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Biochemical Properties of Two Plasmodium malariae Cysteine Proteases, Malapain-2 and Malapain-4
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Le, Huong Giang | - |
dc.contributor.author | Kang, Jung-Mi | - |
dc.contributor.author | Vo, Tuan Cuong | - |
dc.contributor.author | Yoo, Won Gi | - |
dc.contributor.author | Lee, Kon Ho | - |
dc.contributor.author | Na, Byoung-Kuk | - |
dc.date.accessioned | 2024-05-02T05:40:32Z | - |
dc.date.available | 2024-05-02T05:40:32Z | - |
dc.date.created | 2024-04-29 | - |
dc.date.created | 2024-04-29 | - |
dc.date.issued | 2022-01 | - |
dc.identifier.citation | Microorganisms, Vol.10 No.1, p. 193 | - |
dc.identifier.issn | 2076-2607 | - |
dc.identifier.uri | https://hdl.handle.net/10371/200443 | - |
dc.description.abstract | Cysteine proteases belonging to the falcipain (FP) family play a pivotal role in the biology of malaria parasites and have been extensively investigated as potential antimalarial drug targets. Three paralogous FP-family cysteine proteases of Plasmodium malariae, termed malapains 2-4 (MP2-4), were identified in PlasmoDB. The three MPs share similar structural properties with the FP-2/FP-3 subfamily enzymes and exhibit a close phylogenetic lineage with vivapains (VXs) and knowpains (KPs), FP orthologues of P. vivax and P. knowlesi. Recombinant MP-2 and MP-4 were produced in a bacterial expression system, and their biochemical properties were characterized. Both recombinant MP-2 and MP-4 showed enzyme activity across a broad range of pH values with an optimum activity at pH 5.0 and relative stability at neutral pHs. Similar to the FP-2/FP-3 subfamily enzymes in other Plasmodium species, recombinant MP-2 and MP-4 effectively hydrolyzed hemoglobin at acidic pHs. They also degraded erythrocyte cytoskeletal proteins, such as spectrin and band 3, at a neutral pH. These results imply that MP-2 and MP-4 are redundant hemoglobinases of P. malariae and may also participate in merozoite egression by degrading erythrocyte cytoskeletal proteins. However, compared with other FP-2/FP-3 enzymes, MP-2 showed a strong preference for arginine at the P2 position. Meanwhile, MP-4 showed a primary preference for leucine at the P2 position but a partial preference for phenylalanine. These different substrate preferences of MPs underscore careful consideration in the design of optimized inhibitors targeting the FP-family cysteine proteases of human malaria parasites. | - |
dc.language | 영어 | - |
dc.publisher | MDPI AG | - |
dc.title | Biochemical Properties of Two Plasmodium malariae Cysteine Proteases, Malapain-2 and Malapain-4 | - |
dc.type | Article | - |
dc.identifier.doi | 10.3390/microorganisms10010193 | - |
dc.citation.journaltitle | Microorganisms | - |
dc.identifier.wosid | 000760462700001 | - |
dc.identifier.scopusid | 2-s2.0-85122856135 | - |
dc.citation.number | 1 | - |
dc.citation.startpage | 193 | - |
dc.citation.volume | 10 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Yoo, Won Gi | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | FALCIPARUM | - |
dc.subject.keywordPlus | INHIBITORS | - |
dc.subject.keywordPlus | ERYTHROCYTE | - |
dc.subject.keywordPlus | PROTEINASE | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | E-64 | - |
dc.subject.keywordAuthor | Plasmodium malariae | - |
dc.subject.keywordAuthor | cysteine protease | - |
dc.subject.keywordAuthor | hemoglobin | - |
dc.subject.keywordAuthor | erythrocyte skeletal proteins | - |
dc.subject.keywordAuthor | malapain | - |
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