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Volumn 9, Issue 4, 2014, Pages

Estimated secondary structure propensities within V1/V2 region of HIV gp120 are an important global antibody neutralization sensitivity determinant

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GLYCOPROTEIN GP 120; NEUTRALIZING ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; PEPTIDE FRAGMENT;

EID: 84899055507     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0094002     Document Type: Article
Times cited : (12)

References (47)
  • 4
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp 120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • DOI 10.1038/31405
    • Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, et al. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393: 648-659. (Pubitemid 28289647)
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 6
    • 0027194743 scopus 로고
    • Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions
    • Wyatt R, Sullivan N, Thali M, Repke H, Ho D, et al. (1993) Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions. J Virol 67: 4557-4565. (Pubitemid 23215934)
    • (1993) Journal of Virology , vol.67 , Issue.8 , pp. 4557-4565
    • Wyatt, R.1    Sullivan, N.2    Thali, M.3    Repke, H.4    Ho, D.5    Robinson, J.6    Posner, M.7    Sodroski, J.8
  • 8
    • 79959845498 scopus 로고    scopus 로고
    • Contribution of intrinsic reactivity of the HIV-1 envelope glycoproteins to CD4-independent infection and global inhibitor sensitivity
    • Haim H, Strack B, Kassa A, Madani N, Wang L, et al. (2011) Contribution of intrinsic reactivity of the HIV-1 envelope glycoproteins to CD4-independent infection and global inhibitor sensitivity. PLoS pathogens 7: e1002101.
    • (2011) PLoS Pathogens , vol.7
    • Haim, H.1    Strack, B.2    Kassa, A.3    Madani, N.4    Wang, L.5
  • 9
    • 77957940271 scopus 로고    scopus 로고
    • Mutation at a single position in the V2 domain of the HIV-1 envelope protein confers neutralization sensitivity to a highly neutralization-resistant virus
    • O'Rourke SM, Schweighardt B, Phung P, Fonseca DP, Terry K, et al. (2010) Mutation at a single position in the V2 domain of the HIV-1 envelope protein confers neutralization sensitivity to a highly neutralization-resistant virus. J Virol 84: 11200-11209.
    • (2010) J Virol , vol.84 , pp. 11200-11209
    • O'Rourke, S.M.1    Schweighardt, B.2    Phung, P.3    Fonseca, D.P.4    Terry, K.5
  • 10
    • 84869140656 scopus 로고    scopus 로고
    • Sequences in glycoprotein gp41, the CD4 binding site, and the V2 domain regulate sensitivity and resistance of HIV-1 to broadly neutralizing antibodies
    • O'Rourke SM, Schweighardt B, Phung P, Mesa KA, Vollrath AL, et al. (2012) Sequences in glycoprotein gp41, the CD4 binding site, and the V2 domain regulate sensitivity and resistance of HIV-1 to broadly neutralizing antibodies. J Virol 86: 12105-12114.
    • (2012) J Virol , vol.86 , pp. 12105-12114
    • O'Rourke, S.M.1    Schweighardt, B.2    Phung, P.3    Mesa, K.A.4    Vollrath, A.L.5
  • 11
    • 0031666180 scopus 로고    scopus 로고
    • An envelope modification that renders a primary, neutralization- resistant clade B human immunodeficiency virus type 1 isolate highly susceptible to neutralization by sera from other clades
    • Stamatatos L, Cheng-Mayer C (1998) An envelope modification that renders a primary, neutralization-resistant clade B human immunodeficiency virus type 1 isolate highly susceptible to neutralization by sera from other clades. J Virol 72: 7840-7845. (Pubitemid 28421774)
    • (1998) Journal of Virology , vol.72 , Issue.10 , pp. 7840-7845
    • Stamatatos, L.1    Cheng-Mayer, C.2
  • 12
    • 2342644898 scopus 로고    scopus 로고
    • The V1/V2 Domain of gp120 Is a Global Regulator of the Sensitivity of Primary Human Immunodeficiency Virus Type 1 Isolates to Neutralization by Antibodies Commonly Induced upon Infection
    • DOI 10.1128/JVI.78.10.5205-5215.2004
    • Pinter A, Honnen WJ, He Y, Gorny MK, Zolla-Pazner S, et al. (2004) The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection. J Virol 78: 5205-5215. (Pubitemid 38581472)
    • (2004) Journal of Virology , vol.78 , Issue.10 , pp. 5205-5215
    • Pinter, A.1    Honnen, W.J.2    He, Y.3    Gorny, M.K.4    Zolla-Pazner, S.5    Kayman, S.C.6
  • 13
    • 37848999666 scopus 로고    scopus 로고
    • The first hypervariable region of the gp120 Env glycoprotein defines the neutralizing susceptibility of heterologous human immunodeficiency virus type 1 isolates to neutralizing antibodies elicited by the SF162gp140 immunogen
    • Ching LK, Vlachogiannis G, Bosch KA, Stamatatos L (2008) The first hypervariable region of the gp120 Env glycoprotein defines the neutralizing susceptibility of heterologous human immunodeficiency virus type 1 isolates to neutralizing antibodies elicited by the SF162gp140 immunogen. J Virol 82: 949-956.
