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Volumn 91, Issue 10, 2017, Pages

Conformational states of a soluble, uncleaved HIV-1 envelope trimer

Author keywords

cryoEM; Envelope; Human immunodeficiency virus; Immunogen

Indexed keywords

ARTICLE; CRYOELECTRON MICROSCOPY; GEL FILTRATION CHROMATOGRAPHY; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SEQUENCE ALIGNMENT; SURFACE PLASMON RESONANCE; VACCINE PRODUCTION; VIRUS MORPHOLOGY; CHEMISTRY; CONFORMATION; GENETICS; IMMUNOLOGY; METABOLISM; PROTEIN DEGRADATION; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; SOLUBILITY;

EID: 85018259958     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00175-17     Document Type: Article
Times cited : (13)

References (34)
  • 1
    • 26944466459 scopus 로고    scopus 로고
    • Mechanism of membrane fusion by viral envelope proteins
    • Harrison SC. 2005. Mechanism of membrane fusion by viral envelope proteins. Adv Virus Res 64:231-259. https://doi.org/10.1016/S0065-3527(05)64007-9.
    • (2005) Adv Virus Res , vol.64 , pp. 231-259
    • Harrison, S.C.1
  • 2
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273. https://doi.org/10.1016/ S0092-8674(00)80205-6.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 5
    • 84937544544 scopus 로고    scopus 로고
    • HIV-1 envelope. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein
    • Chen J, Kovacs JM, Peng H, Rits-Volloch S, Lu J, Park D, Zablowsky E, Seaman MS, Chen B. 2015. HIV-1 envelope. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein. Science 349:191-195. https://doi.org/10.1126/science.aaa9804.
    • (2015) Science , vol.349 , pp. 191-195
    • Chen, J.1    Kovacs, J.M.2    Peng, H.3    Rits-Volloch, S.4    Lu, J.5    Park, D.6    Zablowsky, E.7    Seaman, M.S.8    Chen, B.9
  • 11
    • 84961231130 scopus 로고    scopus 로고
    • Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
    • Lee JH, Ozorowski G, Ward AB. 2016. Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer. Science 351:1043-1048. https://doi.org/10.1126/science.aad2450.
    • (2016) Science , vol.351 , pp. 1043-1048
    • Lee, J.H.1    Ozorowski, G.2    Ward, A.B.3
  • 14
    • 1242338175 scopus 로고    scopus 로고
    • Expression and characterisation of recombinant oligomeric envelope glycoproteins derived from primary isolates of HIV-1
    • Jeffs SA, Goriup S, Kebble B, Crane D, Bolgiano B, Sattentau Q, Jones S, Holmes H. 2004. Expression and characterisation of recombinant oligomeric envelope glycoproteins derived from primary isolates of HIV-1. Vaccine 22:1032-1046. https://doi.org/10.1016/j.vaccine.2003.08.042.
    • (2004) Vaccine , vol.22 , pp. 1032-1046
    • Jeffs, S.A.1    Goriup, S.2    Kebble, B.3    Crane, D.4    Bolgiano, B.5    Sattentau, Q.6    Jones, S.7    Holmes, H.8
  • 16
    • 84941363719 scopus 로고    scopus 로고
    • Broadly neutralizing antibody 8ANC195 recognizes closed and open states of HIV-1 Env
    • Scharf L, Wang H, Gao H, Chen S, McDowall AW, Bjorkman PJ. 2015. Broadly neutralizing antibody 8ANC195 recognizes closed and open states of HIV-1 Env. Cell 162:1379-1390. https://doi.org/10.1016/j.cell .2015.08.035.
    • (2015) Cell , vol.162 , pp. 1379-1390
    • Scharf, L.1    Wang, H.2    Gao, H.3    Chen, S.4    McDowall, A.W.5    Bjorkman, P.J.6
  • 17
    • 84923154103 scopus 로고    scopus 로고
    • Stable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure
    • Kovacs JM, Noeldeke E, Ha HJ, Peng H, Rits-Volloch S, Harrison SC, Chen B. 2014. Stable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure. Proc Natl Acad Sci U S A 111:18542-18547. https://doi.org/10.1073/pnas.1422269112.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 18542-18547
    • Kovacs, J.M.1    Noeldeke, E.2    Ha, H.J.3    Peng, H.4    Rits-Volloch, S.5    Harrison, S.C.6    Chen, B.7
  • 18
    • 84928379119 scopus 로고    scopus 로고
    • A primer to singleparticle cryo-electron microscopy
    • Cheng Y, Grigorieff N, Penczek PA, Walz T. 2015. A primer to singleparticle cryo-electron microscopy. Cell 161:438-449. https://doi.org/10 .1016/j.cell.2015.03.050.
    • (2015) Cell , vol.161 , pp. 438-449
    • Cheng, Y.1    Grigorieff, N.2    Penczek, P.A.3    Walz, T.4
  • 19
    • 84868444740 scopus 로고    scopus 로고
    • RELION: implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SH. 2012. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180:519-530. https://doi .org/10.1016/j.jsb.2012.09.006.
