Article ; Online: Glycophorin B-PfEMP1 interaction mediates robust rosetting in Plasmodium falciparum.
International journal of biological macromolecules
2024 Volume 262, Issue Pt 1, Page(s) 129868
Abstract: P. falciparumerythrocyte membrane protein 1 (PfEMP1) is the major parasite protein responsible for rosetting by binding to host receptors such as heparan sulfate, CR1 on RBC surface. Usually monomeric protein-carbohydrate interactions are weak [1], ... ...
Abstract | P. falciparumerythrocyte membrane protein 1 (PfEMP1) is the major parasite protein responsible for rosetting by binding to host receptors such as heparan sulfate, CR1 on RBC surface. Usually monomeric protein-carbohydrate interactions are weak [1], therefore PfEMP1 binds to plasma proteins like IgM or α2-macroglobulin that facilitate its clustering on parasitized RBC surface and augment rosetting [2,3]. We show that 3D7A expresses PfEMP1, PF3D7_0412900, and employs its CIDRγ2 domain to interact with glycophorin B on uninfected RBC to form large rosettes but more importantly even in the absence of plasma proteins. Overall, we established the role of PF3D7_0412900 in rosetting as antibodies against CIDRγ2 domain reduced rosetting and also identified its receptor, glycophorin B which could provide clue why glycophorin B null phenotype, S-s-U- RBCs prevalent in malaria endemic areas is protective against severe malaria. |
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MeSH term(s) | Humans ; Plasmodium falciparum/metabolism ; Glycophorins/metabolism ; Protozoan Proteins/chemistry ; Erythrocytes/metabolism ; Blood Proteins/metabolism ; Malaria |
Chemical Substances | Glycophorins ; Protozoan Proteins ; Blood Proteins |
Language | English |
Publishing date | 2024-02-02 |
Publishing country | Netherlands |
Document type | Journal Article |
ZDB-ID | 282732-3 |
ISSN | 1879-0003 ; 0141-8130 |
ISSN (online) | 1879-0003 |
ISSN | 0141-8130 |
DOI | 10.1016/j.ijbiomac.2024.129868 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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