메뉴 건너뛰기




Volumn 517, Issue 7535, 2015, Pages 505-508

Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; CAPSID PROTEIN;

EID: 84924189026     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13838     Document Type: Article
Times cited : (244)

References (46)
  • 2
    • 84863982480 scopus 로고    scopus 로고
    • Structure of the immature retroviral capsid at 8A resolution by cryo-electron microscopy
    • Bharat, T. A. et al. Structure of the immature retroviral capsid at 8A resolution by cryo-electron microscopy. Nature 487, 385-389 (2012).
    • (2012) Nature , vol.487 , pp. 385-389
    • Bharat, T.A.1
  • 3
    • 84875233720 scopus 로고    scopus 로고
    • HIV Gag polyprotein: Processing and early viral particle assembly
    • Bell, N. M. & Lever, A. M. HIV Gag polyprotein: processing and early viral particle assembly. Trends Microbiol. 21, 136-144 (2013).
    • (2013) Trends Microbiol. , vol.21 , pp. 136-144
    • Bell, N.M.1    Lever, A.M.2
  • 4
    • 67650482702 scopus 로고    scopus 로고
    • Structure and assembly ofimmature HIV
    • Briggs, J. A. et al. Structure and assembly ofimmature HIV. Proc.Natl Acad. Sci.USA 106, 11090-11095 (2009).
    • (2009) Proc.Natl Acad. Sci.USA , vol.106 , pp. 11090-11095
    • Briggs, J.A.1
  • 5
    • 80051713783 scopus 로고    scopus 로고
    • The molecular architecture of HIV
    • Briggs, J. A. & Krausslich, H. G. The molecular architecture of HIV. J. Mol. Biol. 410, 491-500 (2011).
    • (2011) J. Mol. Biol. , vol.410 , pp. 491-500
    • Briggs, J.A.1    Krausslich, H.G.2
  • 6
    • 84878381053 scopus 로고    scopus 로고
    • Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics
    • Zhao, G. et al. Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. Nature 497, 643-646 (2013).
    • (2013) Nature , vol.497 , pp. 643-646
    • Zhao, G.1
  • 7
    • 84901846907 scopus 로고    scopus 로고
    • Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly
    • Bharat, T. A. et al. Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly. Proc. Natl Acad. Sci. USA 111, 8233-8238 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 8233-8238
    • Bharat, T.A.1
  • 8
    • 84878527131 scopus 로고    scopus 로고
    • Structural biology in situ-The potential of subtomogram averaging
    • Briggs, J. A. Structural biology in situ-the potential of subtomogram averaging. Curr. Opin. Struct. Biol. 23, 261-267 (2013).
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 261-267
    • Briggs, J.A.1
  • 9
    • 34247185183 scopus 로고    scopus 로고
    • Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells
    • Wright, E. R. et al. Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J. 26, 2218-2226 (2007).
    • (2007) EMBO J. , vol.26 , pp. 2218-2226
    • Wright, E.R.1
  • 10
    • 84888074636 scopus 로고    scopus 로고
    • Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging
    • Schur, F. K., Hagen, W. J., de Marco, A. & Briggs, J. A. Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging. J. Struct. Biol. 184, 394-400 (2013).
    • (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
  • 11
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • Fuller, S. D., Wilk, T., Gowen, B. E., Krasslich, H.-G. & Vogt, V. M. Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Curr. Biol. 7, 729-738 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Krasslich, H.-G.4    Vogt, V.M.5
  • 12
    • 2642607039 scopus 로고    scopus 로고
    • Putative a-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 gag precursor is crucial for viral particle assembly
    • Accola, M. A., Hoglund, S. & Gottlinger, H. G. A. Putative a-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).
    • (1998) J. Virol. , vol.72 , pp. 2072-2078
    • Accola, M.A.1    Hoglund, S.2    Gottlinger, H.G.A.3
  • 13
    • 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, M. F. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nature Struct. Biol. 9, 537-543 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 14
    • 57649116079 scopus 로고    scopus 로고
    • Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein
    • Bartonova, V. et al. Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein. J. Biol. Chem. 283, 32024-32033 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 32024-32033
    • Bartonova, V.1
  • 15
    • 70349267547 scopus 로고    scopus 로고
    • Molecular dynamics flexible fitting: A practical guide to combine cryo-electron microscopy and X-ray crystallography
    • Trabuco, L. G., Villa, E., Schreiner, E., Harrison, C. B. & Schulten, K. Molecular dynamics flexible fitting: a practical guide to combine cryo-electron microscopy and X-ray crystallography. Methods 49, 174-180 (2009).
    • (2009) Methods , vol.49 , pp. 174-180
    • Trabuco, L.G.1    Villa, E.2    Schreiner, E.3    Harrison, C.B.4    Schulten, K.5
  • 16
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler, U. K., Stray, K. M.,Garrus, J. E., Sundquist, W. I. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77, 5439-5450 (2003).