    • (2008) J Virol , vol.82 , pp. 949-956
    • Ching, L.K.1    Vlachogiannis, G.2    Bosch, K.A.3    Stamatatos, L.4
  • 14
    • 79960346105 scopus 로고    scopus 로고
    • Interaction of the gp120 V1V2 loop with a neighboring gp120 unit shields the HIV envelope trimer against cross-neutralizing antibodies
    • Rusert P, Krarup A, Magnus C, Brandenberg OF, Weber J, et al. (2011) Interaction of the gp120 V1V2 loop with a neighboring gp120 unit shields the HIV envelope trimer against cross-neutralizing antibodies. J Exp Med 208: 1419-1433.
    • (2011) J Exp Med , vol.208 , pp. 1419-1433
    • Rusert, P.1    Krarup, A.2    Magnus, C.3    Brandenberg, O.F.4    Weber, J.5
  • 15
    • 84055178652 scopus 로고    scopus 로고
    • Intraprotomer masking of third variable loop (V3) epitopes by the first and second variable loops (V1V2) within the native HIV-1 envelope glycoprotein trimer
    • Liu L, Cimbro R, Lusso P, Berger EA (2011) Intraprotomer masking of third variable loop (V3) epitopes by the first and second variable loops (V1V2) within the native HIV-1 envelope glycoprotein trimer. Proc Natl Acad Sci U S A 108: 20148-20153.
    • (2011) Proc Natl Acad Sci U S a , vol.108 , pp. 20148-20153
    • Liu, L.1    Cimbro, R.2    Lusso, P.3    Berger, E.A.4
  • 17
    • 0030812563 scopus 로고    scopus 로고
    • Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein
    • Cao J, Sullivan N, Desjardin E, Parolin C, Robinson J, et al. (1997) Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein. J Virol 71: 9808-9812. (Pubitemid 27492434)
    • (1997) Journal of Virology , vol.71 , Issue.12 , pp. 9808-9812
    • Cao, J.1    Sullivan, N.2    Desjardin, E.3    Parolin, C.4    Robinson, J.5    Wyatt, R.6    Sodroski, J.7
  • 18
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, Phogat SK, Chan-Hui PY, Wagner D, Phung P, et al. (2009) Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326: 285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1    Phogat, S.K.2    Chan-Hui, P.Y.3    Wagner, D.4    Phung, P.5
  • 19
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, Pancera M, Carrico C, Gorman J, Julien JP, et al. (2011) Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 480: 336-343.
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1    Pancera, M.2    Carrico, C.3    Gorman, J.4    Julien, J.P.5
  • 21
    • 84872809067 scopus 로고    scopus 로고
    • Vaccine induction of antibodies against a structurally heterogeneous site of immune pressure within HIV-1 envelope protein variable regions 1 and 2
    • Liao HX, Bonsignori M, Alam SM, McLellan JS, Tomaras GD, et al. (2013) Vaccine induction of antibodies against a structurally heterogeneous site of immune pressure within HIV-1 envelope protein variable regions 1 and 2. Immunity 38: 176-186.
    • (2013) Immunity , vol.38 , pp. 176-186
    • Liao, H.X.1    Bonsignori, M.2    Alam, S.M.3    McLellan, J.S.4    Tomaras, G.D.5
  • 22
    • 84875034460 scopus 로고    scopus 로고
    • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9
    • Julien JP, Lee JH, Cupo A, Murin CD, Derking R, et al. (2013) Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. Proc Natl Acad Sci U S A 110: 4351-4356.
