MALCHIODI Emilio Luis
Redirection of the immune response to the functional catalytic domain of cruzipain improves protective immunity against Trypanosoma cruzi infection
CAZORLA SI, FRANK FM, BECKER PD, ARNAIZ M, MIRKIN GA, CORRAL RS, GUZMAN CA, MALCHIODI EL
JOURNAL OF INFECTIOUS DISEASES
UNIV CHICAGO PRESS
Año: 2010 vol. 202 p. 136 - 144
Despite the strong responses elicited after natural infection or vaccination, Trypanosoma cruzi survival suggests that immune 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 employing recombinant cruzipain (rCz) or its N- and C-terminal domains allowed to dissect the ability of Cz to circumvent responses against the catalytic domain. This phenomenon is not a property of the parasite, but of Cz itself, since rCz triggers a similar effect to Cz during natural or experimental infection. Cz is not the only antigen having a highly immunogenic region of unknown function which somehow protects an essential domain for parasite survival, suggesting an overall immune escape strategy developed during evolution. However, our studies show that this can be reverted by using the N-terminal domain as tailored immunogen able to redirect host responses to provide enhanced protection.