Mbengue Alassane, Vialla Emilie, Berry Laurence, Fall Gamou, Audiger Nicolas, Demettre-Verceil Edith, Boteller David, Braun-Breton Catherine
University Montpellier II, CNRS UMR 5235, University Montpellier I, Dynamique des Interactions Membranaires Normales et Pathologiques, 34095, Montpellier Cedex 5, France.
Traffic. 2015 May;16(5):461-75. doi: 10.1111/tra.12266. Epub 2015 Feb 24.
The export of numerous proteins to the plasma membrane of its host erythrocyte is essential for the virulence and survival of the malaria parasite Plasmodium falciparum. The Maurer's clefts, membrane structures transposed by the parasite in the cytoplasm of its host erythrocyte, play the role of a marshal platform for such exported parasite proteins. We identify here the export pathway of three resident proteins of the Maurer's clefts membrane: the proteins are exported as soluble forms in the red cell cytoplasm to the Maurer's clefts membrane in association with the parasite group II chaperonin (PfTRIC), a chaperone complex known to bind and address a large spectrum of unfolded proteins to their final location. We have also located the domain of interaction with PfTRiC within the amino-terminal domain of one of these Maurer's cleft proteins, PfSBP1. Because several Maurer's cleft membrane proteins with different export motifs seem to follow the same route, we propose a general role for PfTRiC in the trafficking of malarial parasite proteins to the host erythrocyte.
众多蛋白质向其宿主红细胞质膜的输出对于恶性疟原虫的毒力和存活至关重要。疟原虫在其宿主红细胞细胞质中移位形成的膜结构——毛雷尔氏小带，充当此类输出的寄生虫蛋白的整合平台。我们在此确定了毛雷尔氏小带膜的三种驻留蛋白的输出途径：这些蛋白以可溶性形式在红细胞细胞质中输出至毛雷尔氏小带膜，与寄生虫第二组伴侣蛋白（PfTRIC）相关联，PfTRIC是一种已知能结合大量未折叠蛋白并将其运送至最终位置的伴侣蛋白复合体。我们还在其中一种毛雷尔氏小带蛋白PfSBP1的氨基末端结构域内定位了与PfTRiC相互作用的结构域。由于几种具有不同输出基序的毛雷尔氏小带膜蛋白似乎遵循相同途径，我们提出PfTRiC在疟原虫蛋白向宿主红细胞的运输中具有普遍作用。
