An exported protein of Plasmodium falciparum is synthesized as an integral membrane protein.

Abstract:

:Exp-1 is an antigen of Plasmodium falciparum which is transported from the parasite cell to the membrane of the parasitophorous vacuole and to membranous compartments in the erythrocyte. To investigate how this protein is transported, we studied the synthesis and membrane translocation of exp-1 in a cell-free system. The protein was translocated into canine pancreatic microsomes. Its N-terminal half was thus protected from proteinase K digestion, suggesting that exp-1 is an integral membrane protein with its N-terminus facing the lumen of the microsomes. This conclusion has been confirmed in vivo. In parasitized erythrocytes, exp-1 is membrane-associated and resistant to extraction with alkali, as would be expected for an integral membrane protein. Moreover, using segment-specific monoclonal antibodies, we have shown that here again the N-terminus of exp-1 faces the inside of vesicles, inaccessible to proteases, whereas the C-terminus is degraded. We conclude that exp-1 is an integral membrane protein and infer that it is transported by vesicles from the parasite to a compartment in the host cell cytoplasm.

journal_name

Mol Biochem Parasitol

authors

Günther K,Tümmler M,Arnold HH,Ridley R,Goman M,Scaife JG,Lingelbach K

doi

10.1016/0166-6851(91)90208-n

subject

Has Abstract

pub_date

1991-05-01 00:00:00

pages

149-57

issue

1

eissn

0166-6851

issn

1872-9428

pii

0166-6851(91)90208-N

journal_volume

46

pub_type

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