메뉴 건너뛰기




Volumn 277, Issue 2, 1998, Pages 161-169

Membrane-induced alterations in HIV-1 Gag and matrix protein-protein interactions

Author keywords

Fluorescence anisotropy; Gag MA oligomerization; Human immunodeficiency virus; Membrane binding; Resonance energy transfer

Indexed keywords

FLUORESCEIN; GAG PROTEIN; LYSINE; OLIGOMER; PHOSPHOLIPID; PROTEIN SUBUNIT; RHODAMINE; VIRUS PROTEIN;

EID: 0032571298     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1615     Document Type: Editorial
Times cited : (47)

References (42)
  • 1
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia R.C., Tian H., Jensen F. Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc. Natl Acad. Sci. USA. 90:1993;5181-5185
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.3
  • 3
    • 0027501033 scopus 로고
    • Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus Gag proteins
    • Bennett R.P., Nelle T.D., Wills J.W. Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus Gag proteins. J. Virol. 6:1993;6487-6498
    • (1993) J. Virol. , vol.6 , pp. 6487-6498
    • Bennett, R.P.1    Nelle, T.D.2    Wills, J.W.3
  • 4
    • 0025176624 scopus 로고
    • Myristylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant M., Ratner L. Myristylation-dependent replication and assembly of human immunodeficiency virus 1. Proc. Natl Acad. Sci. USA. 87:1990;523-527
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 8
    • 0027480022 scopus 로고
    • Phosphorylation of HIV-1 gag proteins by protein kinase C
    • Burnette B., Yu G., Felsted R.L. Phosphorylation of HIV-1 gag proteins by protein kinase C. J. Biol. Chem. 268:1993;8698-8703
    • (1993) J. Biol. Chem. , vol.268 , pp. 8698-8703
    • Burnette, B.1    Yu, G.2    Felsted, R.L.3
  • 9
    • 0030791698 scopus 로고    scopus 로고
    • Human immunodeficiency virus matrix tyrosine phosphorylation: Characterization of the kinase and its substrate requirements
    • Camaur D., Gallay P., Swingler S., Trono D. Human immunodeficiency virus matrix tyrosine phosphorylation characterization of the kinase and its substrate requirements. J. Virol. 71:1997;6835-6841
    • (1997) J. Virol. , vol.71 , pp. 6835-6841
    • Camaur, D.1    Gallay, P.2    Swingler, S.3    Trono, D.4
  • 10
    • 0029015825 scopus 로고
    • Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein
    • Craven R.C., Leure-du-Pree A.E., Weldon R.A. Jr, Wills J.W. Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein. J. Virol. 69:1995;4212-4227
    • (1995) J. Virol. , vol.69 , pp. 4212-4227
    • Craven, R.C.1    Leure-Du-Pree, A.E.2    Weldon Jr., R.A.3    Wills, J.W.4
  • 11
    • 0001931483 scopus 로고
    • Protein biosynthesis and assembly
    • R. Weiss, N. Teich, H. Varmus, & J. Coffin. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Dickson C., Eisenman R., Fan H., Hunter E., Teich N. Protein biosynthesis and assembly. Weiss R., Teich N., Varmus H., Coffin J. RNA Tumor Viruses. 1984;513-648 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1984) RNA Tumor Viruses , pp. 513-648
    • Dickson, C.1    Eisenman, R.2    Fan, H.3    Hunter, E.4    Teich, N.5
  • 12
    • 0029807054 scopus 로고    scopus 로고
    • The major homology region of the HIV-1 Gag precursor influences membrane binding
    • Ebbets-Reed D., Scarlata S., Carter C.A. The major homology region of the HIV-1 Gag precursor influences membrane binding. Biochemistry. 35:1996;14268-14275
    • (1996) Biochemistry , vol.35 , pp. 14268-14275
    • Ebbets-Reed, D.1    Scarlata, S.2    Carter, C.A.3
  • 13
    • 0025010060 scopus 로고
    • Expression in Escherica coli and purification of human immunodeficiency virus type 1 capsid protein (p24)
    • Ehrlich L.S., Krausslich H.G., Wimmer E., Carter C.A. Expression in Escherica coli and purification of human immunodeficiency virus type 1 capsid protein (p24). AIDS Res. Hum. Reterovir. 6:1990;1169-1175
    • (1990) AIDS Res. Hum. Reterovir. , vol.6 , pp. 1169-1175
    • Ehrlich, L.S.1    Krausslich, H.G.2    Wimmer, E.3    Carter, C.A.4
  • 14
    • 0028046987 scopus 로고
    • Spectral analysis and tryptic suspecibility as probes of HIV-1 capsid protein structure
