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Abstract
Among several protease inhibitors tested, only leupeptin was found to modify qualitatively
the processing of P126, a major antigen of the parasitophorous vacuole of Plasmodium
falciparum, and to inhibit the release of merozoites. Whereas P126 is normally processed
upon merozoite release into 2 polypeptides of 50 and 73 kDa which are discharged in
the culture medium, leupeptin treatment led to the recovery of a 56 kDa fragment which
was recognized by a monoclonal antibody specific for the 50 kDa polypeptide and of
a 73 kDa fragment comigrating with the one obtained in normal culture conditions.
Mild trypsinization of the 56 kDa polypeptide gave rise to a 50 kDa product the tryptic
fragments of which comigrated with those of the 50 kDa antigen obtained from untreated
cultures.