Structural insights into Plasmodium PPIases
Malaria is one of the most prevalent infectious diseases posing a serious challenge over the years, mainly owing to the emergence of drug-resistant strains, sparking a need to explore and identify novel protein targets. It is a well-known practice to adopt a chemo-genomics approach towards identifyi...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-09-01
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| Series: | Frontiers in Cellular and Infection Microbiology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fcimb.2022.931635/full |
| _version_ | 1797999597947191296 |
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| author | Sreekanth Rajan Ho Sup Yoon Ho Sup Yoon Ho Sup Yoon |
| author_facet | Sreekanth Rajan Ho Sup Yoon Ho Sup Yoon Ho Sup Yoon |
| author_sort | Sreekanth Rajan |
| collection | DOAJ |
| description | Malaria is one of the most prevalent infectious diseases posing a serious challenge over the years, mainly owing to the emergence of drug-resistant strains, sparking a need to explore and identify novel protein targets. It is a well-known practice to adopt a chemo-genomics approach towards identifying targets for known drugs, which can unravel a novel mechanism of action to aid in better drug targeting proficiency. Immunosuppressive drugs cyclosporin A, FK506 and rapamycin, were demonstrated to inhibit the growth of the malarial parasite, Plasmodium falciparum. Peptidyl prolyl cis/trans isomerases (PPIases), comprising cylcophilins and FK506-binding proteins (FKBPs), the specific target of these drugs, were identified in the Plasmodium parasite and proposed as an antimalarial drug target. We previously attempted to decipher the structure of these proteins and target them with non-immunosuppressive drugs, predominantly on FKBP35. This review summarizes the structural insights on Plasmodium PPIases, their inhibitor complexes and perspectives on drug discovery. |
| first_indexed | 2024-04-11T11:07:15Z |
| format | Article |
| id | doaj.art-3f6ef89c8e234518afef5089320355e0 |
| institution | Directory Open Access Journal |
| issn | 2235-2988 |
| language | English |
| last_indexed | 2024-04-11T11:07:15Z |
| publishDate | 2022-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cellular and Infection Microbiology |
| spelling | doaj.art-3f6ef89c8e234518afef5089320355e02022-12-22T04:28:14ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882022-09-011210.3389/fcimb.2022.931635931635Structural insights into Plasmodium PPIasesSreekanth Rajan0Ho Sup Yoon1Ho Sup Yoon2Ho Sup Yoon3School of Biological Sciences, Nanyang Technological University, Singapore, SingaporeSchool of Biological Sciences, Nanyang Technological University, Singapore, SingaporeCollege of Pharmacy, CHA University, Pocheon-si, South KoreaCHA Advanced Research Institute, Seongnam-si, South KoreaMalaria is one of the most prevalent infectious diseases posing a serious challenge over the years, mainly owing to the emergence of drug-resistant strains, sparking a need to explore and identify novel protein targets. It is a well-known practice to adopt a chemo-genomics approach towards identifying targets for known drugs, which can unravel a novel mechanism of action to aid in better drug targeting proficiency. Immunosuppressive drugs cyclosporin A, FK506 and rapamycin, were demonstrated to inhibit the growth of the malarial parasite, Plasmodium falciparum. Peptidyl prolyl cis/trans isomerases (PPIases), comprising cylcophilins and FK506-binding proteins (FKBPs), the specific target of these drugs, were identified in the Plasmodium parasite and proposed as an antimalarial drug target. We previously attempted to decipher the structure of these proteins and target them with non-immunosuppressive drugs, predominantly on FKBP35. This review summarizes the structural insights on Plasmodium PPIases, their inhibitor complexes and perspectives on drug discovery.https://www.frontiersin.org/articles/10.3389/fcimb.2022.931635/fullmalariaplasmodiumPPIaseFKBPcyclophilinFK506 |
| spellingShingle | Sreekanth Rajan Ho Sup Yoon Ho Sup Yoon Ho Sup Yoon Structural insights into Plasmodium PPIases Frontiers in Cellular and Infection Microbiology malaria plasmodium PPIase FKBP cyclophilin FK506 |
| title | Structural insights into Plasmodium PPIases |
| title_full | Structural insights into Plasmodium PPIases |
| title_fullStr | Structural insights into Plasmodium PPIases |
| title_full_unstemmed | Structural insights into Plasmodium PPIases |
| title_short | Structural insights into Plasmodium PPIases |
| title_sort | structural insights into plasmodium ppiases |
| topic | malaria plasmodium PPIase FKBP cyclophilin FK506 |
| url | https://www.frontiersin.org/articles/10.3389/fcimb.2022.931635/full |
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