메뉴 건너뛰기




Volumn 45, Issue 1, 2016, Pages 31-45

A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 160; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS GLYCOPROTEIN; CCR5 PROTEIN, HUMAN; CD4 ANTIGEN; GP120 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; PEPTIDE FRAGMENT; POLYSACCHARIDE; PROTEIN BINDING;

EID: 84990856306     PISSN: 10747613     EISSN: 10974180     Source Type: Journal    
DOI: 10.1016/j.immuni.2016.06.026     Document Type: Article
Times cited : (126)

References (73)
  • 1
    • 84947445736 scopus 로고    scopus 로고
    • Identification of common features in prototype broadly neutralizing antibodies to HIV envelope V2 apex to facilitate vaccine design
    • Andrabi, R., Voss, J.E., Liang, C.-H., Briney, B., McCoy, L.E., Wu, C.-Y., Wong, C.-H., Poignard, P., Burton, D.R., Identification of common features in prototype broadly neutralizing antibodies to HIV envelope V2 apex to facilitate vaccine design. Immunity 43 (2015), 959–973.
    • (2015) Immunity , vol.43 , pp. 959-973
    • Andrabi, R.1    Voss, J.E.2    Liang, C.-H.3    Briney, B.4    McCoy, L.E.5    Wu, C.-Y.6    Wong, C.-H.7    Poignard, P.8    Burton, D.R.9
  • 4
    • 80052938385 scopus 로고    scopus 로고
    • Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors
    • Bonsignori, M., Hwang, K.-K., Chen, X., Tsao, C.-Y., Morris, L., Gray, E., Marshall, D.J., Crump, J.A., Kapiga, S.H., Sam, N.E., et al. Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors. J. Virol. 85 (2011), 9998–10009.
    • (2011) J. Virol. , vol.85 , pp. 9998-10009
    • Bonsignori, M.1    Hwang, K.-K.2    Chen, X.3    Tsao, C.-Y.4    Morris, L.5    Gray, E.6    Marshall, D.J.7    Crump, J.A.8    Kapiga, S.H.9    Sam, N.E.10
  • 6
    • 84969835812 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies to HIV and their role in vaccine design
    • Burton, D.R., Hangartner, L., Broadly neutralizing antibodies to HIV and their role in vaccine design. Annu. Rev. Immunol. 34 (2016), 635–659.
    • (2016) Annu. Rev. Immunol. , vol.34 , pp. 635-659
    • Burton, D.R.1    Hangartner, L.2
  • 8
    • 0037471318 scopus 로고    scopus 로고
    • Conformational changes in env oligomer induced by an antibody dependent on the V3 loop base
    • Cavacini, L., Duval, M., Song, L., Sangster, R., Xiang, S.-H., Sodroski, J., Posner, M., Conformational changes in env oligomer induced by an antibody dependent on the V3 loop base. AIDS 17 (2003), 685–689.
    • (2003) AIDS , vol.17 , pp. 685-689
    • Cavacini, L.1    Duval, M.2    Song, L.3    Sangster, R.4    Xiang, S.-H.5    Sodroski, J.6    Posner, M.7
  • 9
    • 84869106867 scopus 로고    scopus 로고
    • Enhanced recognition and neutralization of HIV-1 by antibody-derived CCR5-mimetic peptide variants
    • Chiang, J.J., Gardner, M.R., Quinlan, B.D., Dorfman, T., Choe, H., Farzan, M., Enhanced recognition and neutralization of HIV-1 by antibody-derived CCR5-mimetic peptide variants. J. Virol. 86 (2012), 12417–12421.
    • (2012) J. Virol. , vol.86 , pp. 12417-12421
    • Chiang, J.J.1    Gardner, M.R.2    Quinlan, B.D.3    Dorfman, T.4    Choe, H.5    Farzan, M.6
  • 10
    • 0036333648 scopus 로고    scopus 로고
    • The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus type 1 envelope glycoprotein interactions with the CCR5 coreceptor
    • Cormier, E.G., Dragic, T., The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus type 1 envelope glycoprotein interactions with the CCR5 coreceptor. J. Virol. 76 (2002), 8953–8957.
    • (2002) J. Virol. , vol.76 , pp. 8953-8957
    • Cormier, E.G.1    Dragic, T.2
  • 11
    • 0035000023 scopus 로고    scopus 로고
    • Mapping the determinants of the CCR5 amino-terminal sulfopeptide interaction with soluble human immunodeficiency virus type 1 gp120-CD4 complexes
    • Cormier, E.G., Tran, D.N., Yukhayeva, L., Olson, W.C., Dragic, T., Mapping the determinants of the CCR5 amino-terminal sulfopeptide interaction with soluble human immunodeficiency virus type 1 gp120-CD4 complexes. J. Virol. 75 (2001), 5541–5549.
