The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites
3
Issued Date
2025-01-01
Resource Type
eISSN
22352988
Scopus ID
2-s2.0-105006471374
Journal Title
Frontiers in Cellular and Infection Microbiology
Volume
15
Rights Holder(s)
SCOPUS
Bibliographic Citation
Frontiers in Cellular and Infection Microbiology Vol.15 (2025)
Suggested Citation
Phong Z.Y., Chin J.Y., Ng Y.L., Zakaria N.I., Athirah-Azman S.N., Kosaisavee V., Rénia L., Lee W.C. The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites. Frontiers in Cellular and Infection Microbiology Vol.15 (2025). doi:10.3389/fcimb.2025.1599872 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/110465
Title
The role of periostin (OSF-2) in the cytoadherence phenomena mediated by malaria parasites
Corresponding Author(s)
Other Contributor(s)
Abstract
Introduction: The 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). Methods: Laboratory-adapted P. falciparum and P. knowlesi isolates were cultured, and the late-stage parasites were purified for experiments using recombinant human OSF-2. Results: We 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. Discussion: This work contributes to our understanding of the host-parasite interactions in malaria pathobiology.