    • (2003) J. Virol. , vol.77 , pp. 5439-5450
    • Von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 17
    • 33749356701 scopus 로고    scopus 로고
    • Mutations in the a-helix directly C-terminal to the major homology region of human immunodeficiency virus type 1 capsid protein disrupt gag multimerization and markedly impair virus particle production
    • Chu, H.-H., Chang, Y.-F., Wang, C.-T.Mutations in the a-helix directly C-terminal to the major homology region of human immunodeficiency virus type 1 capsid protein disrupt gag multimerization and markedly impair virus particle production. J. Biomed. Sci. 13, 645-656 (2006).
    • (2006) J. Biomed. Sci. , vol.13 , pp. 645-656
    • Chu, H.-H.1    Chang, Y.-F.2    Wang, C.-T.3
  • 18
    • 0028342554 scopus 로고
    • Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis
    • Mammano, F., Ohagen, A., Hoglund, S. & Gottlinger, H. G. Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis. J. Virol. 68, 4927-4936 (1994).
    • (1994) J. Virol. , vol.68 , pp. 4927-4936
    • Mammano, F.1    Ohagen, A.2    Hoglund, S.3    Gottlinger, H.G.4
  • 19
    • 67549109069 scopus 로고    scopus 로고
    • X-ray structures of the hexameric building block of the HIV capsid
    • Pornillos, O. et al. X-ray structures of the hexameric building block of the HIV capsid. Cell 137, 1282-1292 (2009).
    • (2009) Cell , vol.137 , pp. 1282-1292
    • Pornillos, O.1
  • 20
    • 78149417909 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange analysis of HIV-1 capsid assembly and maturation
    • Monroe, E. B., Kang, S., Kyere, S. K., Li, R.& Prevelige, P. E., Jr. Hydrogen/deuterium exchange analysis of HIV-1 capsid assembly and maturation. Structure 18, 1483-1491 (2010).
    • (2010) Structure , vol.18 , pp. 1483-1491
    • Monroe, E.B.1    Kang, S.2    Kyere, S.K.3    Li, R.4    Prevelige, Jr.P.E.5
  • 21
    • 0031680643 scopus 로고    scopus 로고
    • The C-terminal half of the human immunodeficiency virus type 1 gag precursor is sufficient for efficient particle assembly
    • Borsetti, A.,Ohagen,A . & Gotlinger, H. G. The C-terminal half of the human immunodeficiency virus type 1 gag precursor is sufficient for efficient particle assembly. J. Virol. 72, 9313-9317 (1998).
    • (1998) J. Virol. , vol.72 , pp. 9313-9317
    • Borsetti, A.1    Ohagen, A.2    Gotlinger, H.G.3
  • 22
    • 0032536896 scopus 로고    scopus 로고
    • Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly
    • von Schwedler, U. K. et al. Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly. EMBO J. 17, 1555-1568 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1555-1568
    • Von Schwedler, U.K.1
  • 23
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke, E. K., Yuan, H. E. H. & Luban, J. Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372, 359-362 (1994).
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 24
    • 0014834551 scopus 로고
    • A new virus in a spontaneous mammary tumor of a rhesus monkey
    • Chopra, H. C. & Mason, M. M. A new virus in a spontaneous mammary tumor of a rhesus monkey. Cancer Res. 30, 2081-2086 (1970).
    • (1970) Cancer Res. , vol.30 , pp. 2081-2086
    • Chopra, H.C.1    Mason, M.M.2
  • 25
  • 26
    • 1842737708 scopus 로고    scopus 로고
    • Mutation of the major 59 splice site renders a CMV-driven HIV-1 proviral clone Tat-dependent: Connections between transcription and splicing
    • Bohne, J. & Krasslich, H.-G. Mutation of the major 59 splice site renders a CMV-driven HIV-1 proviral clone Tat-dependent: connections between transcription and splicing. FEBS Lett. 563, 113-118 (2004).
    • (2004) FEBS Lett. , vol.563 , pp. 113-118
    • Bohne, J.1    Krasslich, H.-G.2
  • 27
    • 0033947226 scopus 로고    scopus 로고
    • Amprenavir: A new human immunodeficiency virus type 1 protease inhibitor
    • Fung, H. B., Kirschenbaum, H. L. & Hameed, R. Amprenavir: a new human immunodeficiency virus type 1 protease inhibitor. Clin. Ther. 22, 549-572 (2000).
    • (2000) Clin. Ther. , vol.22 , pp. 549-572
    • Fung, H.B.1    Kirschenbaum, H.L.2    Hameed, R.3
  • 28
    • 0032935035 scopus 로고    scopus 로고
    • Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions
    • Dettenhofer, M. & Yu, X.-F. Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions. J. Virol. 73, 1460-1467 (1999).
