메뉴 건너뛰기




Volumn 89, Issue 20, 2015, Pages 10294-10302

The structure of immature virus-like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; PROTEIN P10; PROTEINASE; UNCLASSIFIED DRUG; VIRAL PROTEASE; PEPTIDE HYDROLASE; RECOMBINANT PROTEIN; VIRUS PROTEIN;

EID: 84942155961     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01502-15     Document Type: Article
Times cited : (47)

References (47)
  • 1
    • 84875233720 scopus 로고    scopus 로고
    • HIV Gag polyprotein: processing and early viral particle assembly
    • Bell NM, Lever AM. 2013. HIV Gag polyprotein: processing and early viral particle assembly. Trends Microbiol 21:136-144. http://dx.doi.org/10.1016/j.tim.2012.11.006.
    • (2013) Trends Microbiol , vol.21 , pp. 136-144
    • Bell, N.M.1    Lever, A.M.2
  • 2
    • 84914176382 scopus 로고    scopus 로고
    • How HIV-1 Gag assembles in cells: putting together pieces of the puzzle
    • Lingappa JR, Reed JC, Tanaka M, Chutiraka K, Robinson BA. 2014. How HIV-1 Gag assembles in cells: putting together pieces of the puzzle. Virus Res 193:89-107. http://dx.doi.org/10.1016/j.virusres.2014.07.001.
    • (2014) Virus Res , vol.193 , pp. 89-107
    • Lingappa, J.R.1    Reed, J.C.2    Tanaka, M.3    Chutiraka, K.4    Robinson, B.A.5
  • 5
    • 0034681298 scopus 로고    scopus 로고
    • Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses
    • Campos-Olivas R, Newman JL, Summers MF. 2000. Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses. J Mol Biol 296:633-649. http://dx.doi.org/10.1006/jmbi.1999.3475.
    • (2000) J Mol Biol , vol.296 , pp. 633-649
    • Campos-Olivas, R.1    Newman, J.L.2    Summers, M.F.3
  • 6
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang C, Ndassa Y, Summers MF. 2002. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat Struct Biol 9:537-543.
    • (2002) Nat Struct Biol , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 9
    • 34247185183 scopus 로고    scopus 로고
    • Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells
    • Wright ER, Schooler JB, Ding JH, Kieffer C, Fillmore C, Sundquist WI, Grant JJ. 2007. Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells.EMBOJ 26:2218-2226. http://dx.doi.org/10.1038/sj.emboj.7601664.
    • (2007) EMBOJ , vol.26 , pp. 2218-2226
    • Wright, E.R.1    Schooler, J.B.2    Ding, J.H.3    Kieffer, C.4    Fillmore, C.5    Sundquist, W.I.6    Grant, J.J.7
  • 12
    • 2642607039 scopus 로고    scopus 로고
    • A putative α-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly
    • Accola MA, Höglund S, Göttlinger HG. 1998. A putative α-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly. J Virol 72:2072-2078.
    • (1998) J Virol , vol.72 , pp. 2072-2078
    • Accola, M.A.1    Höglund, S.2    Göttlinger, H.G.3
  • 14
    • 84924189026 scopus 로고    scopus 로고
    • Structure of the immature HIV-1 capsid in intact virus particles at 8.8 A resolution
    • Schur FK, Hagen WJ, Rumlova M, Ruml T, Muller B, Krausslich HG, Briggs JA. 2015. Structure of the immature HIV-1 capsid in intact virus particles at 8.8 A resolution. Nature 517:505-508. http://dx.doi.org/10.1038/nature13838.
    • (2015) Nature , vol.517 , pp. 505-508
    • Schur, F.K.1    Hagen, W.J.2    Rumlova, M.3    Ruml, T.4    Muller, B.5    Krausslich, H.G.6    Briggs, J.A.7
  • 15
    • 0035123571 scopus 로고    scopus 로고
    • Characterization of Rous sarcoma virus Gag particles assembled in vitro
    • Yu F, Joshi SM, Ma YM, Kingston RL, Simon MN, Vogt VM. 2001. Characterization of Rous sarcoma virus Gag particles assembled in vitro. J Virol 75:2753-2764. http://dx.doi.org/10.1128/JVI.75.6.2753-2764.2001.
    • (2001) J Virol , vol.75 , pp. 2753-2764
    • Yu, F.1    Joshi, S.M.2    Ma, Y.M.3    Kingston, R.L.4    Simon, M.N.5    Vogt, V.M.6
  • 16
    • 0030947591 scopus 로고    scopus 로고
    • In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles
    • Campbell S, Vogt VM. 1997. In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles. J Virol 71:4425-4435.
