The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites
IntroductionThe pathogenesis of severe malaria is primarily attributed to the cytoadherence properties of Plasmodium-infected erythrocytes (IRBC), which include rosetting and IRBC-endothelial cytoadherence. These cytoadherence events are influenced by various parasite- and host-derived factors. Prev...
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Frontiers Media S.A.
2025-05-01
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| Series: | Frontiers in Cellular and Infection Microbiology |
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| author | Zhi-Ying Phong Zhi-Ying Phong Joo-Yie Chin Yee Ling Ng Nurul Izza Zakaria Siti Nur Athirah-Azman Siti Nur Athirah-Azman Varakorn Kosaisavee Laurent Rénia Laurent Rénia Laurent Rénia Wenn-Chyau Lee Wenn-Chyau Lee |
| author_facet | Zhi-Ying Phong Zhi-Ying Phong Joo-Yie Chin Yee Ling Ng Nurul Izza Zakaria Siti Nur Athirah-Azman Siti Nur Athirah-Azman Varakorn Kosaisavee Laurent Rénia Laurent Rénia Laurent Rénia Wenn-Chyau Lee Wenn-Chyau Lee |
| author_sort | Zhi-Ying Phong |
| collection | DOAJ |
| description | IntroductionThe pathogenesis of severe malaria is primarily attributed to the cytoadherence properties of Plasmodium-infected erythrocytes (IRBC), which include rosetting and IRBC-endothelial cytoadherence. These cytoadherence events are influenced by various parasite- and host-derived factors. Previously, antibodies against human periostin (OSF-2), an inflammation-associated protein, were reported to inhibit rosetting. In this study, we aimed to characterize the OSF-2-mediated cytoadherence in infections caused by Plasmodium falciparum (the most fatal human malaria parasite) and P. knowlesi (an emerging, potentially fatal zoonotic malaria parasite).MethodsLaboratory-adapted P. falciparum and P. knowlesi isolates were cultured, and the late-stage parasites were purified for experiments using recombinant human OSF-2.ResultsWe found that OSF-2 at a concentration of 200 ng/ml induced rosette-stimulation in both parasite species. Furthermore, we demonstrated the serum dependency of OSF-2-mediated rosetting. The rosette-stimulating effect of OSF-2 was completely abolished when IRBC were treated with a low concentration of trypsin. This suggests a role for P. falciparum erythrocyte membrane protein 1 (PfEMP1) in OSF-2-mediated rosetting by P. falciparum, and reveals the trypsin-sensitive nature of the P. knowlesi-derived ligands involved in OSF-2-mediated rosetting. We also found that OSF-2-mediated rosetting was independent of the ABO blood group. Additionally, we demonstrated the ability of OSF-2 to disrupt the IRBC-endothelial binding.DiscussionThis work contributes to our understanding of the host-parasite interactions in malaria pathobiology. |
| format | Article |
| id | doaj-art-5d622b78abfc4e3581529b77e386b1a3 |
| institution | OA Journals |
| issn | 2235-2988 |
| language | English |
| publishDate | 2025-05-01 |
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| series | Frontiers in Cellular and Infection Microbiology |
| spelling | doaj-art-5d622b78abfc4e3581529b77e386b1a32025-08-20T02:15:24ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882025-05-011510.3389/fcimb.2025.15998721599872The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasitesZhi-Ying Phong0Zhi-Ying Phong1Joo-Yie Chin2Yee Ling Ng3Nurul Izza Zakaria4Siti Nur Athirah-Azman5Siti Nur Athirah-Azman6Varakorn Kosaisavee7Laurent Rénia8Laurent Rénia9Laurent Rénia10Wenn-Chyau Lee11Wenn-Chyau Lee12Department of Parasitology, Faculty of Medicine, Universiti Malaya, Kuala Lumpur, MalaysiaDepartment of Medical Microbiology, Faculty of Medicine, Universiti Malaya, Kuala Lumpur, MalaysiaDepartment of Parasitology, Faculty of Medicine, Universiti Malaya, Kuala Lumpur, MalaysiaCollaborative Drug Discovery Research (CDDR) Group, Faculty of Pharmacy, Universiti