메뉴 건너뛰기




Volumn 100, Issue 1, 2011, Pages 90-97

Two conserved residues are important for inducing highly ordered membrane domains by the transmembrane domain of influenza hemagglutinin

Author keywords

[No Author keywords available]

Indexed keywords


EID: 78651229088     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.11.014     Document Type: Article
Times cited : (25)

References (39)
  • 1
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • White, J. M., S. E. Delos, ., K. Schornberg. 2008. Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43:189-219.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Schornberg, K.3
  • 2
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • Martens, S., and H. T. McMahon. 2008. Mechanisms of membrane fusion: Disparate players and common principles. Nat. Rev. Mol. Cell Biol. 9:543-556.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 4
    • 0037810986 scopus 로고    scopus 로고
    • Viral fusion proteins: Multiple regions contribute to membrane fusion
    • Peisajovich, S. G., and Y. Shai. 2003. Viral fusion proteins: Multiple regions contribute to membrane fusion. Biochim. Biophys. Acta. 1614:122-129.
    • (2003) Biochim. Biophys. Acta. , vol.1614 , pp. 122-129
    • Peisajovich, S.G.1    Shai, Y.2
  • 5
    • 41149157914 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane (TM) domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: Substitution of heterologous TM domains
    • Li, Z., and G. W. Blissard. 2008. Functional analysis of the transmembrane (TM) domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: Substitution of heterologous TM domains. J. Virol. 82:3329-3341.
    • (2008) J. Virol. , vol.82 , pp. 3329-3341
    • Li, Z.1    Blissard, G.W.2
  • 6
    • 66149118534 scopus 로고    scopus 로고
    • The Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: Analysis of transmembrane domain length and sequence requirements
    • Li, Z., and G.W. Blissard. 2009. The Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: Analysis of transmembrane domain length and sequence requirements. J. Virol. 83:4447-4461.
    • (2009) J. Virol. , vol.83 , pp. 4447-4461
    • Li, Z.1    Blissard, G.W.2
  • 7
    • 31144434388 scopus 로고    scopus 로고
    • Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry
    • Broer, R., B. Boson, ., J. Corver. 2006. Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry. J. Virol. 80:1302-1310.
    • (2006) J. Virol. , vol.80 , pp. 1302-1310
    • Broer, R.1    Boson, B.2    Corver, J.3
  • 8
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G. W., T. Danieli, and J. M. White. 1994. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell. 76:383-391.
    • (1994) Cell. , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 9
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda, M., G. P. Leser, C. J. Russell, and R. A. Lamb. 2003. Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc. Natl. Acad. Sci. USA. 100:14610-14617.
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 10
    • 68949109991 scopus 로고    scopus 로고
    • Fusion peptide from influenza hemagglutinin increases membrane surface order: An electron-spin resonance study
    • Ge, M., and J. H. Freed. 2009. Fusion peptide from influenza hemagglutinin increases membrane surface order: An electron-spin resonance study. Biophys. J. 96:4925-4934.
    • (2009) Biophys. J. , vol.96 , pp. 4925-4934
    • Ge, M.1    Freed, J.H.2
  • 11
    • 0020477449 scopus 로고
    • Role of lipid phase separations and membrane hydration in phospholipid vesicle fusion
    • Hoekstra, D. 1982. Role of lipid phase separations and membrane hydration in phospholipid vesicle fusion. Biochemistry. 21:2833-2840.
    • (1982) Biochemistry. , vol.21 , pp. 2833-2840
    • Hoekstra, D.1
  • 12
