作者: Asrar Alam , Virander S Chauhan , None
DOI: 10.1371/JOURNAL.PONE.0030452
关键词:
摘要: Plasmodium falciparum serine repeat antigen 5 (SERA5) is a target for both drug and vaccine intervention against malaria. SERA5 secreted in the parasitophorous vacuole where it proteolytically processed before schizont rupture. Among products 50.8-kDa central domain of protease, which possesses chymotrypsin-like activity consists 28.9-kDa catalytic with 21.9-kDa N-terminal prodomain, remain attached together. Because has been implicated merozoite egress from host erythrocytes, effect prodomain heptapeptide derived its C-terminus spanning D560 to F566 (DNSDNMF) on parasite growth was studied. When E. coli-expressed incubated culture, significant delay transition ring stages observed up nanomolar concentrations. The peptide, DNSDNMF also showed similar effects but at nearly 1000-fold higher peptide found interact domain. These data demonstrate crucial role process. Given inhibitory potential parasite, we suggest that peptidomimetic inhibitors based sequences can be developed as future therapeutics