메뉴 건너뛰기




Volumn 45, Issue 11, 2008, Pages 3036-3044

High-density rafts preferentially host the complement activator measles virus F glycoprotein but not the regulators of complement activation

Author keywords

Alternative pathway; CD46; CD55; Complement; Measles virus F protein; Membrane rafts

Indexed keywords

CHOLESTEROL; DECAY ACCELERATING FACTOR; GLYCOPROTEIN F; HYBRID PROTEIN; MEMBRANE COFACTOR PROTEIN; VIRUS PROTEIN;

EID: 43649086590     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2008.03.013     Document Type: Article
Times cited : (7)

References (53)
  • 1
    • 0029151519 scopus 로고
    • Differential solubilization of lipids along with membrane proteins by different classes of detergents
    • P. Banerjee J.B. Joo J.T. Buse G. Dawson Differential solubilization of lipids along with membrane proteins by different classes of detergents Chem. Phys. Lipids 77 1995 65 78
    • (1995) Chem. Phys. Lipids , vol.77 , pp. 65-78
    • Banerjee, P.1    Joo, J.B.2    Buse, J.T.3    Dawson, G.4
  • 2
    • 0035213883 scopus 로고    scopus 로고
    • The measles virus glycoproteins interact with cellular chaperones in the endoplasmic reticulum and MV infection upregulates chaperones expression
    • G. Bolt The measles virus glycoproteins interact with cellular chaperones in the endoplasmic reticulum and MV infection upregulates chaperones expression Arch. Virol. 146 2001 2055 2068
    • (2001) Arch. Virol. , vol.146 , pp. 2055-2068
    • Bolt, G.1
  • 3
    • 0034852440 scopus 로고    scopus 로고
    • The relationship between luminal and limiting membranes in swollen late endocytic compartments formed after wortmannin treatment or sucrose accumulation
    • N.A. Bright M.R. Lindsay A. Stewart J.P. Luzio The relationship between luminal and limiting membranes in swollen late endocytic compartments formed after wortmannin treatment or sucrose accumulation Traffic 2 2001 631 642
    • (2001) Traffic , vol.2 , pp. 631-642
    • Bright, N.A.1    Lindsay, M.R.2    Stewart, A.3    Luzio, J.P.4
  • 4
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone HSP70 in detergent-resistant microdomains correlates with its membrane delivery and release
    • A.H. Broquet G. Thomas J. Mashliah G. Trugnan M. Bachelet Expression of the molecular chaperone HSP70 in detergent-resistant microdomains correlates with its membrane delivery and release J. Biol. Chem. 278 2003 21601 21606
    • (2003) J. Biol. Chem. , vol.278 , pp. 21601-21606
    • Broquet, A.H.1    Thomas, G.2    Mashliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 5
    • 33845309656 scopus 로고    scopus 로고
    • Lipid rafts, detergent-resistant membranes, and raft targeting signals
    • D.A. Brown Lipid rafts, detergent-resistant membranes, and raft targeting signals Physiology (Bethesda) 21 2006 430 439
    • (2006) Physiology (Bethesda) , vol.21 , pp. 430-439
    • Brown, D.A.1
  • 6
    • 0031714558 scopus 로고    scopus 로고
    • Measles virus fusion protein is palmitoylated on transmembrane-intracytoplasmic cysteine residues which participate in cell fusion
    • M. Caballero J. Carabana J. Ortego R. Fernandez-Munoz M.L. Celma Measles virus fusion protein is palmitoylated on transmembrane-intracytoplasmic cysteine residues which participate in cell fusion J. Virol. 72 1998 8198 8204
    • (1998) J. Virol. , vol.72 , pp. 8198-8204
    • Caballero, M.1    Carabana, J.2    Ortego, J.3    Fernandez-Munoz, R.4    Celma, M.L.5
  • 7
    • 0031907095 scopus 로고    scopus 로고
    • Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence
    • T. Cathomen H.Y. Naim R. Cattaneo Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence J. Virol. 72 1998 1224 1234
    • (1998) J. Virol. , vol.72 , pp. 1224-1234
    • Cathomen, T.1    Naim, H.Y.2    Cattaneo, R.3
  • 8
    • 0037147217 scopus 로고    scopus 로고