    • 0033539603 scopus 로고    scopus 로고
    • Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: Probing the role of hydrophobic residue size in the central region of the fusion peptide
    • Han, X., D. A. Steinhauer,., L. K. Tamm. 1999. Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: Probing the role of hydrophobic residue size in the central region of the fusion peptide. Biochemistry. 38:15052-15059.
    • (1999) Biochemistry. , vol.38 , pp. 15052-15059
    • Han, X.1    Steinhauer, D.A.2    Tamm, L.K.3
  • 13
    • 77957054960 scopus 로고
    • Cation-induced vesicle fusion modulated by polymers and proteins
    • R. Lipowsky and E. Sackman, editors. Elsevier Science, Amsterdam/ New York.
    • Arnold, K. 1995. Cation-induced vesicle fusion modulated by polymers and proteins. In Structure and Dynamics of Membranes. R. Lipowsky and E. Sackman, editors. Elsevier Science, Amsterdam/ New York. 903-957.
    • (1995) Structure and Dynamics of Membranes , pp. 903-957
    • Arnold, K.1
  • 14
    • 0019889075 scopus 로고
    • Calcium/ magnesium specificity in membrane fusion: Kinetics of aggregation and fusion of phosphatidylserine vesicles and the role of bilayer curvature
    • Wilschut, J., N. Düzgünes x, and D. Papahadjopoulos. 1981. Calcium/ magnesium specificity in membrane fusion: Kinetics of aggregation and fusion of phosphatidylserine vesicles and the role of bilayer curvature. Biochemistry. 20:3126-3133.
    • (1981) Biochemistry. , vol.20 , pp. 3126-3133
    • Wilschut, J.1    Düzgünesx, N.2    Papahadjopoulos, D.3
  • 15
    • 0034711760 scopus 로고    scopus 로고
    • Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin
    • Tatulian, S. A., and L. K. Tamm. 2000. Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin. Biochemistry. 39:496-507.
    • (2000) Biochemistry. , vol.39 , pp. 496-507
    • Tatulian, S.A.1    Tamm, L.K.2
  • 16
    • 40949146126 scopus 로고    scopus 로고
    • Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex
    • Chang, D.-K., S.-F. Cheng, ., Y. T. Liu. 2008. Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex. BMC Biol. 6:2.
    • (2008) BMC Biol. , vol.6 , pp. 2
    • Chang, D.-K.1    Cheng, S.-F.2    Liu, Y.T.3
  • 17
    • 0000326938 scopus 로고    scopus 로고
    • Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm
    • Budil, D. E., S. Lee, ., J. H. Freed. 1996. Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm. J. Magn. Reson. A. 120: 155-189.
    • (1996) J. Magn. Reson. A. , vol.120 , pp. 155-189
    • Budil, D.E.1    Lee, S.2    Freed, J.H.3
  • 18
    • 0000133712 scopus 로고
    • Electron-spin relaxation and ordering in smectic and supercooled nematic liquid crystals
    • Meirovitch, E., D. Igner,., J. H. Freed. 1982. Electron-spin relaxation and ordering in smectic and supercooled nematic liquid crystals. J. Chem. Phys. 77:3915-3938.
    • (1982) J. Chem. Phys. , vol.77 , pp. 3915-3938
    • Meirovitch, E.1    Igner, D.2    Freed, J.H.3
  • 19
    • 0001867405 scopus 로고
    • Calculating slow motional magnetic resonance spectra: A user's guide
    • L. J. Berliner and J. Reuben, editors, Plenum Press, New York
    • Schneider, D. J., and J. H. And. Freed. 1989. Calculating slow motional magnetic resonance spectra: A user's guide. In Spin Labeling Theory and Applications, Vol. 8. L. J. Berliner and J. Reuben, editors. Plenum Press, New York. 1-76.
    • (1989) Spin Labeling Theory and Applications , vol.8 , pp. 1-76
    • Schneider, D.J.1    Freed J.H, A.2
  • 20
    • 0344981517 scopus 로고    scopus 로고
    • Hydration, structure, and molecular interactions in the headgroup region of dioleoylphospatidylcholine bilayers: An electron-spin resonance study
    • Ge, M., and J. H. Freed. 2003. Hydration, structure, and molecular interactions in the headgroup region of dioleoylphospatidylcholine bilayers: An electron-spin resonance study. Biophys. J. 85:4023-4040.
