When the human malaria parasite Plasmodium falciparum infects erythrocytes, proteins associated with host-derived detergent-resistant membrane (DRM) rafts are selectively recruited into the newly formed vacuole, but parasite proteins that contribute to raft-based vacuole development are unknown. In mammalian cells, DRM-associated integral membrane proteins such as caveolin-1 and flotillin-1 that form oligomers have been linked to the formation of DRM-based invaginations called caveolae. Here we show that the P. falciparum genome does not encode caveolins or flotillins but does contain an orthologue of human band 7 stomatin, a protein known to oligomerize, associate with non-caveolar DRMs and is distantly related to flotillins. Stomatins are members of a large protein family conserved in evolution and P. falciparum (Pf) stomatin appears to be a prokaryotic-like molecule. Evidence is presented that it associates with DRMs and may oligomerize, suggesting that these features are conserved in the stomatin family. Further, Pfstomatin is an integral membrane protein concentrated at the apical end of extracellular parasites, where it co-localizes with invasion-associated rhoptry organelles. A resident rhoptry protein, RhopH2 also resides in DRMs. This provides the first evidence that rhoptries of an apicomplexan parasite contain DRM rafts. Further, when the parasite invades erythrocytes, rhoptry Pfstomatin and RhopH2 are inserted into the newly formed vacuole. Thus, like caveolin-1 and flotillin-1, a stomatin may also associate with non-clathrin coated, DRM-enriched vacuoles. We propose a new model of invasion and vacuole formation involving DRM-based interactions of both host and parasite molecules. When the human malaria parasite Plasmodium falciparum infects erythrocytes, proteins associated with host-derived detergent-resistant membrane (DRM) rafts are selectively recruited into the newly formed vacuole, but parasite proteins that contribute to raft-based vacuole development are unknown. In mammalian cells, DRM-associated integral membrane proteins such as caveolin-1 and flotillin-1 that form oligomers have been linked to the formation of DRM-based invaginations called caveolae. Here we show that the P. falciparum genome does not encode caveolins or flotillins but does contain an orthologue of human band 7 stomatin, a protein known to oligomerize, associate with non-caveolar DRMs and is distantly related to flotillins. Stomatins are members of a large protein family conserved in evolution and P. falciparum (Pf) stomatin appears to be a prokaryotic-like molecule. Evidence is presented that it associates with DRMs and may oligomerize, suggesting that these features are conserved in the stomatin family. Further, Pfstomatin is an integral membrane protein concentrated at the apical end of extracellular parasites, where it co-localizes with invasion-associated rhoptry organelles. A resident rhoptry protein, RhopH2 also resides in DRMs. This provides the first evidence that rhoptries of an apicomplexan parasite contain DRM rafts. Further, when the parasite invades erythrocytes, rhoptry Pfstomatin and RhopH2 are inserted into the newly formed vacuole. Thus, like caveolin-1 and flotillin-1, a stomatin may also associate with non-clathrin coated, DRM-enriched vacuoles. We propose a new model of invasion and vacuole formation involving DRM-based interactions of both host and parasite molecules. Plasmodium falciparum is an apicomplexan parasite that causes the most virulent form of human malaria. During the blood stages of infection, it invades mature human erythrocytes and develops within a parasitophorous vacuolar membrane (PVM). 1The abbreviations used are: PVMparasite vacuolar membraneDRMdetergent-resistant membraneSLP-2stomatin-like protein 2GFPgreen fluorescent proteinDOPCdioleyl l-α-phosphatidylcholinePPMparasite plasma membraneMSP-1merozoite surface protein 1Mes4-morpholineethanesulfonic acidPBSphosphate-buffered saline. These host cells are enucleated, have no intracellular organelles and under steady-state conditions have no dedicated machinery for endocytosis of their plasma membrane (1Schrier S.L. Methods Enzymol. 1987; 149: 260-270Crossref PubMed Scopus (9) Google Scholar). Yet electron microscopy studies suggest that the nascent vacuole induced by Plasmodium is formed by an invagination of the erythrocyte membrane (2Bannister L.H. Mitchell G.H. J. Protozool. 