Structure of an unliganded simian immunodeficiency virus gp120 core (original) (raw)

• Wyatt, R. & Sodroski, J. The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens. Science 280, 1884–1888 (1998)
  Article ADS CAS Google Scholar
• Allan, J. S. et al. Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III. Science 228, 1091–1094 (1985)
  Article ADS CAS Google Scholar
• Veronese, F. D. et al. Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene. Science 229, 1402–1405 (1985)
  Article ADS CAS Google Scholar
• Center, R. J. et al. Oligomeric structure of the human immunodeficiency virus type 1 envelope protein on the virion surface. J. Virol. 76, 7863–7867 (2002)
  Article CAS Google Scholar
• Dalgleish, A. G. et al. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 312, 763–767 (1984)
  Article ADS CAS Google Scholar
• Feng, Y., Broder, C. C., Kennedy, P. E. & Berger, E. A. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272, 872–877 (1996)
  Article ADS CAS Google Scholar
• Trkola, A. et al. CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5. Nature 384, 184–187 (1996)
  Article ADS CAS Google Scholar
• Wu, L. et al. CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5. Nature 384, 179–183 (1996)
  Article ADS CAS Google Scholar
• Sattentau, Q. J. & Moore, J. P. Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J. Exp. Med. 174, 407–415 (1991)
  Article CAS Google Scholar
• Sattentau, Q. J., Moore, J. P., Vignaux, F., Traincard, F. & Poignard, P. Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding. J. Virol. 67, 7383–7393 (1993)
  CAS PubMed PubMed Central Google Scholar
• Rizzuto, C. D. et al. A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding. Science 280, 1949–1953 (1998)
  Article ADS CAS Google Scholar
• Chan, D. C., Fass, D., Berger, J. M. & Kim, P. S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263–273 (1997)
  Article CAS Google Scholar
• Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J. & Wiley, D. C. Atomic structure of the ectodomain from HIV-1 gp41. Nature 387, 426–430 (1997)
  Article ADS CAS Google Scholar
• Kwong, P. D. et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648–659 (1998)
  Article ADS CAS Google Scholar
• Chan, D. C., Chutkowski, C. T. & Kim, P. S. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl Acad. Sci. USA 95, 15613–15617 (1998)
  Article ADS CAS Google Scholar
• Rimsky, L. T., Shugars, D. C. & Matthews, T. J. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72, 986–993 (1998)
  CAS PubMed PubMed Central Google Scholar
• Wyatt, R. et al. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 393, 705–711 (1998)
  Article ADS CAS Google Scholar
• Pollard, S. R., Meier, W., Chow, P., Rosa, J. J. & Wiley, D. C. CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion. Proc. Natl Acad. Sci. USA 88, 11320–11324 (1991)
  Article ADS CAS Google Scholar
• Wyatt, R. et al. Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions. J. Virol. 67, 4557–4565 (1993)
  CAS PubMed PubMed Central Google Scholar
• Rud, E. W. et al. in Vaccines 92: Modern Approaches to New Vaccines Including Prevention of AIDS (eds Brown, F., Chanock, R. M., Ginsberg, H. S. & Lerner, R. A.) 229–235 (Cold Spring Harbor Laboratory, New York, 1992)
  Google Scholar
• Chen, B., Vogan, E., Gong, H. Y., Wiley, D. C. & Harrison, S. C. Determining the structure of an unliganded and fully-glycosylated SIV gp120 envelope glycoprotein. Structure (Camb.) (in the press)
• Kwong, P. D. et al. Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1). J. Biol. Chem. 274, 4115–4123 (1999)
  Article CAS Google Scholar
• Thali, M. et al. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120–CD4 binding. J. Virol. 67, 3978–3988 (1993)
  CAS PubMed PubMed Central Google Scholar
• Lin, P. F. et al. A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor binding. Proc. Natl Acad. Sci. USA 100, 11013–11018 (2003)
  Article ADS CAS Google Scholar
• Moore, J. P. & Sodroski, J. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol. 70, 1863–1872 (1996)
  CAS PubMed PubMed Central Google Scholar
• Myszka, D. G. et al. Energetics of the HIV gp120–CD4 binding reaction. Proc. Natl Acad. Sci. USA 97, 9026–9031 (2000)
  Article ADS CAS Google Scholar