    • (2003) Biophys. J. , vol.85 , pp. 4023-4040
    • Ge, M.1    Freed, J.H.2
  • 21
    • 0032907145 scopus 로고    scopus 로고
    • Electron-spin resonance study of aggregation of gramicidin in dipalmitoylphosphatidylcholine bilayers and hydrophobic mismatch
    • Ge, M., and J. H. Freed. 1999. Electron-spin resonance study of aggregation of gramicidin in dipalmitoylphosphatidylcholine bilayers and hydrophobic mismatch. Biophys. J. 76:264-280.
    • (1999) Biophys. J. , vol.76 , pp. 264-280
    • Ge, M.1    Freed, J.H.2
  • 22
    • 0041343028 scopus 로고    scopus 로고
    • Ordered and disordered phases coexist in plasma membrane vesicles of RBL-2H3 mast cells. An ESR study
    • Ge, M., A. Gidwani, ., J. H. Freed. 2003. Ordered and disordered phases coexist in plasma membrane vesicles of RBL-2H3 mast cells. An ESR study. Biophys. J. 85:1278-1288.
    • (2003) Biophys. J. , vol.85 , pp. 1278-1288
    • Ge, M.1    Gidwani, A.2    Freed, J.H.3
  • 23
    • 0019828883 scopus 로고
    • Solid-state carbon-13 nuclear magnetic resonance of the lecithin gel to liquidcrystalline phase transition
    • Wittebort, R. J., C. F. Schmidt, and R. G. Griffin. 1981. Solid-state carbon-13 nuclear magnetic resonance of the lecithin gel to liquidcrystalline phase transition. Biochemistry. 20:4223-4228.
    • (1981) Biochemistry. , vol.20 , pp. 4223-4228
    • Wittebort, R.J.1    Schmidt, C.F.2    Griffin, R.G.3
  • 24
    • 0033594934 scopus 로고    scopus 로고
    • Quantitative analysis of phospholipids in functionally important membrane domains from RBL-2H3 mast cells using tandem highresolution mass spectrometry
    • Fridriksson, E. K., P. A. Shipkova, ., F. W. McLafferty. 1999. Quantitative analysis of phospholipids in functionally important membrane domains from RBL-2H3 mast cells using tandem highresolution mass spectrometry. Biochemistry. 38:8056-8063.
    • (1999) Biochemistry. , vol.38 , pp. 8056-8063
    • Fridriksson, E.K.1    Shipkova, P.A.2    McLafferty, F.W.3
  • 25
    • 0020492209 scopus 로고
    • Phospholipid vesicle aggregation: Effect of monovalent and divalent ions
    • Ohki, S., N. Düzgünes x, and K. Leonards. 1982. Phospholipid vesicle aggregation: Effect of monovalent and divalent ions. Biochemistry. 21:2127-2133.
    • (1982) Biochemistry. , vol.21 , pp. 2127-2133
    • Ohki, S.1    Düzgünes, N.2    Leonards, K.3
  • 26
    • 0342998559 scopus 로고
    • Water-mediated effect of PEG on membrane properties and fusion
    • S. Ohki, D. Doyle, T. D. Flanagan, S.W. Hui, and E. Mayhew., editors, Plenum Press, New York/London
    • Arnold, K., A. Hermman, ., L. Pratsch. 1987. Water-mediated effect of PEG on membrane properties and fusion. In Molecular Mechanism of Membrane Fusion. S. Ohki, D. Doyle, T. D. Flanagan, S.W. Hui, and E. Mayhew., editors. Plenum Press, New York/London. 255-273.
    • (1987) Molecular Mechanism of Membrane Fusion , pp. 255-273
    • Arnold, K.1    Hermman, A.2    Pratsch, L.3
  • 27
    • 34247221062 scopus 로고    scopus 로고
    • Water near lipid membranes as seen by infrared spectroscopy
    • Binder, H. 2007. Water near lipid membranes as seen by infrared spectroscopy. Eur. Biophys. J. 36:265-279.
    • (2007) Eur. Biophys. J. , vol.36 , pp. 265-279
    • Binder, H.1
  • 28
    • 0029181562 scopus 로고
    • Role of interactions at the lipid-water interface for domain formation
    • Gawrisch, K., J. A. Barry, ., J. A. Ferretti. 1995. Role of interactions at the lipid-water interface for domain formation. Mol. Membr. Biol. 12:83-88.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 83-88
    • Gawrisch, K.1    Barry, J.A.2    Ferretti, J.A.3
  • 29
    • 0017595651 scopus 로고
    • Phase separation of acidic and neutral phospholipids induced by human myelin basic protein
