메뉴 건너뛰기




Volumn 7, Issue 11, 1998, Pages 2359-2373

ph-Induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers

Author keywords

Conformational change; Influenza hemagglutinin; Lipid protein interaction; Membrane fusion; Polarized ATR Fourier transform infrared spectroscopy

Indexed keywords

BROMELAIN; VIRUS HEMAGGLUTININ;

EID: 0031793435     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071113     Document Type: Article
Times cited : (34)

References (53)
  • 2
    • 0024291319 scopus 로고
    • 13C=O-labeled phospholipids hydrogen bonding to carbonyl groups
    • 13C=O-labeled phospholipids hydrogen bonding to carbonyl groups. Biochemistry 27:8239-8249.
    • (1988) Biochemistry , vol.27 , pp. 8239-8249
    • Blume, A.1    Hübner, W.2    Messner, G.3
  • 3
    • 0029823936 scopus 로고    scopus 로고
    • Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events
    • Blumenthal R, Sarkar DP, Durell S, Howard DE, Morris SJ. 1996. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. J Cell Biol 135:63-71.
    • (1996) J Cell Biol , vol.135 , pp. 63-71
    • Blumenthal, R.1    Sarkar, D.P.2    Durell, S.3    Howard, D.E.4    Morris, S.J.5
  • 4
    • 0015491828 scopus 로고
    • Crystalline antigen from the influenza virus envelope
    • Brand CM, Skehel JJ. 1972. Crystalline antigen from the influenza virus envelope. Nature New Biol 238:145-147.
    • (1972) Nature New Biol , vol.238 , pp. 145-147
    • Brand, C.M.1    Skehel, J.J.2
  • 5
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 6
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HTV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS. 1997. Core structure of gp41 from the HTV envelope glycoprotein. Cell 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 9
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli T, Pelletier SL, Henis YI, White JM. 1996. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J Cell Biol 133:559-569.
    • (1996) J Cell Biol , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 11
    • 0021984076 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin. The low pH-induced conformational change
    • Doms RW, Helenius A, White J. 1985. Membrane fusion activity of the influenza virus hemagglutinin. The low pH-induced conformational change. J Biol Chem 260:2973-2981.
    • (1985) J Biol Chem , vol.260 , pp. 2973-2981
    • Doms, R.W.1    Helenius, A.2    White, J.3
  • 12
    • 0030010945 scopus 로고    scopus 로고
    • +-induced membrane insertion of influenza virus hemagglutinin involves the HA2 ammo-terminal fusion peptide but not the coiled coil region
    • +-induced membrane insertion of influenza virus hemagglutinin involves the HA2 ammo-terminal fusion peptide but not the coiled coil region. J Biol Chem 271:13417-13421.
    • (1996) J Biol Chem , vol.271 , pp. 13417-13421
    • Durrer, P.1    Galli, C.2    Hoenke, S.3    Corti, C.4    Glück, T.5    Vorherr, T.6    Brunner, J.7
  • 13
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander SW, Mayne L. 1992. Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu Rev Biophys Biomol Struct 21:243-265.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 14
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 Å resolution
    • Fass D, Harrison SC, Kim PS. 1996. Retrovirus envelope domain at 1.7 Å resolution. Nature Struct Biol 3:465-469.
    • (1996) Nature Struct Biol , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 15
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study
    • Frey S, Tamm LK. 1991. Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study. Biophys J 60:922-930.
    • (1991) Biophys J , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 16
    • 0022619527 scopus 로고
    • Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus
    • Gething MJ, Doms RW, York D, White J. 1986. Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus. J Cell Biol 102:11-23.
    • (1986) J Cell Biol , vol.102 , pp. 11-23
    • Gething, M.J.1    Doms, R.W.2    York, D.3    White, J.4
  • 18
    • 0030768271 scopus 로고    scopus 로고
    • Structural studies on membrane-embedded influenza hemagglutinin and its fragments
    • Gray C, Tamm LK. 1997. Structural studies on membrane-embedded influenza hemagglutinin and its fragments. Protein Sci 6:1993-2006.
    • (1997) Protein Sci , vol.6 , pp. 1993-2006
    • Gray, C.1    Tamm, L.K.2
  • 19
    • 0030012221 scopus 로고    scopus 로고
    • Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers
    • Gray C, Tatulian SA, Wharton SA, Tamm LK. 1996. Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers. Biophys J 70:2275-2286.
    • (1996) Biophys J , vol.70 , pp. 2275-2286
    • Gray, C.1    Tatulian, S.A.2    Wharton, S.A.3    Tamm, L.K.4
  • 20
    • 0030019825 scopus 로고    scopus 로고
    • Specific recognition of coiled coils by infrared spectroscopy: Analysis of the three structural domains of type III intermediate filament proteins
    • Heimburg T, Schuenemann J, Weber K, Geisler N. 1996. Specific recognition of coiled coils by infrared spectroscopy: Analysis of the three structural domains of type III intermediate filament proteins. Biochemistry 35:1375-1382.
    • (1996) Biochemistry , vol.35 , pp. 1375-1382
    • Heimburg, T.1    Schuenemann, J.2    Weber, K.3    Geisler, N.4
  • 21
    • 0028043265 scopus 로고
    • Reconstitution of membrane fusion sites. A total internal reflection fluorescence microscopy study of influenza hemagglutinin-mediated membrane fusion
    • Hinterdorfer P, Baber G, Tamm LK. 1994. Reconstitution of membrane fusion sites. A total internal reflection fluorescence microscopy study of influenza hemagglutinin-mediated membrane fusion. J Biol Chem 269:20360-20368.
    • (1994) J Biol Chem , vol.269 , pp. 20360-20368
    • Hinterdorfer, P.1    Baber, G.2    Tamm, L.K.3
  • 22
    • 0029018548 scopus 로고
    • The use and misuse of ETIR spectroscopy in the determination of protein structure
    • Jackson M, Mantsch, HH. 1995. The use and misuse of ETIR spectroscopy in the determination of protein structure. Crit Rev Biochem Mol Biol 30:95-120.
    • (1995) Crit Rev Biochem Mol Biol , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 23
    • 77957095245 scopus 로고
    • Nonlinear least-squares analysis
    • Johnson ML, Frasier SG. 1985. Nonlinear least-squares analysis. Meth Enzymol 117:301-342.
    • (1985) Meth Enzymol , vol.117 , pp. 301-342
    • Johnson, M.L.1    Frasier, S.G.2
  • 24
    • 0026772024 scopus 로고
    • Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin
    • Kemble GW, Bodian DL, Rose J, Wilson IA, White JM. 1992. Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin. J Virol 66:4940-4950.
    • (1992) J Virol , vol.66 , pp. 4940-4950
    • Kemble, G.W.1    Bodian, D.L.2    Rose, J.3    Wilson, I.A.4    White, J.M.5
  • 25
    • 0029665093 scopus 로고    scopus 로고
    • On the dynamics and conformation of the HA2 domain of the influenza virus hemagglutinin
    • Kim C-H, Macosko JC, Yu UG, Shin Y-K. 1996. On the dynamics and conformation of the HA2 domain of the influenza virus hemagglutinin. Biochemistry 35:5359-5365.
    • (1996) Biochemistry , vol.35 , pp. 5359-5365
    • Kim, C.-H.1    Macosko, J.C.2    Yu, U.G.3    Shin, Y.-K.4
  • 26
    • 0030953859 scopus 로고    scopus 로고
    • Transient changes of the conformation of hemagglutinin of influenza virus at low pH detected by time-resolved circular dichroism spectroscopy
    • Korte T, Ludwig K, Krumbiegel M, Zirwer D, Damaschun G, Herrmann A. 1997. Transient changes of the conformation of hemagglutinin of influenza virus at low pH detected by time-resolved circular dichroism spectroscopy. J Biol Chem 272:9764-9770.
