Time-resolved proximity biotinylation implicates a porin protein in export of transmembrane malaria parasite effectors

Author:

Anaguano David12,Dedkhad Watcharatip12ORCID,Brooks Carrie F.2,Cobb David W.12,Muralidharan Vasant12ORCID

Affiliation:

1. University of Georgia 1 Department of Cellular Biology , , Athens, GA , USA

2. Center for Tropical and Emerging Global Diseases, University of Georgia 2 , Athens, GA 30602 , USA

Abstract

ABSTRACT The malaria-causing parasite, Plasmodium falciparum completely remodels its host red blood cell (RBC) through the export of several hundred parasite proteins, including transmembrane proteins, across multiple membranes to the RBC. However, the process by which these exported membrane proteins are extracted from the parasite plasma membrane for export remains unknown. To address this question, we fused the exported membrane protein, skeleton binding protein 1 (SBP1), with TurboID, a rapid, efficient and promiscuous biotin ligase (SBP1TbID). Using time-resolved proximity biotinylation and label-free quantitative proteomics, we identified two groups of SBP1TbID interactors – early interactors (pre-export) and late interactors (post-export). Notably, two promising membrane-associated proteins were identified as pre-export interactors, one of which possesses a predicted translocon domain, that could facilitate the export of membrane proteins. Further investigation using conditional mutants of these candidate proteins showed that these proteins were essential for asexual growth and localize to the host–parasite interface during early stages of the intraerythrocytic cycle. These data suggest that they might play a role in ushering membrane proteins from the parasite plasma membrane for export to the host RBC.

Funder

National Institutes of Health

University of Georgia

Publisher

The Company of Biologists

Subject

Cell Biology

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