The cytoplasmic region of Plasmodium falciparum SURFIN4.2 is required for transport from Maurer’s clefts to the red blood cell surface
10.2149/tmh.2015-38
- Author:
Wataru Kagaya
;
Shinya Miyazaki
;
Kazuhide Yahata
;
Nobuo Ohta
;
Osamu Kaneko
- Publication Type:Journal Article
- Keywords:
malaria;
Maurer’s clefts;
Plasmodium falciparum protein transport;
SURFIN
- From:Tropical Medicine and Health
2015;advpub(0):-
- CountryJapan
- Language:English
-
Abstract:
Background: Plasmodium, the causative agent of malaria, exports many proteinsto the surface of the infected red blood cell (iRBC) in order to modify ittoward a structure more suitable for parasite development and survival. Onesuch exported protein, SURFIN4.2, from the parasite of humanmalignant malaria, P. falciparum, wasidentified in the trypsin-cleaved protein fraction from the iRBC surface, andis thereby inferred to be exposed on the iRBC surface. SURFIN4.2 alsolocalize to Maurer’s clefts – parasite-derived membranous structures establishedin the RBC cytoplasm and tethered to the RBC membrane – and their role intrafficking suggests that they are a pathway for SURFIN4.2 transportto the iRBC surface. It has not been determined the participation of proteindomains and motifs within SURFIN4.2 in transport from Maurer’sclefts to the iRBC surface; and herein we examined if the SURFIN4.2 intracellularregion containing tryptophan-rich (WR) domain is required for its exposure on theiRBC surface. Results: We generated two transgenic parasite lineswhich express modified SURFIN4.2, with or without a part of the intracellularregion. Both recombinant SURFIN4.2 proteins were exported to Maurer’sclefts. However, only SURFIN4.2 possessing the intracellular region wasefficiently cleaved by surface treatment of iRBC with proteinase K. Conclusions: These results indicate that SURFIN4.2is exposed on the iRBC surface and that the intracellular region containing WRdomain plays arole on the transport from Maurer’s clefts to the iRBC membrane.