    • (1997) J Biol Chem , vol.272 , pp. 9764-9770
    • Korte, T.1    Ludwig, K.2    Krumbiegel, M.3    Zirwer, D.4    Damaschun, G.5    Herrmann, A.6
  • 27
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S, Bandekar J. 1986. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv Prot Chem 38:181-364.
    • (1986) Adv Prot Chem , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 28
    • 0027394117 scopus 로고
    • Role of calcium in the adhesion and fusion of bilayers
    • Leckband DE, Helm CA, Israelachvili J. 1993. Role of calcium in the adhesion and fusion of bilayers. Biochemistry 32:1127-1140.
    • (1993) Biochemistry , vol.32 , pp. 1127-1140
    • Leckband, D.E.1    Helm, C.A.2    Israelachvili, J.3
  • 29
    • 0030943586 scopus 로고    scopus 로고
    • Evolution of lipidic structures during model membrane fusion and the relation of this process to cell membrane fusion
    • Lee J, Lentz BR. 1997. Evolution of lipidic structures during model membrane fusion and the relation of this process to cell membrane fusion. Biochemistry 36:6251-6259.
    • (1997) Biochemistry , vol.36 , pp. 6251-6259
    • Lee, J.1    Lentz, B.R.2
  • 30
    • 0027987329 scopus 로고
    • Components of the carbonyl stretching band in the infrared spectra of hydrated 1,2-diacylglycerolipid bilayers: A reevaluation
    • Lewis RNAH, McElhaney RN, Pohle W, Mantsch HH. 1994. Components of the carbonyl stretching band in the infrared spectra of hydrated 1,2-diacylglycerolipid bilayers: A reevaluation. Biophys J 67:2367-2375.
    • (1994) Biophys J , vol.67 , pp. 2367-2375
    • Lewis, R.N.A.H.1    McElhaney, R.N.2    Pohle, W.3    Mantsch, H.H.4
  • 31
    • 0030928208 scopus 로고    scopus 로고
    • Dichroic ratios in polarized Fourier transform infrared for nonaxial symmetry of β-sheet structures
    • Marsh D. 1997. Dichroic ratios in polarized Fourier transform infrared for nonaxial symmetry of β-sheet structures. Biophys J 72:2710-2718.
    • (1997) Biophys J , vol.72 , pp. 2710-2718
    • Marsh, D.1
  • 32
    • 0000238336 scopus 로고
    • A simplex method for function minimization
    • Nelder JA, Mead R. 1965. A simplex method for function minimization. Comput J 7:308-313.
    • (1965) Comput J , vol.7 , pp. 308-313
    • Nelder, J.A.1    Mead, R.2
  • 33
    • 0032526413 scopus 로고    scopus 로고
    • Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity
    • Qiao H, Pelletier SL, Hoffman L, Hacker J, Armstrong RT, White J. 1998. Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity. J Cell Biol 141:1335-1347.
    • (1998) J Cell Biol , vol.141 , pp. 1335-1347
    • Qiao, H.1    Pelletier, S.L.2    Hoffman, L.3    Hacker, J.4    Armstrong, R.T.5    White, J.6
  • 34
    • 0024378918 scopus 로고
    • Hydration forces between phospholipid bilayers
    • Rand RP, Parsegian VA. 1989. Hydration forces between phospholipid bilayers. Biochim Biophys Acta 988:351-376.
    • (1989) Biochim Biophys Acta , vol.988 , pp. 351-376
    • Rand, R.P.1    Parsegian, V.A.2
  • 35
    • 0030062907 scopus 로고    scopus 로고
    • Infrared amide I' band of the coiled coil
    • Reisdorf WC, Krimm S. 1996. Infrared amide I' band of the coiled coil. Biochemistry 35:1383-1386.
    • (1996) Biochemistry , vol.35 , pp. 1383-1386
    • Reisdorf, W.C.1    Krimm, S.2
  • 40
    • 0029828938 scopus 로고    scopus 로고
    • Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity
    • Steinhauer DA, Martin J, Lin YP, Martin SA, Oldstone MB, Skehel JJ, Wiley DC. 1996. Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity. Proc Natl Acad Sci USA 93:12873-12878.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12873-12878
    • Steinhauer, D.A.1    Martin, J.2    Lin, Y.P.3    Martin, S.A.4    Oldstone, M.B.5    Skehel, J.J.6    Wiley, D.C.7
  • 41
    • 0028824850 scopus 로고
    • Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer DA, Wharton SA, Skehel JJ, Wiley DC. 1995. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J Virol 69:6643-6651.
    • (1995) J Virol , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 42
    • 0026750648 scopus 로고
    • Monte Carlo method for determining complete confidence probability distributions of estimated model parameters
    • Straume M, Johnson ML. 1992. Monte Carlo method for determining complete confidence probability distributions of estimated model parameters. Meth Enzymol 210:117-128.
    • (1992) Meth Enzymol , vol.210 , pp. 117-128
    • Straume, M.1    Johnson, M.L.2
  • 43
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy
    • Surewicz WK, Mantsch HH, Chapman D. 1993. Determination of protein secondary structure by Fourier transform infrared spectroscopy. Biochemistry 32:7720-7726.
    • (1993) Biochemistry , vol.32 , pp. 7720-7726
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 44
    • 0027240319 scopus 로고
    • Orientation of functional and nonfunctional PTS permease signal sequences in lipid bilayers. A polarized attenuated total reflection infrared study
    • Tamm LK, Tatulian SA. 1993. Orientation of functional and nonfunctional PTS permease signal sequences in lipid bilayers. A polarized attenuated total reflection infrared study. Biochemistry 32:7720-7726.
    • (1993) Biochemistry , vol.32 , pp. 7720-7726
    • Tamm, L.K.1    Tatulian, S.A.2
  • 45
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm LK, Tatulian SA. 1997. Infrared spectroscopy of proteins and peptides in lipid bilayers. Quart Rev Biophys 30:365-429.
    • (1997) Quart Rev Biophys , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 46
    • 0028820162 scopus 로고
    • Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy
    • Tatulian SA, Hinterdorfer P, Baber G, Tamm LK. 1995. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO J 14:5514-5523.
    • (1995) EMBO J , vol.14 , pp. 5514-5523
    • Tatulian, S.A.1    Hinterdorfer, P.2    Baber, G.3    Tamm, L.K.4
  • 47
    • 0030593483 scopus 로고    scopus 로고
    • Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin
    • Tatulian SA, Tamm LK. 1996. Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin. J Mol Biol 260:312-316.
    • (1996) J Mol Biol , vol.260 , pp. 312-316
    • Tatulian, S.A.1    Tamm, L.K.2
  • 48
    • 0001242101 scopus 로고
    • Infrared dichroism and molecular conformation of α-form poly-γ-benzyl-L-glutamate
    • Tsuboi M. 1962. Infrared dichroism and molecular conformation of α-form poly-γ-benzyl-L-glutamate. J Polymer Sci 59:139-153.
    • (1962) J Polymer Sci , vol.59 , pp. 139-153
    • Tsuboi, M.1
  • 51
    • 0023909196 scopus 로고
    • Conformational aspects of the acid-induced fusion mechanism of influenza virus hemagglutinin. Circular dichroism and fluorescence studies
    • Wharton SA, Ruigrok RWH, Martin SR, Skehel JJ, Bayley PM, Weis W, Wiley DC. 1988. Conformational aspects of the acid-induced fusion mechanism of influenza virus hemagglutinin. Circular dichroism and fluorescence studies. J Biol Chem 263:4474-4480.
    • (1988) J Biol Chem , vol.263 , pp. 4474-4480
    • Wharton, S.A.1    Ruigrok, R.W.H.2    Martin, S.R.3    Skehel, J.J.4    Bayley, P.M.5    Weis, W.6    Wiley, D.C.7
  • 52
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational changes: Low pH-activation of the influenza virus hemagglutinin
    • White JM, Wilson IA. 1987. Anti-peptide antibodies detect steps in a protein conformational changes: Low pH-activation of the influenza virus hemagglutinin. J Cell Biol 105:2887-2896.
    • (1987) J Cell Biol , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 53
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 a resolution
    • Wilson IA, Skehel JJ, Wiley DC. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.