    • (1999) J. Virol. , vol.73 , pp. 1460-1467
    • Dettenhofer, M.1    Yu, X.-F.2
  • 29
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36-51 (2005).
    • (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, J. R., Mastronarde, D. N. & McIntosh, J. R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116, 71-76 (1996).
    • (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 cryo-electron tomography
    • Forster, F., Medalia, O., Zauberman, N., Baumeister, W. & Fass, D. Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography. Proc. Natl Acad. Sci. USA 102, 4729-4734 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4729-4734
    • Forster, F.1    Medalia, O.2    Zauberman, N.3    Baumeister, W.4    Fass, D.5
  • 32
    • 13844264476 scopus 로고    scopus 로고
    • TOM software toolbox: Acquisition and analysis for electron tomography
    • Nickell, S. et al. TOM software toolbox: acquisition and analysis for electron tomography. J. Struct. Biol. 149, 227-234 (2005).
    • (2005) J. Struct. Biol. , vol.149 , pp. 227-234
    • Nickell, S.1
  • 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. 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 (2012).
    • (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, A. S. A visualization and segmentation toolbox for electron microscopy. J. Struct. Biol. 164, 161-165 (2008).
    • (2008) J. Struct. Biol. , vol.164 , pp. 161-165
    • Pruggnaller, S.1    Mayr, M.2    Frangakis, A.S.3
  • 36
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J.Mol. Biol. 333, 721-745 (2003).
    • (2003) J.Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 37
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 38
    • 13244256815 scopus 로고    scopus 로고
    • Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: Implications for particle assembly and RNA packaging
    • Morellet, N., Druillennec, S., Lenoir, C., Bouaziz, S. & Roques, B. P. Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging. Protein Sci. 14, 375-386 (2005).
    • (2005) Protein Sci. , vol.14 , pp. 375-386
    • Morellet, N.1    Druillennec, S.2    Lenoir, C.3    Bouaziz, S.4    Roques, B.P.5
  • 39
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips, J. C. et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26, 1781-1802 (2005).
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 40
    • 68949177099 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of capsid protein fromthe Mason-Pfizer monkey virus
    • Macek, P. et al.NMR structure of the N-terminal domain of capsid protein fromthe Mason-Pfizer monkey virus. J. Mol. Biol. 392, 100-114 (2009).
    • (2009) J. Mol. Biol. , vol.392 , pp. 100-114
    • MacEk, P.1
  • 41
    • 84870664162 scopus 로고    scopus 로고
    • Role of the SP2 domain and its proteolytic cleavage in HIV-1 structural maturation and infectivity
    • de Marco, A. et al. Role of the SP2 domain and its proteolytic cleavage in HIV-1 structural maturation and infectivity. J. Virol. 86, 13708-13716 (2012).
    • (2012) J. Virol. , vol.86 , pp. 13708-13716
    • De Marco, A.1
  • 42
    • 0034659842 scopus 로고    scopus 로고
    • Structure and self-association of the Rous sarcoma virus capsid protein
    • Kingston, R. L. et al. Structure and self-association of the Rous sarcoma virus capsid protein. Structure 8, 617-628 (2000).
    • (2000) Structure , vol.8 , pp. 617-628
    • Kingston, R.L.1
  • 43
    • 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, J. L. & Summers, M. F. 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 (2000).
    • (2000) J. Mol. Biol. , vol.296 , pp. 633-649
    • Campos-Olivas, R.1    Newman, J.L.2    Summers, M.F.3
  • 44
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retroviral capsid hexameric amino-terminal domain
    • Mortuza, G. B. et al. High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 431, 481-485 (2004).
    • (2004) Nature , vol.431 , pp. 481-485
    • Mortuza, G.B.1
  • 45
    • 0035793720 scopus 로고    scopus 로고
    • Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein
    • Cornilescu, C. C., Bouamr, F., Yao, X., Carter, C. & Tjandra, N. Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein. J. Mol. Biol. 306, 783-797 (2001).
    • (2001) J. Mol. Biol. , vol.306 , pp. 783-797
    • Cornilescu, C.C.1    Bouamr, F.2    Yao, X.3    Carter, C.4    Tjandra, N.5
  • 46
    • 0033055277 scopus 로고    scopus 로고
    • Sequence-specific 1H, 13C and 15N chemical shift assignment and secondary structure of the HTLV-I capsid protein
    • Khorasanizadeh, S., Campos-Olivas, R., Clark, C., Summers, M. Sequence-specific 1H, 13C and 15N chemical shift assignment and secondary structure of the HTLV-I capsid protein. J. Biomol. NMR 14, 199-200 (1999).
    • (1999) J. Biomol. NMR , vol.14 , pp. 199-200
    • Khorasanizadeh, S.1    Campos-Olivas, R.2    Clark, C.3    Summers, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.