    • The vesicle- and target-SNARE proteins that mediate Glut4 vesicle fusion are localized in detergent-insoluble lipid rafts present on distinct intracellular membranes
    • L.H. Chamberlain G.W. Gould The vesicle- and target-SNARE proteins that mediate Glut4 vesicle fusion are localized in detergent-insoluble lipid rafts present on distinct intracellular membranes J. Biol. Chem. 277 2002 49750 49754
    • (2002) J. Biol. Chem. , vol.277 , pp. 49750-49754
    • Chamberlain, L.H.1    Gould, G.W.2
  • 9
    • 0038314400 scopus 로고    scopus 로고
    • Virus entry, assembly, budding, and membrane rafts
    • N. Chazal D. Gerlier Virus entry, assembly, budding, and membrane rafts Microbiol. Mol. Biol. Rev. 67 2003 226 237
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 226-237
    • Chazal, N.1    Gerlier, D.2
  • 10
    • 0035077947 scopus 로고    scopus 로고
    • Chimeric CD46/DAF molecules reveal a cryptic functional role for SCR1 of DAF in regulating complement activation
    • D. Christiansen B. Loveland P. Kyriakou M. Lanteri E. Rubinstein D. Gerlier Chimeric CD46/DAF molecules reveal a cryptic functional role for SCR1 of DAF in regulating complement activation Mol. Immunol. 37 2000 687 696
    • (2000) Mol. Immunol. , vol.37 , pp. 687-696
    • Christiansen, D.1    Loveland, B.2    Kyriakou, P.3    Lanteri, M.4    Rubinstein, E.5    Gerlier, D.6
  • 11
    • 0033053789 scopus 로고    scopus 로고
    • Control of C3b and C5b deposition by CD46 (membrane cofactor protein) after alternative but not classical complement activation
    • P. Devaux D. Christiansen M. Fontaine D. Gerlier Control of C3b and C5b deposition by CD46 (membrane cofactor protein) after alternative but not classical complement activation Eur. J. Immunol. 29 1999 815 822
    • (1999) Eur. J. Immunol. , vol.29 , pp. 815-822
    • Devaux, P.1    Christiansen, D.2    Fontaine, M.3    Gerlier, D.4
  • 12
    • 2942644452 scopus 로고    scopus 로고
    • Cell surface activation of the alternative complement pathway by the fusion protein of measles virus
    • P. Devaux D. Christiansen S. Plumet D. Gerlier Cell surface activation of the alternative complement pathway by the fusion protein of measles virus J. Gen. Virol. 85 2004 1665 1673
    • (2004) J. Gen. Virol. , vol.85 , pp. 1665-1673
    • Devaux, P.1    Christiansen, D.2    Plumet, S.3    Gerlier, D.4
  • 13
    • 0025359652 scopus 로고
    • Monoclonal antibody A2B5, which detects cell surface antigens, binds to ganglioside GT3 (II3 (NeuAc)3LacCer) and to its 9-O-acetylated derivative
    • C. Dubois J.C. Manuguerra B. Hauttecoeur J. Maze Monoclonal antibody A2B5, which detects cell surface antigens, binds to ganglioside GT3 (II3 (NeuAc)3LacCer) and to its 9- O -acetylated derivative J. Biol. Chem. 265 1990 2797 2803
    • (1990) J. Biol. Chem. , vol.265 , pp. 2797-2803
    • Dubois, C.1    Manuguerra, J.C.2    Hauttecoeur, B.3    Maze, J.4
  • 15
    • 0030996747 scopus 로고    scopus 로고
    • Antibodies to a new linear site at the topographical or functional interface between the haemagglutinin and fusion proteins protect against measles encephalitis
    • P. Fournier N.H. Brons K.H. Berbers K.H. Wiesmuller B.T. Fleckenstein F. Schneider G. Jung C.P. Muller Antibodies to a new linear site at the topographical or functional interface between the haemagglutinin and fusion proteins protect against measles encephalitis J. Gen. Virol. 78 1997 1295 1302
    • (1997) J. Gen. Virol. , vol.78 , pp. 1295-1302
    • Fournier, P.1    Brons, N.H.2    Berbers, K.H.3    Wiesmuller, K.H.4    Fleckenstein, B.T.5    Schneider, F.6    Jung, G.7    Muller, C.P.8
  • 16
    • 0034635564 scopus 로고    scopus 로고
    • Retention of subunits of the oligosaccharyltransferase complex in the endoplasmic reticulum
