A member of the tryptophan-rich protein family is required for efficient sequestration of Plasmodium berghei schizonts

Protein export and host membrane remodeling are crucial for multiple Plasmodium species to establish a niche in infected hosts. To better understand the contribution of these processes to successful parasite infection in vivo, we sought to find and characterize protein components of the intraerythro...

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Bibliographic Details
Published in:PLoS pathogens 2022-09, Vol.18 (9), p.e1010846-e1010846
Main Authors: Gabelich, Julie-Anne, Grützke, Josephine, Kirscht, Florian, Popp, Oliver, Matz, Joachim M, Dittmar, Gunnar, Rug, Melanie, Ingmundson, Alyssa
Format: Article
Language:English
Subjects:
Biology and Life Sciences
Blood
Blood cells
Blood circulation
CD36 antigen
Cytoplasm
Engineering and Technology
Erythrocytes
Gene deletion
Health aspects
Infections
Liver
Localization
Malaria
Medicine and Health Sciences
Membrane proteins
Membrane structures
Membranes
Morphology
Parasites
Parasitic diseases
Parasitophorous vacuole
Peptides
Plasmodium
Plasmodium berghei
Prevention
Protein transport
Proteins
Red blood cells
Research and Analysis Methods
Risk factors
Schizonts
Tryptophan
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Summary:Protein export and host membrane remodeling are crucial for multiple Plasmodium species to establish a niche in infected hosts. To better understand the contribution of these processes to successful parasite infection in vivo, we sought to find and characterize protein components of the intraerythrocytic Plasmodium berghei-induced membrane structures (IBIS) that form in the cytoplasm of infected erythrocytes. We identified proteins that immunoprecipitate with IBIS1, a signature member of the IBIS in P. berghei-infected erythrocytes. In parallel, we also report our data describing proteins that co-precipitate with the PTEX (Plasmodium translocon of exported proteins) component EXP2. To validate our findings, we examined the location of three candidate IBIS1-interactors that are conserved across multiple Plasmodium species, and we found they localized to IBIS in infected red blood cells and two further colocalized with IBIS1 in the liver-stage parasitophorous vacuole membrane. Successful gene deletion revealed that these two tryptophan-rich domain-containing proteins, termed here IPIS2 and IPIS3 (for intraerythrocytic Plasmodium-induced membrane structures), are required for efficient blood-stage growth. Erythrocytes infected with IPIS2-deficient schizonts in particular fail to bind CD36 as efficiently as wild-type P. berghei-infected cells and therefore fail to effectively sequester out of the circulating blood. Our findings support the idea that intra-erythrocytic membrane compartments are required across species for alterations of the host erythrocyte that facilitate interactions of infected cells with host tissues.
ISSN:1553-7374
1553-7366
1553-7374
DOI:10.1371/journal.ppat.1010846