    • Boggs, J. M., M. A. Moscarello, and D. Papahadjopoulos. 1977. Phase separation of acidic and neutral phospholipids induced by human myelin basic protein. Biochemistry. 16:5420-5426.
    • (1977) Biochemistry. , vol.16 , pp. 5420-5426
    • Boggs, J.M.1    Moscarello, M.A.2    Papahadjopoulos, D.3
  • 30
    • 58149288322 scopus 로고    scopus 로고
    • Pinched multilamellar structure of aggregates of lysozyme and phosphatidylserinecontaining membranes revealed by FRET
    • Coutinho, A., L. M. S. Loura,., M. Prieto. 2008. Pinched multilamellar structure of aggregates of lysozyme and phosphatidylserinecontaining membranes revealed by FRET. Biophys. J. 95:4726-4736.
    • (2008) Biophys. J. , vol.95 , pp. 4726-4736
    • Coutinho, A.1    Loura, L.M.S.2    Prieto, M.3
  • 31
    • 0042485425 scopus 로고
    • Surface tension, hydration energy and membrane fusion
    • S. Ohki, D. Doyle, T. D. Flanagan, S. W. Hui, and E. Mayhew, editors, Plenum Press, New York/London
    • Ohki, S. 1987. Surface tension, hydration energy and membrane fusion. In Molecular Mechanism of Membrane Fusion. S. Ohki, D. Doyle, T. D. Flanagan, S. W. Hui, and E. Mayhew, editors. Plenum Press, New York/London. 123-138.
    • (1987) Molecular Mechanism of Membrane Fusion , pp. 123-138
    • Ohki, S.1
  • 32
    • 0001183290 scopus 로고
    • Direct experimental verification of the Kelvin equation for capillary condensation
    • Fisher, L. R., and J. N. Israelachvili. 1979. Direct experimental verification of the Kelvin equation for capillary condensation. Nature. 277:548-549.
    • (1979) Nature. , vol.277 , pp. 548-549
    • Fisher, L.R.1    Israelachvili, J.N.2
  • 34
    • 0344688277 scopus 로고    scopus 로고
    • Capillary induced negative pressure of water plugs in nanochannels
    • Tas, N. R., P. Mela,., A. van den Berg. 2003. Capillary induced negative pressure of water plugs in nanochannels. Nano Lett. 3:1537-1540.
    • (2003) Nano Lett. , vol.3 , pp. 1537-1540
    • Tas, N.R.1    Mela, P.2    Van Den, Berg.A.3
  • 35
    • 77950528480 scopus 로고    scopus 로고
    • Architecture of a nascent viral fusion pore
    • Lee, K. K. 2010. Architecture of a nascent viral fusion pore. EMBO J. 29:1299-1311.
    • (2010) EMBO J. , vol.29 , pp. 1299-1311
    • Lee, K.K.1
  • 36
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell. 73:823-832.
    • (1993) Cell. , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 37
    • 0033582785 scopus 로고    scopus 로고
    • The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion
    • Epand, R. F., J. C. Macosko,., R. M. Epand. 1999. The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion. J. Mol. Biol. 286:489-503.
    • (1999) J. Mol. Biol. , vol.286 , pp. 489-503
    • Epand, R.F.1    Macosko, J.C.2    Epand, R.M.3
  • 38
    • 0032488623 scopus 로고    scopus 로고
    • The mechanism for low-pH-induced clustering of phospholipid vesicles carrying the HA2 ectodomain of influenza hemagglutinin
    • Kim, C.-H., J. C. Macosko, and Y.-K. Shin. 1998. The mechanism for low-pH-induced clustering of phospholipid vesicles carrying the HA2 ectodomain of influenza hemagglutinin. Biochemistry. 37:137-144.
    • (1998) Biochemistry. , vol.37 , pp. 137-144
    • Kim, C.-H.1    Macosko, J.C.2    Shin, Y.-K.3
  • 39
    • 0034646448 scopus 로고    scopus 로고
    • Factors determining vesicular lipid mixing induced by shortened constructs of influenza hemagglutinin
    • LeDuc, D. L., Y.-K. Shin, ., R. M. Epand. 2000. Factors determining vesicular lipid mixing induced by shortened constructs of influenza hemagglutinin. Biochemistry. 39:2733-2739.
    • (2000) Biochemistry. , vol.39 , pp. 2733-2739
    • LeDuc, D.L.1    Shin, Y.-K.2    Epand, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.