• Kwong, P. D. et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 420, 678–682 (2002)
  Article ADS CAS Google Scholar
• Burton, D. R. et al. Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 266, 1024–1027 (1994)
  Article ADS CAS Google Scholar
• Pantophlet, R. et al. Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120. J. Virol. 77, 642–658 (2003)
  Article CAS Google Scholar
• Etemad-Moghadam, B. et al. Characterization of simian-human immunodeficiency virus envelope glycoprotein epitopes recognized by neutralizing antibodies from infected monkeys. J. Virol. 72, 8437–8445 (1998)
  CAS PubMed PubMed Central Google Scholar
• Zwick, M. B. et al. A novel human antibody against human immunodeficiency virus type 1 gp120 is V1, V2, and V3 loop dependent and helps delimit the epitope of the broadly neutralizing antibody immunoglobulin G1 b12. J. Virol. 77, 6965–6978 (2003)
  Article CAS Google Scholar
• Guo, Q. et al. Biochemical and genetic characterizations of a novel human immunodeficiency virus type 1 inhibitor that blocks gp120–CD4 interactions. J. Virol. 77, 10528–10536 (2003)
  Article CAS Google Scholar
• Madani, N. et al. Localized changes in the gp120 envelope glycoprotein confer resistance to human immunodeficiency virus entry inhibitors BMS-806 and #155. J. Virol. 78, 3742–3752 (2004)
  Article CAS Google Scholar
• Ferrer, M. & Harrison, S. C. Peptide ligands to human immunodeficiency virus type 1 gp120 identified from phage display libraries. J. Virol. 73, 5795–5802 (1999)
  CAS PubMed PubMed Central Google Scholar
• Chen, B. et al. A chimeric protein of simian immunodeficiency virus envelope glycoprotein gp140 and Escherichia coli aspartate transcarbamoylase. J. Virol. 78, 4508–4516 (2004)
  Article CAS Google Scholar
• Moore, J. P., McKeating, J. A., Weiss, R. A. & Sattentau, Q. J. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250, 1139–1142 (1990)
  Article ADS CAS Google Scholar
• Pugach, P. et al. The prolonged culture of human immunodeficiency virus type 1 in primary lymphocytes increases its sensitivity to neutralization by soluble CD4. Virology 321, 8–22 (2004)
  Article CAS Google Scholar
• Puffer, B. A., Altamura, L. A., Pierson, T. C. & Doms, R. W. Determinants within gp120 and gp41 contribute to CD4 independence of SIV Envs. Virology 327, 16–25 (2004)
  Article CAS Google Scholar
• Kolchinsky, P., Kiprilov, E. & Sodroski, J. Increased neutralization sensitivity of CD4-independent human immunodeficiency virus variants. J. Virol. 75, 2041–2050 (2001)
  Article CAS Google Scholar
• Puffer, B. A. et al. CD4 independence of simian immunodeficiency virus Envs is associated with macrophage tropism, neutralization sensitivity, and attenuated pathogenicity. J. Virol. 76, 2595–2605 (2002)
  Article CAS Google Scholar
• Turner, S. et al. Resistance of primary isolates of human immunodeficiency virus type 1 to neutralization by soluble CD4 is not due to lower affinity with the viral envelope glycoprotein gp120. Proc. Natl Acad. Sci. USA 89, 1335–1339 (1992)
  Article ADS CAS Google Scholar
• Kwong, P. D., Wyatt, R., Sattentau, Q. J., Sodroski, J. & Hendrickson, W. A. Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus. J. Virol. 74, 1961–1972 (2000)
  Article CAS Google Scholar
• Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307–326 (1997)
  Article CAS Google Scholar
• Terwilliger, T. C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystallogr. D Biol. Crystallogr. 55, 849–861 (1999)
  Article CAS Google Scholar
• de la Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472–493 (1997)
  Article CAS Google Scholar
• Collaborative Computational Project, N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760–763 (1994)
  Article Google Scholar
• Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905–921 (1998)
  Article CAS Google Scholar
• Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110–119 (1991)
  Article Google Scholar
• McDonald, I. K. & Thornton, J. M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238, 777–793 (1994)
  Article CAS Google Scholar
• Wallace, A. C., Laskowski, R. A. & Thornton, J. M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127–134 (1995)
  Article CAS Google Scholar