New Export Pathway in Plasmodium falciparum‐Infected Erythrocytes: Role of the Parasite Group II Chaperonin,PfTRiC |
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Authors: | Alassane Mbengue Emilie Vialla Laurence Berry Gamou Fall Nicolas Audiger Edith Demettre‐Verceil David Boteller Catherine Braun‐Breton |
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Institution: | 1. University Montpellier II, CNRS UMR 5235, University Montpellier I, Montpellier Cedex 5, France;2. Plate‐forme de Protéomique Fonctionnelle ‐ FPP, UMS CNRS 3426 ‐ US 009 INSERM ‐ UMI ‐ UMII, IGF, Montpellier Cedex 5, France |
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Abstract: | 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. ![image](https://wol-prod-cdn.literatumonline.com/cms/attachment/95da4c5f-1aab-4eda-a466-6de7f4b1964d/tra12266-gra-0001.png) |
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Keywords: | erythrocyte malaria Plasmodium falciparum protein export TRiC group II chaperonin |
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