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Medientyp:
E-Artikel
Titel:
A member of the tryptophan-rich protein family is required for efficient sequestration of Plasmodium berghei schizonts
Beteiligte:
Gabelich, Julie-Anne;
Grützke, Josephine;
Kirscht, Florian;
Popp, Oliver;
Matz, Joachim M.;
Dittmar, Gunnar;
Rug, Melanie;
Ingmundson, Alyssa
Erschienen:
Public Library of Science (PLoS), 2022
Erschienen in:PLOS Pathogens
Sprache:
Englisch
DOI:
10.1371/journal.ppat.1010846
ISSN:
1553-7374
Entstehung:
Anmerkungen:
Beschreibung:
<jats:p>Protein export and host membrane remodeling are crucial for multiple <jats:italic>Plasmodium</jats:italic> species to establish a niche in infected hosts. To better understand the contribution of these processes to successful parasite infection <jats:italic>in vivo</jats:italic>, we sought to find and characterize protein components of the intraerythrocytic <jats:italic>Plasmodium berghei</jats:italic>-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 <jats:italic>P</jats:italic>. <jats:italic>berghei</jats:italic>-infected erythrocytes. In parallel, we also report our data describing proteins that co-precipitate with the PTEX (<jats:italic>Plasmodium</jats:italic> translocon of exported proteins) component EXP2. To validate our findings, we examined the location of three candidate IBIS1-interactors that are conserved across multiple <jats:italic>Plasmodium</jats:italic> 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 <jats:italic>Plasmodium</jats:italic>-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 <jats:italic>P</jats:italic>. <jats:italic>berghei</jats:italic>-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.</jats:p>