Leupeptin alters the proteolytic processing of P126, the major parasitophorous vacuole antigen of Plasmodium falciparum.

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.

journal_name

Mol Biochem Parasitol

authors

Debrabant A,Delplace P

doi

10.1016/0166-6851(89)90029-7

subject

Has Abstract

pub_date

1989-03-01 00:00:00

pages

151-8

issue

2

eissn

0166-6851

issn

1872-9428

pii

0166-6851(89)90029-7

journal_volume

33

pub_type

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