1989; 36: 362-367Crossref PubMed Scopus (72) Google Scholar). Although major erythrocyte proteins are excluded from the PVM, proteins that reside in buoyant cholesterol-rich detergent-resistant membrane (DRM) rafts concentrate in the vacuole (3Nagao E. Seydel K.B. Dvorak J.A. Exp. Parasitol. 2002; 102: 57-59Crossref PubMed Scopus (35) Google Scholar, 4Lauer S. VanWye J. Harrison T. McManus H. Samuel B.U. Hiller N.L. Mohandas N. Haldar K. EMBO J. 2000; 19: 3556-3564Crossref PubMed Scopus (195) Google Scholar). In addition, mild depletion of erythrocyte cholesterol that has no significant effect on major erythrocyte membrane function but disrupts DRM rafts, blocks malarial infection (5Samuel B.U. Mohandas N. Harrison T. McManus H. Rosse W. Reid M. Haldar K. J. Biol. Chem. 2001; 276: 29319-29329Abstract Full Text Full Text PDF PubMed Scopus (160) Google Scholar). Emerging evidence suggests that DRM rafts play a role in membrane curvature (6Smart E.J. Graf G.A. McNiven M.A. Sessa W.C. Engelman J.A. Scherer P.E. Okamoto T. Lisanti M.P. Mol. Cell. Biol. 1999; 19: 7289-7304Crossref PubMed Scopus (926) Google Scholar, 7Huttner W.B. Zimmerberg J. Curr. Opin. Cell Biol. 2001; 13: 478-484Crossref PubMed Scopus (199) Google Scholar, 8Anderson R.G. Jacobson K. Science. 2002; 296: 1821-1825Crossref PubMed Scopus (1012) Google Scholar). Together these studies imply that PVM formation may involve recruitment of erythrocyte DRM components induced by P. falciparum (9Haldar K. Mohandas N. Samuel B.U. Harrison T. Hiller N.L. Akompong T. Cheresh P. Cell Microbiol. 2002; 4: 383-395Crossref PubMed Scopus (66) Google Scholar). However, parasite molecules and mechanisms contributing to raft-based vacuole biogenesis remain unknown. parasite vacuolar membrane detergent-resistant membrane stomatin-like protein 2 green fluorescent protein dioleyl l-α-phosphatidylcholine parasite plasma membrane merozoite surface protein 1 4-morpholineethanesulfonic acid phosphate-buffered saline. Malarial infection of the erythrocyte is initiated by the extracellular merozoite stage. As the merozoite enters, it appears to release content from apical secretory organelles into the junction of invasion: specifically, contents of organelles called rhoptries are thought to be delivered to the newly forming vacuole. This is seen in both Plasmodium as well as the related apicomplexan parasite Toxoplasma gondii (reviewed in Refs. 10Berzins K. Chem Immunol. 2002; 80: 125-143Crossref PubMed Scopus (19) Google Scholar and 11Blackman M.J. Bannister L.H. Mol. Biochem. Parasitol. 2001; 117: 11-25Crossref PubMed Scopus (123) Google Scholar). In P. falciparum, studies have suggested that the vacuolar membrane is derived mostly from lipids of the apical organelles (12Dluzewski A.R. Mitchell G.H. Fryer P.R. Griffiths S. Wilson R.J. Gratzer W.B. J. Cell Sci. 1992; 102: 527-532PubMed Google Scholar, 13Dluzewski A.R. Zicha D. Dunn G.A. Gratzer W.B. Eur J. Cell Biol. 1995; 68: 446-449PubMed Google Scholar). In T. gondii the current model suggests that the newly formed PVM is extensively modified by fusion of rhoptry-derived secretory vesicles (14Hakansson S. Charron A.J. Sibley L.D. EMBO J. 2001; 20: 3132-3144Crossref PubMed Scopus (242) Google Scholar). Thus, the contents of the rhoptries are thought to play a critical role in formation of the PVM, but evidence that rhoptry proteins into the new vacuolar and into their membrane have been Further, of apical proteins that contribute to are in T. gondii (reviewed in 11Blackman M.J. Bannister L.H. Mol. Biochem. Parasitol. 2001; 117: 11-25Crossref PubMed Scopus (123) Google to be related to known proteins in or Thus, host it has been to into the membrane of apicomplexan apical of the rhoptries that may contribute to vacuole raft-based plasma membrane invaginations in mammalian cells are (reviewed in R.G. Biochem. PubMed Scopus Google Scholar). These are in a of and have been to be of DRM rafts (reviewed in R.G. Biochem. PubMed Scopus Google Scholar). A resident DRM protein of is is associated with the of W.C. R.G. Cell. 1992; 68: Full Text PDF PubMed Scopus Google Scholar, D. Sci. S. 1992; PubMed Scopus Google Scholar, P. R.G. K. EMBO J. PubMed Scopus Google and appears to play a role in J. R.G. Sci. S. 2002; PubMed Scopus Google Scholar). of protein is to in cells E. K. R.G. Sci. S. 1995; PubMed Scopus Google Scholar, S. Lisanti M.P. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google to to both associate with DRM rafts and M. M. Lisanti M.P. J. Cell Biol. PubMed Scopus Google Scholar, S. R.G. J. Mol. Biol. Cell. 1995; PubMed Scopus Google Scholar, M. Scherer P.E. E. Lisanti M.P. Sci. S. 1995; PubMed Scopus Google a to raft-based protein flotillin-1, is DRM-associated and oligomers has also been to formation in cells that not caveolin-1 D. S. K. Okamoto T. Lisanti M.P. J. Biol. Chem. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). 7 stomatin is a of flotillin-1 N. M. Biochem. Sci. 1999; Full Text Full Text PDF PubMed Scopus Google large oligomers E. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google but is a of non-caveolar DRM rafts (5Samuel B.U. Mohandas N. Harrison T. McManus H. Rosse W. Reid M. Haldar K. J. Biol. Chem. 2001; 276: 29319-29329Abstract Full Text Full Text PDF PubMed Scopus (160) Google Scholar, 2001; PubMed Scopus Google Scholar). flotillin-1 is also in non-caveolar DRM rafts, P.E. Scherer P.E. P. Lisanti M.P. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). that band 7 stomatin is a of a large protein family of both and proteins N. M. Biochem. Sci. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). the stomatin of the of erythrocyte band 7 protein with a by to in blood cells J. Biol. Chem. 1995; Full Text Full Text PDF PubMed Scopus Google Scholar). However, stomatin is not linked to T. S. P. P. M. Mohandas N. W. 1999; PubMed Google Scholar). Further, stomatin have been and linked to the of in the function of is M. E. M. 1995; PubMed Scopus Google Scholar, S. J. PubMed Scopus Google Scholar, S. Sci. S. PubMed Scopus Google Scholar, S. 1999; PubMed Google Scholar, J. Cell 2001; PubMed Google Scholar, M. 2002; PubMed Scopus Google Scholar). evidence suggests that band 7 stomatin may membrane in DRM rafts (reviewed in R.G. Curr. Opin. Cell Biol. 1999; PubMed Scopus Google but DRM is a conserved of the stomatin family and reside at the of to rafts unknown. Here we show that the P. falciparum genome an orthologue of band 7 stomatin but not of caveolins or flotillins. Pfstomatin is most to stomatin-like J. Biol. Chem. 2000; Full Text Full Text PDF PubMed Scopus Google a prokaryotic-like orthologue of band 7 stomatin that is also in mammalian Pfstomatin and like stomatin, associate with DRM rafts. In the extracellular merozoite Pfstomatin co-localizes with with DRM protein it is delivered to the of the PVM induced by the of these we propose a new model of PVM biogenesis where of DRM proteins from parasite rhoptries as well as DRM-associated host erythrocyte proteins vacuolar development in the and of P. P. falciparum as W. Science. PubMed Scopus Google Scholar, K. M.A. G.A. J. Biol. Chem. Full Text PDF PubMed Google Scholar). When parasite to within a by a and K. Methods Cell Biol. PubMed Scopus Google Scholar). of and and used in a to the of Pfstomatin from a from and initiated with of 1 at 1 at and 1 at to for of by of 1 at 1 at and 1 at by and into and and the protein Pfstomatin as a used to of of or protein by the with the and used as a in and used in of the by used to the for and of a of a Pfstomatin the and into a protein that an and a and and into the protein the cells in to the to a of 1 and cells for at the to the cells in and to to a with at and Pfstomatin from the at used to the protein of of a used to protein of on the of the protein to an the of the acid protein, as by protein at the of is with a in suggesting the of an of of protein to Pfstomatin band in Pfstomatin a of the protein to a in the and of with a with the and the protein with a and of of Pfstomatin of the and protein, and at with of protein with the by of into and a protein in with of and by of 1 used at a of in and at a of in by a of by S. VanWye J. Harrison T. McManus H. Samuel B.U. Hiller N.L. Mohandas N. Haldar K. EMBO J. 2000; 19: 3556-3564Crossref PubMed Scopus (195) Google Scholar). cells in and at 1 and to to with in for at in the cells in or in for with in or in and with in with the to and in surface protein 1 by and by J. In studies cells with for cells with used P. Harrison T. H. Haldar K. J. Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus (35) Google Scholar). cells, parasite by with of for and as P. Harrison T. H. Haldar K. J. Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus (35) Google with an fluorescent and a by of DRM rafts as S. VanWye J. Harrison T. McManus H. Samuel B.U. Hiller N.L. Mohandas N. Haldar K. EMBO J. 2000; 19: 3556-3564Crossref PubMed Scopus (195) Google Scholar, B.U. Mohandas N. Harrison T. McManus H. Rosse W. Reid M. Haldar K. J. Biol. Chem. 2001; 276: 29319-29329Abstract Full Text Full Text PDF PubMed Scopus (160) Google Scholar). vacuolar from the membrane or erythrocytes on in 2 of in for in the of a of and as well as and 1 This with an of and with of in and 2 of in to at in a the 1 to as and 2 to as used to protein where proteins concentrated and of protein to under the Haldar K. EMBO J. PubMed Scopus Google J. Biol. Chem. 2000; Full Text Full Text PDF PubMed Scopus Google T. S. M. Mol. Biochem. Parasitol. PubMed Scopus Google and used to the and of at M. K. Akompong T. Haldar K. 2000; 68: PubMed Scopus Google in and in for to release from the host erythrocyte by in and in of in the of at These with or such that at a of or or in membrane proteins not from the membrane a in membrane proteins are from the membrane a in but not a in These to at for 1 to the membrane and in to and in with and fluorescent protein by of Pfstomatin into with l-α-phosphatidylcholine or of and cholesterol in and in the lipids in M. J. K. Sci. S. 1995; PubMed Scopus Google Scholar). This in a for at and to a of 2 of in 2 and the to at for with Pfstomatin at into and A of of protein to the This with an of and with of in of in and 2 of in to at for to and for a and and of the Cell is a that be used to selectively plasma M.J. J. K. J. Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar). cells on as with of of for at cells with as well as of in for at in for in for at and with the for at As a for PVM cells also with to for 2 in in for and in for in for in in for at and with of the with and to of a in the P. falciparum of the P. falciparum genome J. M.J. D. P. A.J. J. 2002; PubMed Scopus Google human band 7 stomatin as a malarial orthologue Pfstomatin the stomatin J. Biol. Chem. 2000; Full Text Full Text PDF PubMed Scopus Google that is conserved in evolution by a green in and is as of the family with a of in that Pfstomatin is a of the stomatin family. is distantly related to and these proteins are members of the members stomatin, and N. M. Biochem. Sci. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). of or and However, and are in the P. falciparum band 7 stomatin may associate with a that the but does not both and are at the of the membrane PubMed Scopus Google Scholar). of the protein inserted into the membrane in band 7 stomatin is by a in This integral membrane is conserved the of human band 7 stomatin, such as stomatin and J. Biochem. Cell Biol. PubMed Scopus Google but is in J. Biol. Chem. 2000; Full Text Full Text PDF PubMed Scopus Google Scholar). However, Pfstomatin is by to have an integral membrane in a band 7 stomatin, but in the as orthologue in Thus, in Pfstomatin also form a that the Pfstomatin does contain an and in is Pfstomatin a of and of the the acid of human band 7 stomatin, and in and suggested that Pfstomatin is related to and proteins human band 7 stomatin does have a with mammalian with the of these in that the where Pfstomatin from the stomatin are to used in the with in A the of that and are A Pfstomatin the with These are in of members of and and and of the stomatin family is of a stomatin in P. falciparum suggests an function for protein in of of Pfstomatin in and Evidence for of contain of an and of the protein as by and on the by protein and to with in by This to from an is not of proteins the content of the in acid Mol. Biochem. Parasitol. PubMed Scopus Google Scholar). As the of Pfstomatin in used for and band 7 are of we the that to Pfstomatin with these We for of with cells not of not with or band We the of the to the of the parasite resident in we in a that Pfstomatin but not or band the to the and a band in from but not erythrocytes This as of Pfstomatin is and the human band 7 stomatin human not with or cells not These suggest that the Pfstomatin in the also of a protein and proteins in These may of Pfstomatin also form in may be in the of to the formation of oligomers of that are in erythrocytes J. Biol. Chem. 2000; Full Text Full Text PDF PubMed Scopus Google Scholar). intracellular parasite develops and stages and parasite proteins show We the steady-state of Pfstomatin at stages of As in a for of erythrocytes, of Pfstomatin at and This suggests that the and stages contain of protein these stages used in of Pfstomatin and in DRM has been