    • J. Fu G. Kreibich Retention of subunits of the oligosaccharyltransferase complex in the endoplasmic reticulum J. Biol. Chem. 275 2000 3984 3990
    • (2000) J. Biol. Chem. , vol.275 , pp. 3984-3990
    • Fu, J.1    Kreibich, G.2
  • 17
    • 0035943423 scopus 로고    scopus 로고
    • Emerging themes in lipid rafts and caveolae
    • F. Galbiati B. Razani M.P. Lisanti Emerging themes in lipid rafts and caveolae Cell 106 2001 403 411
    • (2001) Cell , vol.106 , pp. 403-411
    • Galbiati, F.1    Razani, B.2    Lisanti, M.P.3
  • 18
    • 0021319361 scopus 로고
    • A study of measles virus antigens in acutely and persistently infected cells using monoclonal antibodies: differences in the accumulation of certain viral proteins
    • P. Giraudon C. Gerald T.F. Wild A study of measles virus antigens in acutely and persistently infected cells using monoclonal antibodies: differences in the accumulation of certain viral proteins Intervirology 21 1984 110 120
    • (1984) Intervirology , vol.21 , pp. 110-120
    • Giraudon, P.1    Gerald, C.2    Wild, T.F.3
  • 19
    • 0037470068 scopus 로고    scopus 로고
    • T cell receptor can be recruited to a subset of plasma membrane rafts, independently of cell signaling and attendantly to raft clustering
    • E. Giurisato D.P. McIntosh M. Tassi A. Gamberucci A. Benedetti T cell receptor can be recruited to a subset of plasma membrane rafts, independently of cell signaling and attendantly to raft clustering J. Biol. Chem. 278 2003 6771 6778
    • (2003) J. Biol. Chem. , vol.278 , pp. 6771-6778
    • Giurisato, E.1    McIntosh, D.P.2    Tassi, M.3    Gamberucci, A.4    Benedetti, A.5
  • 22
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • T. Harder K. Simons Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains Curr. Opin. Cell. Biol. 9 1997 534 542
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 23
    • 0028899494 scopus 로고
    • Influence of N-linked oligosaccharide chains on the processing, cell surface expression and function of the measles virus fusion protein
    • A. Hu T. Cathomen R. Cattaneo E. Norrby Influence of N-linked oligosaccharide chains on the processing, cell surface expression and function of the measles virus fusion protein J. Gen. Virol. 76 1995 705 710
    • (1995) J. Gen. Virol. , vol.76 , pp. 705-710
    • Hu, A.1    Cathomen, T.2    Cattaneo, R.3    Norrby, E.4
  • 25
    • 0017858332 scopus 로고
    • Proteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristic of rough microsomes
    • G. Kreibich B.L. Ultich D.D. Sabatini Proteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristic of rough microsomes J. Cell. Biol. 77 1978 464 487
    • (1978) J. Cell. Biol. , vol.77 , pp. 464-487
    • Kreibich, G.1    Ultich, B.L.2    Sabatini, D.D.3
  • 26
    • 0037388897 scopus 로고    scopus 로고
    • Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation
    • N. Li A. Mak D.P. Richards C. Naber B.O. Keller L. Li A.R.E. Shaw Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation Proteomics 3 2003 536 548
    • (2003) Proteomics , vol.3 , pp. 536-548
    • Li, N.1    Mak, A.2    Richards, D.P.3    Naber, C.4    Keller, B.O.5    Li, L.6    Shaw, A.R.E.7
  • 28
    • 0033573083 scopus 로고    scopus 로고
    • Functionally different GPI proteins are organized in different domains on the neuronal surface
    • N. Madore K.L. Smith C.H. Graham A. Jen K. Brady S. Hall R. Morris Functionally different GPI proteins are organized in different domains on the neuronal surface EMBO J. 18 1999 6917 6926
    • (1999) EMBO J. , vol.18 , pp. 6917-6926
    • Madore, N.1    Smith, K.L.2    Graham, C.H.3    Jen, A.4    Brady, K.5    Hall, S.6    Morris, R.7
  • 30
    • 0033987081 scopus 로고    scopus 로고
    • Measles virus structural components are enriched into lipid raft microdomains: a potential cellular location for virus assembly