    • (1997) J Virol , vol.71 , pp. 4425-4435
    • Campbell, S.1    Vogt, V.M.2
  • 17
    • 84881194271 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals conserved and divergent features of Gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus
    • Briggs JAG, Johnson MC, Simon MN, Fuller SD, Vogt VM. 2006. Cryo-electron microscopy reveals conserved and divergent features of Gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus. J Mol Biol 355:157-168. http://dx.doi.org/10.1016/j.jmb.2005.10.025.
    • (2006) J Mol Biol , vol.355 , pp. 157-168
    • Briggs, J.A.G.1    Johnson, M.C.2    Simon, M.N.3    Fuller, S.D.4    Vogt, V.M.5
  • 18
    • 0033771218 scopus 로고    scopus 로고
    • Role of the Rous sarcoma virus p10 domain in shape determination of Gag virus-like particles assembled in vitro and within Escherichia coli
    • Joshi SM, Vogt VM. 2000. Role of the Rous sarcoma virus p10 domain in shape determination of Gag virus-like particles assembled in vitro and within Escherichia coli. J Virol 74:10260-10268. http://dx.doi.org/10.1128/JVI.74.21.10260-10268.2000.
    • (2000) J Virol , vol.74 , pp. 10260-10268
    • Joshi, S.M.1    Vogt, V.M.2
  • 19
    • 43249087612 scopus 로고    scopus 로고
    • A molecular switch required for retrovirus assembly participates in the hexagonal immature lattice
    • Phillips JM, Murray PS, Murray D, Vogt VM. 2008. A molecular switch required for retrovirus assembly participates in the hexagonal immature lattice. EMBO J 27:1411-1420. http://dx.doi.org/10.1038/emboj.2008.71.
    • (2008) EMBO J , vol.27 , pp. 1411-1420
    • Phillips, J.M.1    Murray, P.S.2    Murray, D.3    Vogt, V.M.4
  • 21
    • 0026013779 scopus 로고
    • Amino acids encoded downstream of gag are not required by Rous sarcoma virus protease during gag-mediated assembly
    • Bennett RP, Rhee S, Craven RC, Hunter E, Wills JW. 1991. Amino acids encoded downstream of gag are not required by Rous sarcoma virus protease during gag-mediated assembly. J Virol 65:272-280.
    • (1991) J Virol , vol.65 , pp. 272-280
    • Bennett, R.P.1    Rhee, S.2    Craven, R.C.3    Hunter, E.4    Wills, J.W.5
  • 22
    • 0029166751 scopus 로고
    • Differential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses
    • Pepinsky RB, Papayannopoulos IA, Chow EP, Krishna NK, Craven RC, Vogt VM. 1995. Differential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses. J Virol 69:6430-6438.
    • (1995) J Virol , vol.69 , pp. 6430-6438
    • Pepinsky, R.B.1    Papayannopoulos, I.A.2    Chow, E.P.3    Krishna, N.K.4    Craven, R.C.5    Vogt, V.M.6
  • 23
    • 0030419901 scopus 로고    scopus 로고
    • Proteolytic processing and particle maturation
    • Kräusslich H-G (ed), Springer, Berlin, Germany
    • Vogt VM. 1996. Proteolytic processing and particle maturation, p 95-131. In Kräusslich H-G (ed), Morphogenesis and maturation of retroviruses, vol 214. Springer, Berlin, Germany.
    • (1996) Morphogenesis and maturation of retroviruses , vol.214 , pp. 95-131
    • Vogt, V.M.1
  • 24
    • 85016962662 scopus 로고    scopus 로고
    • In Vitro Assembly of Retroviruses
    • Bush DL, Vogt VM. 2014. In Vitro Assembly of Retroviruses. Annu Rev Virol 1:561-580. http://dx.doi.org/10.1146/annurev-virology-031413-085427.
    • (2014) Annu Rev Virol , vol.1 , pp. 561-580
    • Bush, D.L.1    Vogt, V.M.2
  • 25
    • 3543073550 scopus 로고    scopus 로고
    • SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins
    • Malakhov MP, Mattern MR, Malakhova OA, Drinker M, Weeks SD, Butt TR. 2004. SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins. J Struct Funct Genomics 5:75-86. http://dx.doi.org/10.1023/B:JSFG.0000029237.70316.52.