that human band 7 stomatin is in DRM rafts (5Samuel B.U. Mohandas N. Harrison T. McManus H. Rosse W. Reid M. Haldar K. J. Biol. Chem. 2001; 276: 29319-29329Abstract Full Text Full Text PDF PubMed Scopus (160) Google Scholar, 2001; PubMed Scopus Google Scholar). is not conserved in Pfstomatin or the a and is associated with J. Biol. Chem. 2000; Full Text Full Text PDF PubMed Scopus Google Scholar). Further, of the of DRM rafts are not to be a of However, we to prokaryotic-like such as Pfstomatin and that are in cells associate with DRM rafts, to into the of of in the stomatin family. In to DRM rafts from erythrocytes, membrane from erythrocytes with in at to a and associated with DRM rafts in 2 in and associated proteins in the and As in Pfstomatin in 2 well as in and In a parasite protein in the that membrane associated but proteins not on in from erythrocytes as for DRM rafts in not These suggest that Pfstomatin and are and their membrane are from of band into DRM rafts. of band 7 stomatin and have an integral membrane PubMed Scopus (72) Google Scholar). However, is not a by as by the of J. Biol. Chem. 2000; Full Text Full Text PDF PubMed Scopus Google also in In for Pfstomatin the an integral membrane with a of are the is with a in Thus, to the of membrane with or from green fluorescent protein provides a of membrane and for Pfstomatin and content by and that of the Pfstomatin associated with the membrane as for an integral membrane In of the in the that the cells the these suggest that Pfstomatin is an integral membrane protein in 7 stomatin is in to caveolin-1 R.G. Curr. Opin. Cell Biol. 1999; PubMed Scopus Google a form of into vesicles in a M. J. K. Sci. S. 1995; PubMed Scopus Google is thought to an of DRM in However, the of with membrane also cholesterol unknown. in has been the in band 7 we to a of Pfstomatin as protein, we membrane of we the of Pfstomatin with l-α-phosphatidylcholine in the and of cholesterol of the is by a the in to in to the at the of the protein in the in the As in of the protein to be at the of the in the 2 and when cholesterol Pfstomatin also to a of These suggest that the of Pfstomatin associate with This is not but not on suggesting that in DRM rafts may be by features of of Pfstomatin to in and of the RhopH2 in DRM of the of and Pfstomatin suggested that these may function as However, resides at the erythrocyte plasma membrane J. Biol. Chem. 2000; Full Text Full Text PDF PubMed Scopus Google suggesting that for the may not the of Pfstomatin to cells with and in in and Pfstomatin in no the and green that Pfstomatin does not to the In to the P. falciparum a called the J. N. PubMed Scopus Google Scholar). In a related apicomplexan parasite T. are the and M. J. Cell Sci. 2000; Google Scholar, R.G. E. N. Sci. S. PubMed Scopus Google Scholar). However, as in in erythrocytes Pfstomatin to with the to the These suggest that Pfstomatin does not reside in the or the it a at the apical end of the suggesting an Further, is a of Pfstomatin and the resident rhoptry protein RhopH2 in in as well as in the extracellular Thus, it appears that Pfstomatin is at the apical end of the in the is evidence of host DRM rafts in the PVM of P. erythrocytes S. VanWye J. Harrison T. McManus H. Samuel B.U. Hiller N.L. Mohandas N. Haldar K. EMBO J. 2000; 19: 3556-3564Crossref PubMed Scopus (195) Google Pfstomatin is the first DRM protein in parasite apical organelles. RhopH2 co-localizes with we RhopH2 also associates with DRM rafts. As in RhopH2 in buoyant DRM from These that rhoptries contain DRM rafts. the parasite plasma membrane is also in DRM rafts This with that is in DRM on the merozoite surface M. S. D. J. Biochem. PubMed Scopus Google Scholar). In Pfstomatin and RhopH2 into the PVM and on components of merozoite apical organelles are to the parasitophorous vacuole of or invasion (reviewed in 10Berzins K. Chem Immunol. 2002; 80: 125-143Crossref PubMed Scopus (19) Google Scholar). Further, release of apical contents is thought to be in the of the nascent vacuole. Pfstomatin a we an where with to Pfstomatin and the As is of both in with of Pfstomatin to the of As T. S. M. Mol. Biochem. Parasitol. PubMed Scopus Google RhopH2 also to the of newly formed Although rhoptry proteins are into the nascent vacuole (reviewed in 10Berzins K. Chem Immunol. 