    • (2001) J. Virol. , vol.75 , pp. 5541-5549
    • Cormier, E.G.1    Tran, D.N.2    Yukhayeva, L.3    Olson, W.C.4    Dragic, T.5
  • 12
    • 84875551472 scopus 로고    scopus 로고
    • Broadly neutralizing antiviral antibodies
    • Corti, D., Lanzavecchia, A., Broadly neutralizing antiviral antibodies. Annu. Rev. Immunol. 31 (2013), 705–742.
    • (2013) Annu. Rev. Immunol. , vol.31 , pp. 705-742
    • Corti, D.1    Lanzavecchia, A.2
  • 14
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores, K.J., Burton, D.R., Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J. Virol. 84 (2010), 10510–10521.
    • (2010) J. Virol. , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 15
    • 33749410635 scopus 로고    scopus 로고
    • A tyrosine-sulfated peptide derived from the heavy-chain CDR3 region of an HIV-1-neutralizing antibody binds gp120 and inhibits HIV-1 infection
    • Dorfman, T., Moore, M.J., Guth, A.C., Choe, H., Farzan, M., A tyrosine-sulfated peptide derived from the heavy-chain CDR3 region of an HIV-1-neutralizing antibody binds gp120 and inhibits HIV-1 infection. J. Biol. Chem. 281 (2006), 28529–28535.
    • (2006) J. Biol. Chem. , vol.281 , pp. 28529-28535
    • Dorfman, T.1    Moore, M.J.2    Guth, A.C.3    Choe, H.4    Farzan, M.5
  • 18
    • 83755183801 scopus 로고    scopus 로고
    • The role of neutralizing antibodies in hepatitis C virus infection
    • Edwards, V.C., Tarr, A.W., Urbanowicz, R.A., Ball, J.K., The role of neutralizing antibodies in hepatitis C virus infection. J. Gen. Virol. 93 (2012), 1–19.
    • (2012) J. Gen. Virol. , vol.93 , pp. 1-19
    • Edwards, V.C.1    Tarr, A.W.2    Urbanowicz, R.A.3    Ball, J.K.4
  • 21
    • 84900517557 scopus 로고    scopus 로고
    • Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers
    • Falkowska, E., Le, K.M., Ramos, A., Doores, K.J., Lee, J.H., Blattner, C., Ramirez, A., Derking, R., van Gils, M.J., Liang, C.-H., et al. Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers. Immunity 40 (2014), 657–668.
    • (2014) Immunity , vol.40 , pp. 657-668
    • Falkowska, E.1    Le, K.M.2    Ramos, A.3    Doores, K.J.4    Lee, J.H.5    Blattner, C.6    Ramirez, A.7    Derking, R.8    van Gils, M.J.9    Liang, C.-H.10
  • 22
    • 0034700083 scopus 로고    scopus 로고
    • Hepatitis C virus lacking the hypervariable region 1 of the second envelope protein is infectious and causes acute resolving or persistent infection in chimpanzees
    • Forns, X., Thimme, R., Govindarajan, S., Emerson, S.U., Purcell, R.H., Chisari, F.V., Bukh, J., Hepatitis C virus lacking the hypervariable region 1 of the second envelope protein is infectious and causes acute resolving or persistent infection in chimpanzees. Proc. Natl. Acad. Sci. USA 97 (2000), 13318–13323.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13318-13323
    • Forns, X.1    Thimme, R.2    Govindarajan, S.3    Emerson, S.U.4    Purcell, R.H.5    Chisari, F.V.6    Bukh, J.7
  • 25
    • 79955389756 scopus 로고    scopus 로고
    • The neutralization breadth of HIV-1 develops incrementally over four years and is associated with CD4+ T cell decline and high viral load during acute infection
    • Gray, E.S., Madiga, M.C., Hermanus, T., Moore, P.L., Wibmer, C.K., Tumba, N.L., Werner, L., Mlisana, K., Sibeko, S., Williamson, C., et al., CAPRISA002 Study Team. The neutralization breadth of HIV-1 develops incrementally over four years and is associated with CD4+ T cell decline and high viral load during acute infection. J. Virol. 85 (2011), 4828–4840.
