Decoding substrate recognition in malapain-2 through structural and mutational insights.

ABSTRACT: Cysteine proteases of the falcipain (FP) family are essential for the survival and pathogenicity of Plasmodium parasites and represent promising targets for antimalarial drug development. These enzymes mediate haemoglobin degradation during the intraerythrocytic stage, providing nutrients and facilitating parasite growth. While FP-family proteases from P. falciparum (e.g., FP-2A and FP-3) are well-characterized, their orthologs in less-studied species like P. malariae remain poorly understood. Given the rising concern over drug-resistant malaria and mixed-species infections, targeting diverse FP-family ortholog enzymes in other human malaria parasites is a timely and promising therapeutic strategy. In this study, we investigated malapain-2 (MP-2), a cysteine protease f

SUBMITTER: D'silva S 

PROVIDER: S-EPMC12617615 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature