14T11:31:08Z
dc.date.issued2010-07-01
dc.identifier.citationRedirection of the immune response to the functional catalytic domain of the cystein proteinase cruzipain improves protective immunity against Trypanosoma cruzi infection. 2010, 202 (1):136-44 J. Infect. Dis.en
dc.identifier.issn1537-6613
dc.identifier.pmid20497050
dc.identifier.doi10.1086/652872
dc.identifier.urihttp://hdl.handle.net/10033/119387
dc.description.abstractDespite the strong immune responses elicited after natural infection with Trypanosoma cruzi or vaccination against it, parasite survival suggests that these responses are insufficient or inherently inadequate. T. cruzi contains a major cystein proteinase, cruzipain, which has a catalytic N-terminal domain and a C-terminal extension. Immunizations that employed recombinant cruzipain or its N- and C-terminal domains allowed evaluation of the ability of cruzipain to circumvent responses against the catalytic domain. This phenomenon is not a property of the parasite but of cruzipain itself, because recombinant cruzipain triggers a response similar to that of cruzipain during natural or experimental infection. Cruzipain is not the only antigen with a highly immunogenic region of unknown function that somehow protects an essential domain for parasite survival. However, our studies show that this can be reverted by using the N-terminal domain as a tailored immunogen able to redirect host responses to provide enhanced protection.
dc.language.isoenen
dc.subject.meshAnimalsen
dc.subject.meshAntibodies, Protozoanen
dc.subject.meshChagas Diseaseen
dc.subject.meshCysteine Endopeptidasesen
dc.subject.meshFemaleen
dc.subject.meshMiceen
dc.subject.meshMice, Inbred C3Hen
dc.subject.meshMuscle, Skeletalen
dc.subject.meshMyocardiumen
dc.subject.meshProtozoan Proteinsen
dc.subject.meshProtozoan Vaccinesen
dc.subject.meshRecombinant Proteinsen
dc.subject.meshTrypanosoma cruzien
dc.titleRedirection of the immune response to the functional catalytic domain of the cystein proteinase cruzipain improves protective immunity against Trypanosoma cruzi infection.en
dc.typeArticleen
dc.contributor.departmentCátedra de Inmunología and Instituto de Estudios de la Inmunidad Humoral (IDEHU), Universidad de BuenosAires, 1113 Buenos Aires, Argentina.en
dc.identifier.journalThe Journal of infectious diseasesen
refterms.dateFOA2011-07-15T00:00:00Z
html.description.abstractDespite the strong immune responses elicited after natural infection with Trypanosoma cruzi or vaccination against it, parasite survival suggests that these responses are insufficient or inherently inadequate. T. cruzi contains a major cystein proteinase, cruzipain, which has a catalytic N-terminal domain and a C-terminal extension. Immunizations that employed recombinant cruzipain or its N- and C-terminal domains allowed evaluation of the ability of cruzipain to circumvent responses against the catalytic domain. This phenomenon is not a property of the parasite but of cruzipain itself, because recombinant cruzipain triggers a response similar to that of cruzipain during natural or experimental infection. Cruzipain is not the only antigen with a highly immunogenic region of unknown function that somehow protects an essential domain for parasite survival. However, our studies show that this can be reverted by using the N-terminal domain as a tailored immunogen able to redirect host responses to provide enhanced protection.


Files in this item

Thumbnail
Name:
Cazorla et al_final.pdf
Size:
666.9Kb
Format:
PDF
Description:
allowed publisher's PDF

This item appears in the following Collection(s)

Show simple item record