2002; 80: 125-143Crossref PubMed Scopus (19) Google are inserted into the vacuolar to membrane has not been We in the of RhopH2 Pfstomatin in their to the of the vacuole, to evidence that these proteins are inserted into the we a to selectively the erythrocyte membrane the This by erythrocytes with the M.J. J. K. J. Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus Google to these cells may proteins on the of the PVM but not in the of the vacuole or in the parasite plasma membrane In in the of both the PVM and As in and in cells, to Pfstomatin and RhopH2 a of the protein associated with the vacuolar to a major of the M.J. S. J. Exp. PubMed Scopus Google to their In when the PVM is with cells be for and RhopH2 and These show that parasite DRM proteins from the rhoptries into the vacuolar and proteins like Pfstomatin and RhopH2 are on the of the both Pfstomatin and RhopH2 to with large protein and J.A. D. A.J. Mol. Biochem. Parasitol. PubMed Scopus Google Scholar, their suggests that may the of for protein in DRM rafts in the PVM model in Although mammalian cells studies that the P. falciparum a stomatin Pfstomatin is but it has a orthologue in in mammalian large the human band 7 stomatin and suggests that are into at and that have proteins from These in to the of Pfstomatin to the apical suggest that the of a prokaryotic-like stomatin in P. falciparum is not a of the that the or the but of the flotillin-1 and band 7 stomatin in a where the is thought to function as a that the protein in the of the to the extracellular R.G. Curr. Opin. Cell Biol. 1999; PubMed Scopus Google Scholar). studies have suggested that of the of band 7 stomatin in or of membrane E. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). In we that the of Pfstomatin to with to of that with the This a of with it is that the of may membrane the of Pfstomatin may integral membrane with the also suggest that the of Pfstomatin by the of human may with in a is known to be associated with erythrocyte plasma the of in DRM rafts is not on an membrane or integral membrane proteins within the Together the suggest that may be mechanisms to membrane and DRM of in a of Pfstomatin to the apical organelles of P. This is these are in the infection of host cells by as well as by the related apicomplexan Toxoplasma gondii orthologue of Pfstomatin be in the T. gondii of an apical Pfstomatin the newly formed vacuolar membrane that protein may a model in to that of caveolin-1 and flotillin-1 that the formation of model in caveolin-1 and flotillin-1 are thought to by their to associate with DRM rafts and oligomerize, with it has been that DRM of proteins and to form in may play an role in to rafts R.G. Jacobson K. Science. 2002; 296: 1821-1825Crossref PubMed Scopus (1012) Google Scholar). show that Pfstomatin is in DRMs and may have to In addition, Pfstomatin may and studies have that RhopH2 resides in a J.A. D. A.J. Mol. Biochem. Parasitol. PubMed Scopus Google with parasite Thus, RhopH2 and rhoptry DRM proteins may of in vacuole In the invasion of apicomplexan parasites, resident proteins of the are to the parasite surface and or of to the host plasma membrane (reviewed in 11Blackman M.J. Bannister L.H. Mol. Biochem. Parasitol. 2001; 117: 11-25Crossref PubMed Scopus (123) Google Scholar). from the rhoptries may be M.A. 102: PubMed Scopus Google into the vacuole is to the vacuole, but the membrane of the and the of parasite protein into the PVM are not well In studies of P. falciparum, (12Dluzewski A.R. Mitchell G.H. Fryer P.R. Griffiths S. Wilson R.J. Gratzer W.B. J. Cell Sci. 1992; 102: 527-532PubMed Google Scholar, 13Dluzewski A.R. Zicha D. Dunn G.A. Gratzer W.B. Eur J. Cell Biol. 1995; 68: 446-449PubMed Google have that the membrane of the newly formed vacuole is derived mostly from apical organelles. In L.H. Dvorak J.A. J. Cell Sci. Google suggest that it from the erythrocyte We show that integral DRM Pfstomatin and RhopH2 are the parasitophorous vacuole and on has that erythrocyte DRM proteins are recruited into the cholesterol-rich vacuole at the of parasite and that of erythrocyte DRM rafts blocks infection S. VanWye J. Harrison T. McManus H. Samuel B.U. Hiller N.L. Mohandas N. Haldar K. EMBO J. 2000; 19: 3556-3564Crossref PubMed Scopus (195) Google Scholar). Thus, we propose that the of the vacuole may be linked to DRM raft-based interactions of both host and parasite molecules in and may be to apicomplexan vacuoles. We and Samuel for their and for and and for of the
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