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Spatial organization of protein export in malaria parasite blood stages
Author(s) -
Charnaud Sarah C.,
Jonsdottir Thorey K.,
Sanders Paul R.,
Bullen Hayley E.,
Dickerman Benjamin K.,
Kouskousis Betty,
Palmer Catherine S.,
Pietrzak Halina M.,
Laumaea Annamarie E.,
Erazo AnnaBelen,
McHugh Emma,
Tilley Leann,
Crabb Brendan S.,
Gilson Paul R.
Publication year - 2018
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12577
Subject(s) - translocon , biology , microbiology and biotechnology , parasite hosting , effector , transport protein , plasmodium falciparum , plasmodium (life cycle) , membrane protein , malaria , biochemistry , immunology , membrane , world wide web , computer science
Malaria parasites export proteins into the human erythrocytes they infect. The exported proteins modify the erythrocyte thereby enabling parasite survival. A protein translocon called PTEX (complex of EXP2, PTEX150 and HSP101), encircles the parasite inside the erythrocyte and knockdown of PTEX appears to arrest protein export. To determine if PTEX directly unfolds and exports proteins we made reporters that were chemically resistant to unfolding. We found the reporters became bound to PTEX as if lodged in the complex implicating a direct role for PTEX in export. The compound WR99210 binds to exported reporter protein (Hyp1‐Nluc‐DH) preventing it from being unfolded and resulting in the reporter becoming trapped in the PTEX complex in the parasite. PV, parasitophorous vacuole; ER, endoplasmic reticulum; TVN, tubulo‐vesicular network and RBC, red blood cell.