    • (2013) Proc Natl Acad Sci U S a , vol.110 , pp. 4351-4356
    • Julien, J.P.1    Lee, J.H.2    Cupo, A.3    Murin, C.D.4    Derking, R.5
  • 23
    • 84880678141 scopus 로고    scopus 로고
    • Molecular architecture of the uncleaved HIV-1 envelope glycoprotein trimer
    • Mao Y, Wang L, Gu C, Herschhorn A, Desormeaux A, et al. (2013) Molecular architecture of the uncleaved HIV-1 envelope glycoprotein trimer. Proc Natl Acad Sci U S A 110: 12438-12443.
    • (2013) Proc Natl Acad Sci U S a , vol.110 , pp. 12438-12443
    • Mao, Y.1    Wang, L.2    Gu, C.3    Herschhorn, A.4    Desormeaux, A.5
  • 24
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien JP, Cupo A, Sok D, Stanfield RL, Lyumkis D, et al. (2013) Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 342: 1477-1483.
    • (2013) Science , vol.342 , pp. 1477-1483
    • Julien, J.P.1    Cupo, A.2    Sok, D.3    Stanfield, R.L.4    Lyumkis, D.5
  • 26
    • 84868589536 scopus 로고    scopus 로고
    • The Thai Phase III HIV Type 1 Vaccine trial (RV144) regimen induces antibodies that target conserved regions within the V2 loop of gp120
    • Karasavvas N, Billings E, Rao M, Williams C, Zolla-Pazner S, et al. (2012) The Thai Phase III HIV Type 1 Vaccine trial (RV144) regimen induces antibodies that target conserved regions within the V2 loop of gp120. AIDS research and human retroviruses 28: 1444-1457.
    • (2012) AIDS Research and Human Retroviruses , vol.28 , pp. 1444-1457
    • Karasavvas, N.1    Billings, E.2    Rao, M.3    Williams, C.4    Zolla-Pazner, S.5
  • 27
    • 84867653590 scopus 로고    scopus 로고
    • Increased HIV-1 vaccine efficacy against viruses with genetic signatures in Env V2
    • Rolland M, Edlefsen PT, Larsen BB, Tovanabutra S, Sanders-Buell E, et al. (2012) Increased HIV-1 vaccine efficacy against viruses with genetic signatures in Env V2. Nature 490: 417-420.
    • (2012) Nature , vol.490 , pp. 417-420
    • Rolland, M.1    Edlefsen, P.T.2    Larsen, B.B.3    Tovanabutra, S.4    Sanders-Buell, E.5
  • 28
    • 84880816240 scopus 로고    scopus 로고
    • Epitope mapping of conformational V2-specific anti-HIV human monoclonal antibodies reveals an immunodominant site in V2
    • Mayr LM, Cohen S, Spurrier B, Kong XP, Zolla-Pazner S (2013) Epitope mapping of conformational V2-specific anti-HIV human monoclonal antibodies reveals an immunodominant site in V2. PLoS ONE 8: e70859.
    • (2013) PLoS ONE , vol.8
    • Mayr, L.M.1    Cohen, S.2    Spurrier, B.3    Kong, X.P.4    Zolla-Pazner, S.5
  • 29
    • 84862173040 scopus 로고    scopus 로고
    • Monoclonal antibodies to the V2 domain of MN-rgp120: Fine mapping of epitopes and inhibition of alpha4beta7 binding
    • Nakamura GR, Fonseca DP, O'Rourke SM, Vollrath AL, Berman PW (2012) Monoclonal antibodies to the V2 domain of MN-rgp120: fine mapping of epitopes and inhibition of alpha4beta7 binding. PLoS ONE 7: e39045.
    • (2012) PLoS ONE , vol.7
    • Nakamura, G.R.1    Fonseca, D.P.2    O'Rourke, S.M.3    Vollrath, A.L.4    Berman, P.W.5
  • 30
    • 79952579682 scopus 로고    scopus 로고
    • Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop
    • Moore PL, Gray ES, Sheward D, Madiga M, Ranchobe N, et al. (2011) Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop. J Virol 85: 3128-3141.
    • (2011) J Virol , vol.85 , pp. 3128-3141
    • Moore, P.L.1    Gray, E.S.2    Sheward, D.3    Madiga, M.4    Ranchobe, N.5
  • 31
    • 0000181415 scopus 로고
    • The Influence of Amino Acid Side Chains on the Free Energy of Helix-Coil Transitions1
    • Nemethy G, Leach SJ, Scheraga HA (1966) The Influence of Amino Acid Side Chains on the Free Energy of Helix-Coil Transitions1. The Journal of Physical Chemistry 70: 998-1004.