    • Ehrlich L.S., Agresta B., Gelfand C., Jentoft J., Carter C.A. Spectral analysis and tryptic suspecibility as probes of HIV-1 capsid protein structure. Virology. 204:1994;515-525
    • (1994) Virology , vol.204 , pp. 515-525
    • Ehrlich, L.S.1    Agresta, B.2    Gelfand, C.3    Jentoft, J.4    Carter, C.A.5
  • 16
    • 0027177935 scopus 로고
    • A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum
    • Facke M., Janetzko A., Shoeman R.L., Krausslich H.-G. A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum. J. Virol. 67:1993;4972-4980
    • (1993) J. Virol. , vol.67 , pp. 4972-4980
    • Facke, M.1    Janetzko, A.2    Shoeman, R.L.3    Krausslich, H.-G.4
  • 17
    • 0028234481 scopus 로고
    • Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production
    • Freed E.O., Orenstein J.M., Buckler-White A.J., Martin M.A. Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production. J. Virol. 68:1994;5311-5320
    • (1994) J. Virol. , vol.68 , pp. 5311-5320
    • Freed, E.O.1    Orenstein, J.M.2    Buckler-White, A.J.3    Martin, M.A.4
  • 18
    • 0028839344 scopus 로고
    • HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of the integrase
    • Gallay P., Swingler S., Song J., Bushman F., Trono D. HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of the integrase. Cell. 83:1995;569-576
    • (1995) Cell , vol.83 , pp. 569-576
    • Gallay, P.1    Swingler, S.2    Song, J.3    Bushman, F.4    Trono, D.5
  • 19
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Gottlinger H.G., Sodroski J.G., Haseltine W.A. Role of capsid precursor processing and myristylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc. Natl Acad. Sci. USA. 86:1989;5781-5785
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5781-5785
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 21
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric HIV-1 matrix protein: Implications for membrane association and assembly
    • Hill C., Worthylake D., Bancroft D.P., Christensen A.M., Sundquist W.I. Crystal structures of the trimeric HIV-1 matrix protein implications for membrane association and assembly. Proc. Natl Acad. Sci. USA. 93:1996;3099-3104
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 3099-3104
    • Hill, C.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 22
    • 0021909644 scopus 로고
    • Production of large, unilamellar vesicles by a rapid extrusion procedure: Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • Hope M., Bally M., Webb G., Cullis P. Production of large, unilamellar vesicles by a rapid extrusion procedure characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochim. Biophys. Acta. 812:1985;55-65
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.1    Bally, M.2    Webb, G.3    Cullis, P.4
  • 24
    • 0028168754 scopus 로고
    • Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal
    • Lee P.P., Linial M.L. Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal. J. Virol. 68:1994;6644-6654
    • (1994) J. Virol. , vol.68 , pp. 6644-6654
    • Lee, P.P.1    Linial, M.L.2
  • 27
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • McLaughlin S., Aderem A. The myristoyl-electrostatic switch a modulator of reversible protein-membrane interactions. Trends Biol. Sci. 20:1995;272-276
    • (1995) Trends Biol. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 28
    • 0028292220 scopus 로고
    • Fullerene-like organization of Gag-protein shell particles produced by recombinant baculvirus
    • Nermut M.V., Hockley D.J., Jowett J.B.M., Jones I.M., Garreau M., Thomas D. Fullerene-like organization of Gag-protein shell particles produced by recombinant baculvirus. Virology. 198:1994;288-296
    • (1994) Virology , vol.198 , pp. 288-296
    • Nermut, M.V.1    Hockley, D.J.2    Jowett, J.B.M.3    Jones, I.M.4    Garreau, M.5    Thomas, D.6
  • 29
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: Relevance to myristoylated proteins
    • Peitzsch R.M., McLaughlin S. Binding of acylated peptides and fatty acids to phospholipid vesicles relevance to myristoylated proteins. Biochemistry. 32:1993;10436-10443
