@article{oai:nagasaki-u.repo.nii.ac.jp:00013564,
 author = {Alexandre, Jean Semé Fils and Yahata, Kazuhide and Kawai, Satoru and Torii, Motomi and Kaneko, Osamu},
 issue = {3},
 journal = {Parasitology International},
 month = {Sep},
 note = {SURFIN(4.2) is a parasite-infected red blood cell (iRBC) surface associated protein of Plasmodium falciparum. To analyze the region responsible for the intracellular trafficking of SURFIN(4.2) to the iRBC and Maurer's clefts, a panel of transgenic parasite lines expressing recombinant SURFIN(4.2) fused with green fluorescent protein was generated and evaluated for their localization. We found that the cytoplasmic region containing a tryptophan rich (WR) domain is not necessary for trafficking, whereas the transmembrane (TM) region was. Two PEXEL-like sequences were shown not to be responsible for the trafficking of SURFIN(4.2), demonstrating that the protein is trafficked in a PEXEL-independent manner. N-terminal replacement, deletion of the cysteine-rich domain or the variable region also did not prevent the protein from localizing at the iRBC or Maurer's clefts. A recombinant SURFIN(4.2) protein possessing 50 amino acids upstream of the TM region, TM region itself and a part of the cytoplasmic region was shown to be trafficked into the iRBC and Maurer's clefts, suggesting that there are no essential trafficking motifs in the SURFIN(4.2) extracellular region. A mini-SURFIN(4.2) protein containing WR domain was shown by Western blotting to be more abundantly detected in a Triton X-100-insoluble fraction, compared to the one without WR domain. We suggest that the cytoplasmic region containing the WR may be responsible for their difference in solubility., Parasitology International, 60(3), pp.313-320; 2011},
 pages = {313--320},
 title = {PEXEL-independent trafficking of Plasmodium falciparum SURFIN4.2 to the parasite-infected red blood cell and Maurer's clefts.},
 volume = {60},
 year = {2011}
}