OpenLink Software

About: Invasion of human erythrocytes by Plasmodium falciparum merozoites involves multiple interactions between host receptors and their merozoite ligands. Here we report human Cyclophilin B as a receptor for PfRhopH3 during merozoite invasion. Localization and binding studies show that Cyclophilin B is present on the erythrocytes and binds strongly to merozoites. We demonstrate that PfRhopH3 binds to the RBCs and their treatment with Cyclosporin A prevents merozoite invasion. We also show a multi-protein complex involving Cyclophilin B and Basigin, as well as PfRhopH3 and PfRh5 that aids the invasion. Furthermore, we report identification of a de novo peptide CDP3 that binds Cyclophilin B and blocks invasion by up to 80%. Collectively, our data provide evidence of compounded interactions between host receptors and merozoite surface proteins and paves the way for developing peptide and small-molecules that inhibit the protein−protein interactions, individually or in toto, leading to abrogation of the invasion process.

 Permalink

an Entity references as follows:

Faceted Search & Find service v1.13.91

Alternative Linked Data Documents: Sponger | ODE     Raw Data in: CXML | CSV | RDF ( N-Triples N3/Turtle JSON XML ) | OData ( Atom JSON ) | Microdata ( JSON HTML) | JSON-LD    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] This material is Open Knowledge Creative Commons License Valid XHTML + RDFa
This work is licensed under a Creative Commons Attribution-Share Alike 3.0 Unported License.
OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Copyright © 2009-2025 OpenLink Software