메뉴 건너뛰기




Volumn 8, Issue 12, 2013, Pages

Structural analysis of influenza a virus matrix protein M1 and Its self-assemblies at low pH

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX PROTEIN; MATRIX PROTEIN M1; UNCLASSIFIED DRUG;

EID: 84892742823     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0082431     Document Type: Article
Times cited : (58)

References (46)
  • 1
    • 0001178028 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • Knipe D, Howley P (ed), 4th ed. Lippincott Williams & Wilkins, Philadelphia, Pa
    • Lamb R, Krug V (2001) Orthomyxoviridae: the viruses and their replication, In: Knipe D, Howley P (ed), Fundamental virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, Pa, pp. 725-770.
    • (2001) Fundamental Virology , pp. 725-770
    • Lamb, R.1    Krug, V.2
  • 3
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman JS, Lamb RA (2005) Influenza virus assembly and budding. Virology 411:229-236.
    • (2005) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 4
    • 70350786508 scopus 로고    scopus 로고
    • The concept of transmembrane asymmetry of lateral domains in biomemranes and influenza virus envelope fine structure
    • Rus
    • Radyukhin V (2009) The concept of transmembrane asymmetry of lateral domains in biomemranes and influenza virus envelope fine structure. Mol Biol (Rus) 43:533-542.
    • (2009) Mol Biol , vol.43 , pp. 533-542
    • Radyukhin, V.1
  • 5
    • 77950528480 scopus 로고    scopus 로고
    • Architecture of a nascent viral fusion pore
    • Lee V (2010) Architecture of a nascent viral fusion pore. The EMBO J 29:1299-1311.
    • (2010) The EMBO J , vol.29 , pp. 1299-1311
    • Lee, V.1
  • 6
    • 33846822057 scopus 로고    scopus 로고
    • Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes
    • Boulo S, Akarsu H, Ruigrock R, Baudin F (2007) Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes. Virus Res 12:12-21.
    • (2007) Virus Res , vol.12 , pp. 12-21
    • Boulo, S.1    Akarsu, H.2    Ruigrock, R.3    Baudin, F.4
  • 7
    • 0034652401 scopus 로고    scopus 로고
    • Membrane interaction of influenza virus M1 protein
    • Ruigrok R, Barge A, Durrer P, Brunner J, Ma K, et al (2000) Membrane interaction of influenza virus M1 protein. Virology 267:289-298.
    • (2000) Virology , vol.267 , pp. 289-298
    • Ruigrok, R.1    Barge, A.2    Durrer, P.3    Brunner, J.4    Ma, K.5
  • 8
    • 0035840794 scopus 로고    scopus 로고
    • The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1
    • Harris A, Forouhar F, Qiu S, Sha B, Luo M (2001) The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1. Virology 289:34-44.
    • (2001) Virology , vol.289 , pp. 34-44
    • Harris, A.1    Forouhar, F.2    Qiu, S.3    Sha, B.4    Luo, M.5
  • 10
    • 84861358303 scopus 로고    scopus 로고
    • Dissection of Influenza A virus M1 protein: PH dependent oligomerizarion of N-terminal domain and dimerization of C-terminal domain
    • Zhang K, Wang Z, Liu X, Yin C, Basit Z, et al (2012) Dissection of Influenza A virus M1 protein: pH dependent oligomerizarion of N-terminal domain and dimerization of C-terminal domain. PloS One 7:e37786.
    • (2012) PloS One , vol.7
    • Zhang, K.1    Wang, Z.2    Liu, X.3    Yin, C.4    Basit, Z.5
  • 11
    • 0031039724 scopus 로고    scopus 로고
    • Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1
    • Sha B, Luo M (1997) Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1. Nat Struct Biol 4:239-244.
    • (1997) Nat Struct Biol , vol.4 , pp. 239-244
    • Sha, B.1    Luo, M.2
  • 12
    • 0035864293 scopus 로고    scopus 로고
    • Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer
    • Arzt S, Baudin F, Barge A, Timmins P, Burmeister W, et al (2001) Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer. Virology 297:439-444.
    • (2001) Virology , vol.297 , pp. 439-444
    • Arzt, S.1    Baudin, F.2    Barge, A.3    Timmins, P.4    Burmeister, W.5
  • 13
    • 82755192842 scopus 로고    scopus 로고
    • Spatial structure peculiarities of influenza A virus matrix M1 protein in an acidic solution that simulates the internal lysosomal medium