    • (2012) J Struct Biol , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 20
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury PB, Zhang T, Kim PS, Alber T. 1993. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262:1401-1407. https://doi.org/10.1126/science.8248779.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 21
    • 0036178009 scopus 로고    scopus 로고
    • Domain organization, folding and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein
    • Boudko SP, Londer YY, Letarov AV, Sernova NV, Engel J, Mesyanzhinov VV. 2002. Domain organization, folding and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein. Eur J Biochem 269:833-841. https://doi.org/10.1046/j.1432-1033.2002.02734.x.
    • (2002) Eur J Biochem , vol.269 , pp. 833-841
    • Boudko, S.P.1    Londer, Y.Y.2    Letarov, A.V.3    Sernova, N.V.4    Engel, J.5    Mesyanzhinov, V.V.6
  • 22
    • 84974849211 scopus 로고    scopus 로고
    • Frealign: an exploratory tool for single-particle cryo-EM
    • Grigorieff N. 2016. Frealign: an exploratory tool for single-particle cryo-EM. Methods Enzymol 579:191-226. https://doi.org/10.1016/bs.mie.2016 .04.013.
    • (2016) Methods Enzymol , vol.579 , pp. 191-226
    • Grigorieff, N.1
  • 23
    • 51349162563 scopus 로고    scopus 로고
    • Molecular architecture of native HIV-1 gp120 trimers
    • Liu J, Bartesaghi A, Borgnia MJ, Sapiro G, Subramaniam S. 2008. Molecular architecture of native HIV-1 gp120 trimers. Nature 455:109-113. https://doi.org/10.1038/nature07159.
    • (2008) Nature , vol.455 , pp. 109-113
    • Liu, J.1    Bartesaghi, A.2    Borgnia, M.J.3    Sapiro, G.4    Subramaniam, S.5
  • 24
    • 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. https://doi.org/10.1038/289366a0.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 25
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC. 1998. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95:409-417. https://doi.org/10.1016/S0092-8674(00)81771-7.
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5    Wiley, D.C.6
  • 28
    • 41649090223 scopus 로고    scopus 로고
    • A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies
    • Frey G, Peng H, Rits-Volloch S, Morelli M, Cheng Y, Chen B. 2008. A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proc Natl Acad Sci U S A 105:3739-3744. https://doi.org/10 .1073/pnas.0800255105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3739-3744
    • Frey, G.1    Peng, H.2    Rits-Volloch, S.3    Morelli, M.4    Cheng, Y.5    Chen, B.6
  • 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. https://doi.org/10.1016/j.jsb.2005.07.007.
    • (2005) J Struct Biol , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 30
    • 84930634509 scopus 로고    scopus 로고
    • Measuring the optimal exposure for single particle cryo-EM using a 2.6 A reconstruction of rotavirus VP6
    • Grant T, Grigorieff N. 2015. Measuring the optimal exposure for single particle cryo-EM using a 2.6 A reconstruction of rotavirus VP6. eLife 4:e06980. https://doi.org/10.7554/eLife.06980.
    • (2015) ELife , vol.4
    • Grant, T.1    Grigorieff, N.2
  • 31
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: an extensible image processing suite for electron microscopy
    • Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, Rees I, Ludtke SJ. 2007. EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol 157:38-46. https://doi.org/10.1016/j.jsb.2006.05.009.
    • (2007) J Struct Biol , vol.157 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 32
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh TR, Gao H, Baxter WT, Asturias FJ, Boisset N, Leith A, Frank J. 2008. SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat Protoc 3:1941-1974. https://doi.org/10.1038/nprot.2008.156.
    • (2008) Nat Protoc , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1    Gao, H.2    Baxter, W.T.3    Asturias, F.J.4    Boisset, N.5    Leith, A.6    Frank, J.7
  • 34
    • 0031570687 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain
    • Tao Y, Strelkov SV, Mesyanzhinov VV, Rossmann MG. 1997. Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure 5:789-798. https://doi.org/10.1016/S0969-2126(97)00233-5.
    • (1997) Structure , vol.5 , pp. 789-798
    • Tao, Y.1    Strelkov, S.V.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.