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 30
    • 0028296723 scopus 로고
    • Characterization of human immunodeficiency virus type 1 Pr55gag membrane association in a cell-free system: Requirement for a C-terminal domain
    • Platt E.J., Haffar O.K. Characterization of human immunodeficiency virus type 1 Pr55gag membrane association in a cell-free system requirement for a C-terminal domain. Proc. Natl Acad. Sci. USA. 91:1994;4594-4598
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4594-4598
    • Platt, E.J.1    Haffar, O.K.2
  • 31
    • 0029565831 scopus 로고
    • Crystal structure of SIV matrix antigen and implications for virus assembly
    • Rao Z., Belyav A., Fry E., Roy P., Jones I.M., Stuart D.I. Crystal structure of SIV matrix antigen and implications for virus assembly. Nature. 378:1995;743-747
    • (1995) Nature , vol.378 , pp. 743-747
    • Rao, Z.1    Belyav, A.2    Fry, E.3    Roy, P.4    Jones, I.M.5    Stuart, D.I.6
  • 32
    • 0029117442 scopus 로고
    • Theory and application of fluorescence homotransfer to melittin oligomerization
    • Runnels L., Scarlata S. Theory and application of fluorescence homotransfer to melittin oligomerization. Biophys. J. 69:1995;1569-1583
    • (1995) Biophys. J. , vol.69 , pp. 1569-1583
    • Runnels, L.1    Scarlata, S.2
  • 33
    • 0028355603 scopus 로고
    • Identification of human immunodeficiency virus type 1 gag protein domains essential to membrane binding and particle assembly
    • Spearman P., Wang J.J., Heyden N.V., Ratner L. Identification of human immunodeficiency virus type 1 gag protein domains essential to membrane binding and particle assembly. J. Virol. 68:1994;3232-3242
    • (1994) J. Virol. , vol.68 , pp. 3232-3242
    • Spearman, P.1    Wang, J.J.2    Heyden, N.V.3    Ratner, L.4
  • 34
    • 0030763024 scopus 로고    scopus 로고
    • Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism
    • Spearman P., Horton R., Ratner L., Kuli-Zade I. Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism. J. Virol. 71:1997;6582-6592
    • (1997) J. Virol. , vol.71 , pp. 6582-6592
    • Spearman, P.1    Horton, R.2    Ratner, L.3    Kuli-Zade, I.4
  • 36
    • 0028136474 scopus 로고
    • Mass analysis of biological macromolecular complexes by STEM
    • Thomas D., Schultz P., Steven A.C., Wall J.S. Mass analysis of biological macromolecular complexes by STEM. Biol. Cell. 80:1994;181-192
    • (1994) Biol. Cell , vol.80 , pp. 181-192
    • Thomas, D.1    Schultz, P.2    Steven, A.C.3    Wall, J.S.4
  • 39
    • 0028234528 scopus 로고
    • The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infection in macrophages and quiescent T lymphocytes
    • von Schwedler U., Kornbluth R.S., Trono D. The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infection in macrophages and quiescent T lymphocytes. Proc. Natl Acad. Sci. USA. 91:1994;6992-6996
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6992-6996
    • Von Schwedler, U.1    Kornbluth, R.S.2    Trono, D.3
  • 40
    • 0022526226 scopus 로고
    • Mass mapping with the scanning transmission electron microscope
    • Wall J.S., Hainfeld J.F. Mass mapping with the scanning transmission electron microscope. Annu. Rev. Biophys. Biophys. Chem. 15:1986;355-376
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 355-376
    • Wall, J.S.1    Hainfeld, J.F.2
  • 41
    • 0029861657 scopus 로고    scopus 로고
    • Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
    • Zhou W., Resh M. Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 70:1996;8540-8548
    • (1996) J. Virol. , vol.70 , pp. 8540-8548
    • Zhou, W.1    Resh, M.2
  • 42
    • 0028218274 scopus 로고
    • Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 gag protein which interacts with acidic phospholipids
    • Zhou W., Parent J., Wills J., Resh M. Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 gag protein which interacts with acidic phospholipids. J. Virol. 68:1994;2556-2569
    • (1994) J. Virol. , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, J.2    Wills, J.3    Resh, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.