    • Shishkov A, Bogacheva E, Fedorova N, Ksenofontov A, Badun G, et al (2011) Spatial structure peculiarities of influenza A virus matrix M1 protein in an acidic solution that simulates the internal lysosomal medium. FEBS J 278:4905-4916.
    • (2011) FEBS J , vol.278 , pp. 4905-4916
    • Shishkov, A.1    Bogacheva, E.2    Fedorova, N.3    Ksenofontov, A.4    Badun, G.5
  • 15
    • 35748982423 scopus 로고    scopus 로고
    • Analysis of X-ray and neutron scattering from biomacromolecular solutions
    • Petoukhov MV, Svergun DI (2007) Analysis of X-ray and neutron scattering from biomacromolecular solutions. Curr Opin Struct Biol 17:562-571.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 562-571
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 16
    • 77954580347 scopus 로고    scopus 로고
    • Small-angle X-ray and neutron scattering as a tool for structural systems biology
    • Svergun DI (2010) Small-angle X-ray and neutron scattering as a tool for structural systems biology. Biol Chem 391:737-743.
    • (2010) Biol Chem , vol.391 , pp. 737-743
    • Svergun, D.I.1
  • 17
    • 77956190770 scopus 로고    scopus 로고
    • Structural characterization of proteins and complexes using small-angle X-ray solution scattering
    • Mertens HD, Svergun DI (2010) Structural characterization of proteins and complexes using small-angle X-ray solution scattering. J Struct Biol 172:128-41.
    • (2010) J Struct Biol , vol.172 , pp. 128-141
    • Mertens, H.D.1    Svergun, D.I.2
  • 18
    • 0026517512 scopus 로고
    • Isolation of matrix protein M1 from influenza viruses by acid-dependent extraction with nonionic detergent
    • Zhirnov O (1992) Isolation of matrix protein M1 from influenza viruses by acid-dependent extraction with nonionic detergent. Virology 186:324-330.
    • (1992) Virology , vol.186 , pp. 324-330
    • Zhirnov, O.1
  • 19
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.1
  • 21
    • 34248347847 scopus 로고    scopus 로고
    • Upgrade of the Small Angle X-ray scattering Beamline X33 at the EMBL Hamburg
    • Roessle MW, Klaering R, Ristau U, Robrahn B, Jahn D, et al (2007) Upgrade of the Small Angle X-ray scattering Beamline X33 at the EMBL Hamburg. J Appl Cryst 40:s190.
    • (2007) J Appl Cryst , vol.40
    • Roessle, M.W.1    Klaering, R.2    Ristau, U.3    Robrahn, B.4    Jahn, D.5
  • 22
    • 51949084084 scopus 로고    scopus 로고
    • Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33
    • Round AR, Franke D, Moritz S, Huchler R, Fritsche M, et al (2008) Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33. J Appl Cryst 41:913-920.
    • (2008) J Appl Cryst , vol.41 , pp. 913-920
    • Round, A.R.1    Franke, D.2    Moritz, S.3    Huchler, R.4    Fritsche, M.5
  • 24
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirecttransform methods using perceptual criteria
    • Svergun DI (1992) Determination of the regularization parameter in indirecttransform methods using perceptual criteria. J Appl Crystallogr 25:495-505.
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-505
    • Svergun, D.I.1
  • 25
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing, Biophys J 76:2879-2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 26
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from x-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MHJ (2001) Determination of domain structure of proteins from x-ray solution scattering, Biophys J 80:2946-2953.
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 27
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modelling of macromo-lecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI (2005) Global rigid body modelling of macromo-lecular complexes against small-angle scattering data. Biophys J 89:1237-1250.
    • (2005) Biophys J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 28
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • PetoukhovMV, Franke D, Shkumatov AV, Tria G, Kikhney AG, et al (2012) New developments in the ATSAS program package for small-angle scattering data analysis. J Appl Cryst 45:342-350.
    • (2012) J Appl Cryst , vol.45 , pp. 342-350
    • Petoukhov, M.V.1    Franke, D.2    Shkumatov, A.V.3    Tria, G.4    Kikhney, A.G.5
  • 29
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin MV, Svergun DI (2001) Automated matching of high- and low-resolution structural models. J Appl Crystallogr 34:33-41.