    • S.N. Manié S. Debreyne S. Vincent D. Gerlier Measles virus structural components are enriched into lipid raft microdomains: a potential cellular location for virus assembly J. Virol. 74 2000 305 311
    • (2000) J. Virol. , vol.74 , pp. 305-311
    • Manié, S.N.1    Debreyne, S.2    Vincent, S.3    Gerlier, D.4
  • 31
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • K.A. Melkonian A.G. Ostermeyer J.Z. Chen M.G. Roth D.A. Brown Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated J. Biol. Chem. 274 1999 3910 3917
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 32
    • 38449083374 scopus 로고    scopus 로고
    • Lipid raft heterogeneity: an enigma
    • S. Mishra P.G. Joshi Lipid raft heterogeneity: an enigma J. Neurochem. 103 Suppl. 1 2007 135 142
    • (2007) J. Neurochem. , vol.103 , Issue.Suppl. 1 , pp. 135-142
    • Mishra, S.1    Joshi, P.G.2
  • 34
    • 0027177368 scopus 로고
    • Measles virus haemagglutinin induces down-regulation of gp57/67, a molecule involved in virus binding
    • D. Naniche T.F. Wild C. Rabourdin-Combe D. Gerlier Measles virus haemagglutinin induces down-regulation of gp57/67, a molecule involved in virus binding J. Gen. Virol. 74 1993 1073 1079
    • (1993) J. Gen. Virol. , vol.74 , pp. 1073-1079
    • Naniche, D.1    Wild, T.F.2    Rabourdin-Combe, C.3    Gerlier, D.4
  • 35
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membrane
    • T. Nebl K.N. Pestonjamas J.D. Leszyk J.L. Crowley S.W. Oh E.J. Luna Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membrane J. Biol. Chem. 277 2002 43399 43409
    • (2002) J. Biol. Chem. , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamas, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 36
    • 0029839350 scopus 로고    scopus 로고
    • The highly inducible member of the 70kDa family of heat shock proteins increases canine distemper virus polymerase activity
    • M.J. Oglesbee Z. Liu H. Kenney C.L. Brooks The highly inducible member of the 70 kDa family of heat shock proteins increases canine distemper virus polymerase activity J. Gen. Virol. 77 1996 2125 2135
    • (1996) J. Gen. Virol. , vol.77 , pp. 2125-2135
    • Oglesbee, M.J.1    Liu, Z.2    Kenney, H.3    Brooks, C.L.4
  • 37
    • 0034680917 scopus 로고    scopus 로고
    • Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum
    • Y. Okazaki H. Ohno K. Takase T. Ochiai T. Saito Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum J. Biol. Chem. 275 2000 35751 35758
    • (2000) J. Biol. Chem. , vol.275 , pp. 35751-35758
    • Okazaki, Y.1    Ohno, H.2    Takase, K.3    Ochiai, T.4    Saito, T.5
  • 38
    • 0032900090 scopus 로고    scopus 로고
    • Enhanced measles virus cDNA rescue and gene expression after heat shock
    • C.L. Parks R.A. Lerch P. Walpita M.S. Sidhu S.A. Udem Enhanced measles virus cDNA rescue and gene expression after heat shock J. Virol. 73 1999 3560 3566
    • (1999) J. Virol. , vol.73 , pp. 3560-3566
    • Parks, C.L.1    Lerch, R.A.2    Walpita, P.3    Sidhu, M.S.4    Udem, S.A.5
  • 39
    • 0021068591 scopus 로고
    • Oligopeptides that specifically inhibit membrane fusion by paramyxoviruses: studies on the site of action
    • C.D. Richardson P.W. Choppin Oligopeptides that specifically inhibit membrane fusion by paramyxoviruses: studies on the site of action Virology 131 1983 518 532
    • (1983) Virology , vol.131 , pp. 518-532
    • Richardson, C.D.1    Choppin, P.W.2
  • 40
    • 0026321291 scopus 로고
    • High level bacterial expression, purification and characterization of human calreticulin
    • L.A. Rokeach J.A. Haselby S.O. Hoch High level bacterial expression, purification and characterization of human calreticulin Prot. Eng. 4 1991 981 987
    • (1991) Prot. Eng. , vol.4 , pp. 981-987
    • Rokeach, L.A.1    Haselby, J.A.2    Hoch, S.O.3