    • (2004) J Struct Funct Genomics , vol.5 , pp. 75-86
    • Malakhov, M.P.1    Mattern, M.R.2    Malakhova, O.A.3    Drinker, M.4    Weeks, S.D.5    Butt, T.R.6
  • 26
    • 0035027229 scopus 로고    scopus 로고
    • Importance of the N terminus of Rous sarcoma virus protease for structure and enzymatic function
    • Schatz GW, Reinking J, Zippin J, Nicholson LK, Vogt VM. 2001. Importance of the N terminus of Rous sarcoma virus protease for structure and enzymatic function. J Virol 75:4761-4770. http://dx.doi.org/10.1128/JVI.75.10.4761-4770.2001.
    • (2001) J Virol , vol.75 , pp. 4761-4770
    • Schatz, G.W.1    Reinking, J.2    Zippin, J.3    Nicholson, L.K.4    Vogt, V.M.5
  • 27
    • 84925250052 scopus 로고    scopus 로고
    • Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied byNMRspectroscopy
    • Deshmukh L, Ghirlando R, Clore GM. 2015. Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied byNMRspectroscopy. Proc Natl Acad SciUSA112:3374-3379. http://dx.doi.org/10.1073/pnas.1501985112.
    • (2015) Proc Natl Acad SciUSA , vol.112 , pp. 3374-3379
    • Deshmukh, L.1    Ghirlando, R.2    Clore, G.M.3
  • 28
    • 84888074636 scopus 로고    scopus 로고
    • Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging
    • Schur FK, Hagen WJ, de Marco A, Briggs JA. 2013. Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging. J Struct Biol 184:394-400. http://dx.doi.org/10.1016/j.jsb.2013.10.015.
    • (2013) J Struct Biol , vol.184 , pp. 394-400
    • Schur, F.K.1    Hagen, W.J.2    de Marco, A.3    Briggs, J.A.4
  • 29
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde DN. 2005. Automated electron microscope tomography using robust prediction of specimen movements. J Struct Biol 152:36-51. http://dx.doi.org/10.1016/j.jsb.2005.07.007.
    • (2005) J Struct Biol , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 30
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer JR, Mastronarde DN, McIntosh JR. 1996. Computer visualization of three-dimensional image data using IMOD. J Struct Biol 116:71-76. http://dx.doi.org/10.1006/jsbi.1996.0013.
    • (1996) J Struct Biol , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 31
    • 16344390563 scopus 로고    scopus 로고
    • Retrovirus envelope protein complex structure in situ studied by cryoelectron tomography
    • Forster F, Medalia O, Zauberman N, Baumeister W, Fass D. 2005. Retrovirus envelope protein complex structure in situ studied by cryoelectron tomography. Proc Natl Acad Sci U S A 102:4729-4734. http://dx.doi.org/10.1073/pnas.0409178102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4729-4734
    • Forster, F.1    Medalia, O.2    Zauberman, N.3    Baumeister, W.4    Fass, D.5
  • 33
    • 84860574289 scopus 로고    scopus 로고
    • Dynamo: a flexible, user-friendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments
    • Castano-Diez D, Kudryashev M, Arheit M, Stahlberg H. 2012. Dynamo: a flexible, user-friendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments. J Struct Biol 178:139-151. http://dx.doi.org/10.1016/j.jsb.2011.12.017.
    • (2012) J Struct Biol , vol.178 , pp. 139-151
    • Castano-Diez, D.1    Kudryashev, M.2    Arheit, M.3    Stahlberg, H.4
  • 34
    • 51549110953 scopus 로고    scopus 로고
    • A visualization and segmentation toolbox for electron microscopy
    • Pruggnaller S, Mayr M, Frangakis AS. 2008. A visualization and segmentation toolbox for electron microscopy. J Struct Biol 164:161-165. http://dx.doi.org/10.1016/j.jsb.2008.05.003.
    • (2008) J Struct Biol , vol.164 , pp. 161-165
    • Pruggnaller, S.1    Mayr, M.2    Frangakis, A.S.3
  • 35
    • 70350217328 scopus 로고    scopus 로고
    • CTF determination and correction for low dose tomographic tilt series
    • Xiong Q, Morphew MK, Schwartz CL, Hoenger AH, Mastronarde DN. 2009. CTF determination and correction for low dose tomographic tilt series. J Struct Biol 168:378-387. http://dx.doi.org/10.1016/j.jsb.2009.08.016.
    • (2009) J Struct Biol , vol.168 , pp. 378-387
    • Xiong, Q.1    Morphew, M.K.2    Schwartz, C.L.3    Hoenger, A.H.4    Mastronarde, D.N.5
  • 36
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R. 2003. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333:721-745. http://dx.doi.org/10.1016/j.jmb.2003.07.013.