Teknologi MARA (UiTM), Bandar Puncak Alam, Selangor, MalaysiaDepartment of Pathology, Hospital Tengku Ampuan Afzan, Kuantan, Pahang, MalaysiaHigher Institution Centre of Excellence, Tropical Infectious Diseases Research and Education Centre (TIDREC), Universiti Malaya, Kuala Lumpur, MalaysiaInstitute for Advanced Studies, Universiti Malaya, Kuala Lumpur, MalaysiaDepartment of Parasitology and Entomology, Faculty of Public Health, Mahidol University, Bangkok, ThailandLee Kong Chian School of Medicine, Nanyang Technological University (NTU), Singapore, SingaporeSchool of Biological Sciences, Nanyang Technological University (NTU), Singapore, Singapore0A*STAR Infectious Diseases Labs, Agency for Science, Technology and Research (A*STAR), Singapore, SingaporeDepartment of Parasitology, Faculty of Medicine, Universiti Malaya, Kuala Lumpur, Malaysia0A*STAR Infectious Diseases Labs, Agency for Science, Technology and Research (A*STAR), Singapore, SingaporeIntroductionThe pathogenesis of severe malaria is primarily attributed to the cytoadherence properties of Plasmodium-infected erythrocytes (IRBC), which include rosetting and IRBC-endothelial cytoadherence. These cytoadherence events are influenced by various parasite- and host-derived factors. Previously, antibodies against human periostin (OSF-2), an inflammation-associated protein, were reported to inhibit rosetting. In this study, we aimed to characterize the OSF-2-mediated cytoadherence in infections caused by Plasmodium falciparum (the most fatal human malaria parasite) and P. knowlesi (an emerging, potentially fatal zoonotic malaria parasite).MethodsLaboratory-adapted P. falciparum and P. knowlesi isolates were cultured, and the late-stage parasites were purified for experiments using recombinant human OSF-2.ResultsWe found that OSF-2 at a concentration of 200 ng/ml induced rosette-stimulation in both parasite species. Furthermore, we demonstrated the serum dependency of OSF-2-mediated rosetting. The rosette-stimulating effect of OSF-2 was completely abolished when IRBC were treated with a low concentration of trypsin. This suggests a role for P. falciparum erythrocyte membrane protein 1 (PfEMP1) in OSF-2-mediated rosetting by P. falciparum, and reveals the trypsin-sensitive nature of the P. knowlesi-derived ligands involved in OSF-2-mediated rosetting. We also found that OSF-2-mediated rosetting was independent of the ABO blood group. Additionally, we demonstrated the ability of OSF-2 to disrupt the IRBC-endothelial binding.DiscussionThis work contributes to our understanding of the host-parasite interactions in malaria pathobiology.https://www.frontiersin.org/articles/10.3389/fcimb.2025.1599872/fullPlasmodium falciparumPlasmodium knowlesiOSF-2endothelial bindingrosetting |
| spellingShingle | Zhi-Ying Phong Zhi-Ying Phong Joo-Yie Chin Yee Ling Ng Nurul Izza Zakaria Siti Nur Athirah-Azman Siti Nur Athirah-Azman Varakorn Kosaisavee Laurent Rénia Laurent Rénia Laurent Rénia Wenn-Chyau Lee Wenn-Chyau Lee The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites Frontiers in Cellular and Infection Microbiology Plasmodium falciparum Plasmodium knowlesi OSF-2 endothelial binding rosetting |
| title | The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites |
| title_full | The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites |
| title_fullStr | The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites |
| title_full_unstemmed | The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites |
| title_short | The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites |
| title_sort | role of periostin osf 2 in the cytoadherence phenomena mediated by malaria parasites |
| topic | Plasmodium falciparum Plasmodium knowlesi OSF-2 endothelial binding rosetting |
| url | https://www.frontiersin.org/articles/10.3389/fcimb.2025.1599872/full |
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