  • 41
    • 0037478593 scopus 로고    scopus 로고
    • Caveolin-1 regulates the functional localization of N-acetylglucosaminetransferase III within the Golgi apparatus
    • K. Sasai Y. Ikeda H. Ihara K. Jhonke N. Tanigushi Caveolin-1 regulates the functional localization of N -acetylglucosaminetransferase III within the Golgi apparatus J. Biol. Chem. 278 2003 25295 25301
    • (2003) J. Biol. Chem. , vol.278 , pp. 25295-25301
    • Sasai, K.1    Ikeda, Y.2    Ihara, H.3    Jhonke, K.4    Tanigushi, N.5
  • 43
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • A. Shevchenko M. Wilm O. Vorm M. Mann Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels Anal. Chem. 68 1996 850 858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 45
    • 0018865734 scopus 로고
    • Antibody-independent activation of the alternative complement pathway by measles virus-infected cells
    • J.G.P. Sissons M.B.A. Oldstone R.D. Schreiber Antibody-independent activation of the alternative complement pathway by measles virus-infected cells Proc. Natl. Acad. Sci. U.S.A. 77 1980 559 562
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 559-562
    • Sissons, J.G.P.1    Oldstone, M.B.A.2    Schreiber, R.D.3
  • 47
    • 0031823614 scopus 로고    scopus 로고
    • The cellular stress response increases measles virus-induced cytopathic effect
    • D.Y. Vasconcelos E. Norrby M.J. Oglesbee The cellular stress response increases measles virus-induced cytopathic effect J. Gen. Virol. 79 1998 1769 1773
    • (1998) J. Gen. Virol. , vol.79 , pp. 1769-1773
    • Vasconcelos, D.Y.1    Norrby, E.2    Oglesbee, M.J.3
  • 48
    • 0031719703 scopus 로고    scopus 로고
    • Constitutive overexpression of the major inducible 70kDa heat shock protein mediates large plaque formation by measles virus
    • D.Y. Vasconcelos X.H. Cai M.J. Oglesbee Constitutive overexpression of the major inducible 70 kDa heat shock protein mediates large plaque formation by measles virus J. Gen. Virol. 79 1998 2239 2247
    • (1998) J. Gen. Virol. , vol.79 , pp. 2239-2247
    • Vasconcelos, D.Y.1    Cai, X.H.2    Oglesbee, M.J.3
  • 49
    • 0033779038 scopus 로고    scopus 로고
    • Measles virus assembly within membrane rafts
    • S. Vincent D. Gerlier S.N. Manié Measles virus assembly within membrane rafts J. Virol. 74 2000 9911 9915
    • (2000) J. Virol. , vol.74 , pp. 9911-9915
    • Vincent, S.1    Gerlier, D.2    Manié, S.N.3
  • 50
    • 0036100576 scopus 로고    scopus 로고
    • Restriction of measles virus RNA synthesis by a mouse host cell line: trans-complementation by polymerase components or a human cellular factor(s)
    • S. Vincent I. Tigaud H. Schneider C.J. Buchholz Y. Yanagi D. Gerlier Restriction of measles virus RNA synthesis by a mouse host cell line: trans-complementation by polymerase components or a human cellular factor(s) J. Virol. 76 2002 6121 6130
    • (2002) J. Virol. , vol.76 , pp. 6121-6130
    • Vincent, S.1    Tigaud, I.2    Schneider, H.3    Buchholz, C.J.4    Yanagi, Y.5    Gerlier, D.6
  • 52
    • 0037470139 scopus 로고    scopus 로고
    • Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B
    • J. Zhang H. Herscovitz Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B J. Biol. Chem. 278 2003 7459 7468
    • (2003) J. Biol. Chem. , vol.278 , pp. 7459-7468
    • Zhang, J.1    Herscovitz, H.2
  • 53
    • 0036337962 scopus 로고    scopus 로고
    • Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein
    • X. Zhang C. Glendening H. Linke C.L. Parks C. Brooks S.A. Udem M.J. Oglesbee Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein J. Virol. 76 2002 8737 8746
    • (2002) J. Virol. , vol.76 , pp. 8737-8746
    • Zhang, X.1    Glendening, C.2    Linke, H.3    Parks, C.L.4    Brooks, C.5    Udem, S.A.6    Oglesbee, M.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.