    • (2003) J Mol Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 38
    • 65149095269 scopus 로고    scopus 로고
    • Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly
    • Bailey GD, Hyun JK, Mitra AK, Kingston RL. 2009. Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly. Structure 17:737-748. http://dx.doi.org/10.1016/j.str.2009.03.010.
    • (2009) Structure , vol.17 , pp. 737-748
    • Bailey, G.D.1    Hyun, J.K.2    Mitra, A.K.3    Kingston, R.L.4
  • 39
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132. http://dx.doi.org/10.1107/S0907444904019158.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 40
    • 70349267547 scopus 로고    scopus 로고
    • Molecular dynamics flexible fitting: a practical guide to combine cryoelectron microscopy and X-ray crystallography
    • Trabuco LG, Villa E, Schreiner E, Harrison CB, Schulten K. 2009. Molecular dynamics flexible fitting: a practical guide to combine cryoelectron microscopy and X-ray crystallography. Methods 49:174-180. http://dx.doi.org/10.1016/j.ymeth.2009.04.005.
    • (2009) Methods , vol.49 , pp. 174-180
    • Trabuco, L.G.1    Villa, E.2    Schreiner, E.3    Harrison, C.B.4    Schulten, K.5
  • 42
    • 80051713783 scopus 로고    scopus 로고
    • The molecular architecture of HIV
    • Briggs JA, Krausslich HG. 2011. The molecular architecture of HIV. J Mol Biol 410:491-500. http://dx.doi.org/10.1016/j.jmb.2011.04.021.
    • (2011) J Mol Biol , vol.410 , pp. 491-500
    • Briggs, J.A.1    Krausslich, H.G.2
  • 43
    • 84938740418 scopus 로고    scopus 로고
    • Atomic modeling of an immature retroviral lattice using molecular dynamics and mutagenesis
    • Goh BC, Perilla JR, England MR, Heyrana KJ, Craven RC, Schulten K. 2015. Atomic modeling of an immature retroviral lattice using molecular dynamics and mutagenesis. Structure http://dx.doi.org/10.1016/j.str.2015 .05.017.
    • (2015) Structure
    • Goh, B.C.1    Perilla, J.R.2    England, M.R.3    Heyrana, K.J.4    Craven, R.C.5    Schulten, K.6
  • 44
    • 47049101458 scopus 로고    scopus 로고
    • Mutations in the spacer peptide and adjoining sequences in Rous sarcoma virus Gag lead to tubular budding
    • Keller PW, Johnson MC, Vogt VM. 2008. Mutations in the spacer peptide and adjoining sequences in Rous sarcoma virus Gag lead to tubular budding. J Virol 82:6788-6797. http://dx.doi.org/10.1128/JVI.00213-08.
    • (2008) J Virol , vol.82 , pp. 6788-6797
    • Keller, P.W.1    Johnson, M.C.2    Vogt, V.M.3
  • 45
    • 84899058295 scopus 로고    scopus 로고
    • Higher-order structure of the Rous sarcoma virus SP assembly domain
    • Bush DL, Monroe EB, Bedwell GJ, Prevelige PE, Jr, Phillips JM, Vogt VM. 2014. Higher-order structure of the Rous sarcoma virus SP assembly domain. J Virol 88:5617-5629. http://dx.doi.org/10.1128/JVI.02659-13.
    • (2014) J Virol , vol.88 , pp. 5617-5629
    • Bush, D.L.1    Monroe, E.B.2    Bedwell, G.J.3    Prevelige, P.E.4    Phillips, J.M.5    Vogt, V.M.6
  • 46
    • 84857658242 scopus 로고    scopus 로고
    • A structural model for the generation of continuous curvature on the surface of a retroviral capsid
    • Bailey GD, Hyun JK, Mitra AK, Kingston RL. 2012. A structural model for the generation of continuous curvature on the surface of a retroviral capsid. J Mol Biol 417:212-223. http://dx.doi.org/10.1016/j.jmb.2012.01.014.
    • (2012) J Mol Biol , vol.417 , pp. 212-223
    • Bailey, G.D.1    Hyun, J.K.2    Mitra, A.K.3    Kingston, R.L.4
  • 47
    • 59649084913 scopus 로고    scopus 로고
    • Visualization of a missing link in retrovirus capsid assembly
    • Cardone G, Purdy JG, Cheng N, Craven RC, Steven AC. 2009. Visualization of a missing link in retrovirus capsid assembly. Nature 457:694-698. http://dx.doi.org/10.1038/nature07724.
    • (2009) Nature , vol.457 , pp. 694-698
    • Cardone, G.1    Purdy, J.G.2    Cheng, N.3    Craven, R.C.4    Steven, A.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.