    • (1966) The Journal of Physical Chemistry , vol.70 , pp. 998-1004
    • Nemethy, G.1    Leach, S.J.2    Scheraga, H.A.3
  • 32
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou PY, Fasman GD (1978) Empirical predictions of protein conformation. Annu Rev Biochem 47: 251-276.
    • (1978) Annu Rev Biochem , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 34
    • 0029865495 scopus 로고    scopus 로고
    • Analysis of thermodynamic determinants in helix propensities of nonpolar amino acids through a novel free energy calculation
    • DOI 10.1021/ja953347o
    • Wang J, Purisima EO (1996) Analysis of Thermodynamic Determinants in Helix Propensities of Nonpolar Amino Acids through a Novel Free Energy Calculation. Journal of the American Chemical Society 118: 995-1001. (Pubitemid 26074342)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.5 , pp. 995-1001
    • Wang, J.1    Purisima, E.O.2
  • 35
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz V, Serrano L (1995) Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J Mol Biol 245: 275-296.
    • (1995) J Mol Biol , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 36
    • 0028175780 scopus 로고
    • A thermodynamic scale for the beta-sheet forming tendencies of the amino acids
    • Smith CK, Withka JM, Regan L (1994) A thermodynamic scale for the beta-sheet forming tendencies of the amino acids. Biochemistry 33: 5510-5517.
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 37
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace CN, Scholtz JM (1998) A helix propensity scale based on experimental studies of peptides and proteins. Biophys J 75: 422-427. (Pubitemid 28311831)
    • (1998) Biophysical Journal , vol.75 , Issue.1 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 38
    • 73949127978 scopus 로고    scopus 로고
    • Tiered categorization of a diverse panel of HIV-1 Env pseudoviruses for assessment of neutralizing antibodies
    • Seaman MS, Janes H, Hawkins N, Grandpre LE, Devoy C, et al. (2010) Tiered categorization of a diverse panel of HIV-1 Env pseudoviruses for assessment of neutralizing antibodies. J Virol 84: 1439-1452.
    • (2010) J Virol , vol.84 , pp. 1439-1452
    • Seaman, M.S.1    Janes, H.2    Hawkins, N.3    Grandpre, L.E.4    Devoy, C.5
  • 41
    • 77958103698 scopus 로고    scopus 로고
    • Viral disorder or disordered viruses: Do viral proteins possess unique features?
    • Xue B, Williams RW, Oldfield CJ, Goh GK, Dunker AK, et al. (2010) Viral disorder or disordered viruses: do viral proteins possess unique features? Protein Pept Lett 17: 932-951.
    • (2010) Protein Pept Lett , vol.17 , pp. 932-951
    • Xue, B.1    Williams, R.W.2    Oldfield, C.J.3    Goh, G.K.4    Dunker, A.K.5
  • 42
    • 84860843718 scopus 로고    scopus 로고
    • Protein intrinsic disorder as a flexible armor and a weapon of HIV-1
    • Xue B, Mizianty MJ, Kurgan L, Uversky VN (2012) Protein intrinsic disorder as a flexible armor and a weapon of HIV-1. Cell Mol Life Sci 69: 1211-1259.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1211-1259
    • Xue, B.1    Mizianty, M.J.2    Kurgan, L.3    Uversky, V.N.4
  • 43
    • 33745796735 scopus 로고    scopus 로고
    • Factors determining the breadth and potency of neutralization by V3-specific human monoclonal antibodies derived from subjects infected with clade A or clade B strains of human immunodeficiency virus type 1
    • DOI 10.1128/JVI.02619-05
    • Krachmarov CP, Honnen WJ, Kayman SC, Gorny MK, Zolla-Pazner S, et al. (2006) Factors determining the breadth and potency of neutralization by V3-specific human monoclonal antibodies derived from subjects infected with clade A or clade B strains of human immunodeficiency virus type 1. J Virol 80: 7127-7135. (Pubitemid 44025209)
    • (2006) Journal of Virology , vol.80 , Issue.14 , pp. 7127-7135
    • Krachmarov, C.P.1    Honnen, W.J.2    Kayman, S.C.3    Gorny, M.K.4    Zolla-Pazner, S.5    Pinter, A.6


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