Novartis Foundation Symposium 226 – Transport and Trafficking in the Malaria–infected Erythrocyte

The Novartis Foundation is an international scientific and educational charity which promotes the study and general knowledge of science and in particular encourages international co-operation in scientific research.

Introduction: host-parasite interrelations in the genomic age H. GINSBURG Erythrocyte membrane transport Z. I. CABANTCHIK Chemical and physical in vitro alterations of the erythrocyte membrane: a model for its pathophysiological states? B. DEUTICKE The effects of transport perturbations on the homeostasis of red blood cells V. LEW and A.R. HOCKADAY Transport properties of the host cell membrane K. KIRK, H.M. STAINES, R.E. MARTIN and K.J. SALIBA Transport of phospholipid synthesis precursors and lipid trafficking into malaria-infected erythrocytes H.J. VIAL, P. ELDIN, D. MARTIN, L. GANNOUN, M. CALAS and M.L. ANCELIN A nutrient-permeable channel on the intraerythrocytic malaria parasite S.A. DESAI The permeability properties of the parasite cell membrane H. GINSBURG Macromolecular transport in malaria-infected erythrocytes T. F. TARASCHI Expression of parasite transporters in Xenopus oocytes S. KRISHNA and C.J. WOODROW Reconstitution of protein transport across the vacuolar membrane in Plasmodium falciparum-infected permeabilized erythrocytes S. BAUMEISTER, A. BURGWEDEL, U.-G. MAIER and K. LINGELBACH Export of parasite proteins to the erythrocyte cytoplasm: secretory machinery and signalling motifs F.R. ALBANO, M. FOLEY and L. TILLEY Transport and trafficking: Toxoplasma as a model for Plasmodium D.S. ROOS, M.J. CRAWFORD, R.G.K. DONALD, L.M. FOHL, K.M. HAGER, J.C. KISSINGER, M.G. REYNOLDS, B. STREIPEN and W.J. SULLIVAN Jr An alternative secretory pathway in Plasmodium: more questions than answers M.F. WISER, D.J. GRAB, and H.N. LANNERS The transport of the histidine-rich protein I from Plasmodium falciparum is insensitive to brefeldin A D. MATTEI, L. BERRY, S. COUFFIN and O. RICHARD Protein transport in the host cell cytoplasm and ATP-binding cassette proteins in Plasmodium falciparum-infected erythrocytes Z. BOZDECH and E. SCHURR Chloroquine uptake and activity is determined by binding to ferriprotoporphyrin IX in Plasmodium faciparum P.G. BRAY, O. JANNEH and S.A. WARD Chloroquine uptake, altered partiitioning and the basis of drug resistance: evidence for chloride dependent ionic regulation J.A. MARTINEY, A.S. FERRER, A. CERAMI, S. DZEKUNOV and P. ROEPE