An exported kinase family mediates species-specific erythrocyte remodelling and virulence in human malaria.
Erythrocytes
/ metabolism
Gene Deletion
Gene Knockdown Techniques
Gene Targeting
Humans
Malaria
/ metabolism
Multigene Family
Phosphoproteins
Phosphorylation
Phosphotransferases
/ genetics
Plasmodium
/ physiology
Protein Interaction Mapping
Protein Interaction Maps
Proteomics
/ methods
Protozoan Proteins
/ metabolism
Species Specificity
Virulence
Journal
Nature microbiology
ISSN: 2058-5276
Titre abrégé: Nat Microbiol
Pays: England
ID NLM: 101674869
Informations de publication
Date de publication:
06 2020
06 2020
Historique:
received:
18
11
2019
accepted:
05
03
2020
pubmed:
15
4
2020
medline:
21
10
2020
entrez:
15
4
2020
Statut:
ppublish
Résumé
The most severe form of human malaria is caused by Plasmodium falciparum. Its virulence is closely linked to the increase in rigidity of infected erythrocytes and their adhesion to endothelial receptors, obstructing blood flow to vital organs. Unlike other human-infecting Plasmodium species, P. falciparum exports a family of 18 FIKK serine/threonine kinases into the host cell, suggesting that phosphorylation may modulate erythrocyte modifications. We reveal substantial species-specific phosphorylation of erythrocyte proteins by P. falciparum but not by Plasmodium knowlesi, which does not export FIKK kinases. By conditionally deleting all FIKK kinases combined with large-scale quantitative phosphoproteomics we identified unique phosphorylation fingerprints for each kinase, including phosphosites on parasite virulence factors and host erythrocyte proteins. Despite their non-overlapping target sites, a network analysis revealed that some FIKKs may act in the same pathways. Only the deletion of the non-exported kinase FIKK8 resulted in reduced parasite growth, suggesting the exported FIKKs may instead support functions important for survival in the host. We show that one kinase, FIKK4.1, mediates both rigidification of the erythrocyte cytoskeleton and trafficking of the adhesin and key virulence factor PfEMP1 to the host cell surface. This establishes the FIKK family as important drivers of parasite evolution and malaria pathology.
Identifiants
pubmed: 32284562
doi: 10.1038/s41564-020-0702-4
pii: 10.1038/s41564-020-0702-4
pmc: PMC7116245
mid: EMS85986
doi:
Substances chimiques
Phosphoproteins
0
Protozoan Proteins
0
Phosphotransferases
EC 2.7.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
848-863Subventions
Organisme : Medical Research Council
ID : FC001189
Pays : United Kingdom
Organisme : Cancer Research UK
ID : FC001999
Pays : United Kingdom
Organisme : Department of Health
Pays : United Kingdom
Organisme : Wellcome Trust
ID : FC001999
Pays : United Kingdom
Organisme : Medical Research Council
ID : FC001999
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/P010288/1
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 206508/Z/17/Z
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 206508
Pays : United Kingdom
Organisme : Wellcome Trust
ID : FC001189
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Cancer Research UK
ID : FC001189
Pays : United Kingdom
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