Recruitment of human aquaporin 3 to internal membranes in the Plasmodium falciparum infected erythrocyte.
The molecular mechanisms underlying the formation of the parasitophorous vacuolar membrane in Plasmodium falciparum infected erythrocytes are incompletely understood, and the protein composition of this membrane is still enigmatic. Although the differentiated mammalian erythrocyte lacks the machinery required for endocytosis, some reports have described a localisation of host cell membrane proteins at the parasitophorous vacuolar membrane. Aquaporin 3 is an abundant plasma membrane protein of various cells, including mammalian erythrocytes where it is found in distinct oligomeric states. Here we show that human aquaporin 3 is internalized into infected erythrocytes, presumably during or soon after invasion. It is integrated into the PVM where it is organized in novel oligomeric states which are not found in non-infected cells.
Bietz
Sven
S
Department of Parasitology, Faculty of Biology, Philipps Universität, 35032 Marburg, Germany.
Montilla
Irine
I
Külzer
Simone
S
Przyborski
Jude M
JM
Lingelbach
Klaus
K
D000818:Animals; D051400:Aquaporin 3 / Q000032:analysis*; D002462:Cell Membrane / Q000737:chemistry*; D004912:Erythrocytes / Q000469:parasitology*; D006801:Humans; D010963:Plasmodium falciparum / Q000254:growth & development*; D014617:Vacuoles / Q000469:parasitology*
C496027:AQP3 protein, human; D051400:Aquaporin 3