Lipid raft-a gateway for passing through the cell membrane for pathogens

Transcription

1 Chinese Bulletin of Life Sciences Vol. 16, No. 3 Jun., (2004) / GPI (GPI) Q241 Q257 R37 A Lipid rafta gateway for passing through the cell membrane for pathogens ZHOU YiRan, SONG JianGuo (Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai , China) Abstract: Lipid rafts are membrane structure enriched in cholesterol and sphingolipids, and form liquid ordered domains of decreased membrane fluidity. Lipid rafts play important roles in many biological processes including transmembrane signal transduction, endocytosis, lipid and protein sorting, and so on. Two principal proteins modifications are found in lipid rafts: one is covalent binding to glycosylphosphatidylinositol (GPI), the other is myristoylization. A series of GPIanchored proteins are identified as receptors of many different pathogen organisms. Increasing amount of reports demonstrate that many pathogens (bacteria, parasites, and viruses) and toxins preferentially utilize rafts for interacting with their target cells, entry, replication and infection. Also, the lipid raft domains provide sites for assembly and budding of certain viruses. The progress in understanding the roles of lipid rafts in pathogen infections may facilitate the development of new strategies for antiinfections. rafts) [1] (microdomain) (lipid (1976 ) (1956 )

2 145 / 50~70 nm [2] 1 [5~6] Triton X100 (caveolae) [3] (caveolin) [7] DRMs (detergentresistant membranes) Simons Ikonen [4] (PI) (PS) (PE) [8~10] (liquidordered phase, lo) (liquidcrystalline phase, lc) lc lo GPI GPI (GPI) 2

3 146 ) (2) 3, FimH Malaviya [11] (Vibrio cholerae) (cholera toxin, CT) B CTB G [12] FimH 4 CT ER ER A CT CTB [16~17] Caveolin β Peyron [15] Myco. bovis Myco. kansasii [13] Gatfield [14] DNA MHCI MHCI [18] ER (1) ( GPI GPI GPI C DNA ER [19] Myco. kansasii Myco. bovis 2

4 147 [20] 5 HA) A (hemagglutinin, (neuraminidase, NA) M1 HA NA DRMs [21] Scheiffele [22] HA Gag H9 1 / [23] Triton X100 Gag DRMs Thy1 CD59 CD45 [24] 1 6 [1] Kurzchalia T V, Parton R G. Membrane microdomains and caveolae. Curr Opin Cell Biol, 1999, 11(4): 424~431 [2] van der Goot F G, Harder T. Raft membrane domains: from a liquidordered membrane phase to a site of pathogen attack. Semin Immunol, 2001, 13(2): 89~97 [3] Melkonian K A, Chu T, Tortorella L B, et al. Characterization of proteins in detergentresistant membrane complexes from MadinDarby canine kidney epithelial cells. Biochemistry, 1995, 34(49): 16161~16170 [4] Simons K, Ikonen E. Functional rafts in cell membranes. Nature, 1997, 387: 569~572 [5] Brown D. Structure and function of membrane rafts. Int J Med Microbiol, 2002, 291(67): 433~437 [6] Brown D A, London E. Structure and function of sphingolipid and cholesterolrich membrane rafts. J Biol Chem, 2000, 275(23): 17221~ [7] Anderson R G. The caveolae membrane system. Annu Rev Biochem, 1998, 67: 199~225 [8] Fielding C J. Caveolae and signaling. Curr Opin Lipidol, 2001, 12(3): 281~287 [9] Nichols B J, LippincottSchwartz J. Endocytosis without

5 148 clathrin coats. Trends Cell Biol, 2001, 11(10): 406~412 [10] Fielding C J, Fielding P E. Caveolae and intracellular trafficking of cholesterol. Adv Drug Deliv Rev, 2001, 49: 251~264 [11] Malaviya R, Gao Z M, Thankavel K, et al. The mast cell tumor necrosis factor α response to FimHexpressing Escherichia coli is mediated by the glycosylphosphatidylinositolanchored molecule. Proc Natl Acad Sci USA, 1999, 96(14): 8110~8115 [12] Baorto D M, Gao Z M, Malaviya R, et al. Survival of FimHexpressing enterobacteria in macrophages relies on glycolipid traffic. Nature, 1997, 389: 636~639 [13] Shin J S, Gao Z M, Abraham S N. Involvement of cellular caveolae in bacterial entry into mast cells. Science. 2000, 289: 785~788 [14] Gatfield J, Pieters J. Essential role for cholesterol in entry of mycobacteria into macrophages. Science, 2000, 288: 1647~1650 [15] Peyron P, Bordier C, N'Diaye E N, et al. Nonopsonic phagocytosis of Mycobacterium kansasii by human neutrophils depends on cholesterol and is mediated by CR3 associated with glycosylphosphatidylinositolanchored proteins. J Immunol, 2000, 165(9): 5186~5191 [16] Wolf A A, Jobling M G, WimerMackin S, et al. Ganglioside structure dictates signal transduction by cholera toxin and association with caveolaelike membrane domains in polarized epithelia. J Cell Biol, 1998, 141: 917~927 [17] Lencer W I, Moe S, Rufo P A, et al. Transcytosis of cholera toxin subunits across model human intestinal epithelia. Proc Natl Acad Sci USA, 1995, 92: 10094~10098 [18] Parton R G, Lindsay M. Exploitation of major histocompatibility complex class I molecules and caveolae by simian virus 40. Immunol Rev, 1999, 168: 23~31 [19] Pelkmans L, Kartenbeck J, Helenius A. Caveolae endocytosis of simian virus 40 reveals a new twostep vesiculartransport pathway to the ER. Nat Cell Biol, 2001, 3: 473~483 [20] Pelkmans L, Püntener D, Helenius A. Local actin polymerization and dynamin recruitment in induced internalization of caveolae. Science, 2002, 296: 535~539 [21] Zhang J, Pekosz A, Lamb R A. Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tail of the spike glycoproteins. J Virol, 2000, 74: 4634~4644 [22] Scheiffele P, Rietveld A, Wilk T, et al. Influenza viruses select ordered lipid domains during budding from the plasma membrane. J Biol Chem, 1999, 274: 2038~2044 [23] Aloia R C, Tian H R, Jensen F C. Lipid composition and? uidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc Natl Acad Sci USA, 1993, 90: 5181~5185 [24] Rousso I, Mixon M B, Chen B K, et al. Palmitoylation of the 1 envelope glycoprotein is critical for viral infectivity. Proc Natl Acad Sci USA, 2000, 97: 13523~13525