    • (2001) J Appl Crystallogr , vol.34 , pp. 33-41
    • Kozin, M.V.1    Svergun, D.I.2
  • 30
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small angle scattering
    • Volkov VV, Svergun DI (2003) Uniqueness of ab initio shape determination in small angle scattering. J Appl Crystallogr 36:860-864.
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 31
    • 34247891557 scopus 로고    scopus 로고
    • Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering
    • Bernado P, Mylonas E, Petoukhov MV, Blackledge M, Svergun DI (2007) Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering. J Am Chem. Soc 129:5656-5664.
    • (2007) J Am Chem. Soc , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 32
    • 0029185933 scopus 로고
    • CRYSOL - A Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates
    • Svergun DI, Barberato C, Koch MHJ (1995) CRYSOL - a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates. J Appl Cryst 28:768-773.
    • (1995) J Appl Cryst , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 33
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J 78:1606-1619.
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 36
    • 84862222355 scopus 로고    scopus 로고
    • Publication guidelines for structural modeling of small-angle scattering data from biomolecules in solution
    • Jacques DA, Guss JM, Svergun DI, Trewhella J (2012) Publication guidelines for structural modeling of small-angle scattering data from biomolecules in solution. Acta Cryst D 68:620-626.
    • (2012) Acta Cryst D , vol.68 , pp. 620-626
    • Jacques, D.A.1    Guss, J.M.2    Svergun, D.I.3    Trewhella, J.4
  • 38
    • 0029861558 scopus 로고    scopus 로고
    • Effect of M1 Protein and Low pH on Nuclear Transport of Influenza Virus Ribonucleoproteins
    • Bui M, Whittaker G, Helenius A (1996) Effect of M1 Protein and Low pH on Nuclear Transport of Influenza Virus Ribonucleoproteins. J Virology 70:8391-8401.
    • (1996) J Virology , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 39
    • 0015456108 scopus 로고
    • Further investigation on the fine structure of influenza virus
    • Nermut MV (1972) Further investigation on the fine structure of influenza virus. J Gen Virol 17:317-331.
    • (1972) J Gen Virol , vol.17 , pp. 317-331
    • Nermut, M.V.1
  • 41
    • 0024443823 scopus 로고
    • Electron microscopy of the influenza virus submembranal structure
    • Ruigrok RWH, Calder LJ, Wharton SA (1989) Electron microscopy of the influenza virus submembranal structure. Virology 173:311-316.
    • (1989) Virology , vol.173 , pp. 311-316
    • Ruigrok, R.W.H.1    Calder, L.J.2    Wharton, S.A.3
  • 42
    • 0034468745 scopus 로고    scopus 로고
    • Influenza virus matrix protein is the major driving force in virus budding
    • Gomez-Puertas P, Albo C, Perez-Pastrana E, Vivo A, Portela A (2000) Influenza virus matrix protein is the major driving force in virus budding. J Virol 74:11538-11547.
    • (2000) J Virol , vol.74 , pp. 11538-11547
    • Gomez-Puertas, P.1    Albo, C.2    Perez-Pastrana, E.3    Vivo, A.4    Portela, A.5
  • 43
    • 0034972583 scopus 로고    scopus 로고
    • Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins
    • Latham T, Galarza JM (2001) Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins. J Virol 75:6154-6165.
    • (2001) J Virol , vol.75 , pp. 6154-6165
    • Latham, T.1    Galarza, J.M.2
  • 44
    • 34250792678 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles
    • Chen BJ, Leser GP, Morita E, Lamb RA (2007) Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles. J Virol 81:7111-7123.
    • (2007) J Virol , vol.81 , pp. 7111-7123
    • Chen, B.J.1    Leser, G.P.2    Morita, E.3    Lamb, R.A.4
  • 45
    • 77950789595 scopus 로고    scopus 로고
    • The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles
    • Wang D, Harmon A, Jin J, Francis DH, Christopher-Hennings J, et al (2010) The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles. J Virol 84:4673- 4681.
    • (2010) J Virol , vol.84 , pp. 4673-4681
    • Wang, D.1    Harmon, A.2    Jin, J.3    Francis, D.H.4    Christopher-Hennings, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.