    • (2011) J. Virol. , vol.85 , pp. 4828-4840
    • Gray, E.S.1    Madiga, M.C.2    Hermanus, T.3    Moore, P.L.4    Wibmer, C.K.5    Tumba, N.L.6    Werner, L.7    Mlisana, K.8    Sibeko, S.9    Williamson, C.10
  • 26
    • 84860759632 scopus 로고    scopus 로고
    • B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study
    • Haynes, B.F., Kelsoe, G., Harrison, S.C., Kepler, T.B., Kepler, T.B., B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study. Nat. Biotechnol. 30 (2012), 423–433.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 423-433
    • Haynes, B.F.1    Kelsoe, G.2    Harrison, S.C.3    Kepler, T.B.4    Kepler, T.B.5
  • 32
    • 84878519611 scopus 로고    scopus 로고
    • Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans
    • Julien, J.-P., Sok, D., Khayat, R., Lee, J.H., Doores, K.J., Walker, L.M., Ramos, A., Diwanji, D.C., Pejchal, R., Cupo, A., et al. Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans. PLoS Pathog., 9, 2013, e1003342.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003342
    • Julien, J.-P.1    Sok, D.2    Khayat, R.3    Lee, J.H.4    Doores, K.J.5    Walker, L.M.6    Ramos, A.7    Diwanji, D.C.8    Pejchal, R.9    Cupo, A.10
  • 37
    • 0026753639 scopus 로고
    • Evolution of the V3 envelope domain in proviral sequences and isolates of human immunodeficiency virus type 1 during transition of the viral biological phenotype
    • Kuiken, C.L., de Jong, J.J., Baan, E., Keulen, W., Tersmette, M., Goudsmit, J., Evolution of the V3 envelope domain in proviral sequences and isolates of human immunodeficiency virus type 1 during transition of the viral biological phenotype. J. Virol. 66 (1992), 4622–4627.
    • (1992) J. Virol. , vol.66 , pp. 4622-4627
    • Kuiken, C.L.1    de Jong, J.J.2    Baan, E.3    Keulen, W.4    Tersmette, M.5    Goudsmit, J.6
  • 39
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P.D., Wyatt, R., Robinson, J., Sweet, R.W., Sodroski, J., Hendrickson, W.A., Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393 (1998), 648–659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 40
    • 82955241840 scopus 로고    scopus 로고
    • Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1
    • a007278–a007278
    • Kwong, P.D., Mascola, J.R., Nabel, G.J., Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1. Cold Spring Harb. Perspect. Med., 1, 2011 a007278–a007278.
    • (2011) Cold Spring Harb. Perspect. Med. , vol.1
    • Kwong, P.D.1    Mascola, J.R.2    Nabel, G.J.3
  • 42
    • 84921847141 scopus 로고    scopus 로고
    • Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies
    • Lee, P.S., Wilson, I.A., Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies. Curr. Top. Microbiol. Immunol. 386 (2015), 323–341.
    • (2015) Curr. Top. Microbiol. Immunol. , vol.386 , pp. 323-341
    • Lee, P.S.1    Wilson, I.A.2
  • 43
    • 84961231130 scopus 로고    scopus 로고
    • Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
    • Lee, J.H., Ozorowski, G., Ward, A.B., Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer. Science 351 (2016), 1043–1048.
    • (2016) Science , vol.351 , pp. 1043-1048
    • Lee, J.H.1    Ozorowski, G.2    Ward, A.B.3
  • 49
    • 0033865498 scopus 로고    scopus 로고
    • Patterns of changes in human immunodeficiency virus type 1 V3 sequence populations late in infection
    • Nelson, J.A., Baribaud, F., Edwards, T., Swanstrom, R., Patterns of changes in human immunodeficiency virus type 1 V3 sequence populations late in infection. J. Virol. 74 (2000), 8494–8501.
    • (2000) J. Virol. , vol.74 , pp. 8494-8501
    • Nelson, J.A.1    Baribaud, F.2    Edwards, T.3    Swanstrom, R.4
  • 52
    • 12144287132 scopus 로고    scopus 로고
    • Phenotypic and genotypic comparisons of CCR5- and CXCR4-tropic human immunodeficiency virus type 1 biological clones isolated from subtype C-infected individuals
    • Pollakis, G., Abebe, A., Kliphuis, A., Chalaby, M.I.M., Bakker, M., Mengistu, Y., Brouwer, M., Goudsmit, J., Schuitemaker, H., Paxton, W.A., Phenotypic and genotypic comparisons of CCR5- and CXCR4-tropic human immunodeficiency virus type 1 biological clones isolated from subtype C-infected individuals. J. Virol. 78 (2004), 2841–2852.
    • (2004) J. Virol. , vol.78 , pp. 2841-2852
    • Pollakis, G.1    Abebe, A.2    Kliphuis, A.3    Chalaby, M.I.M.4    Bakker, M.5    Mengistu, Y.6    Brouwer, M.7    Goudsmit, J.8    Schuitemaker, H.9    Paxton, W.A.10
  • 54
    • 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, A.W., Bjorkman, P.J., Broadly neutralizing antibody 8ANC195 recognizes closed and open states of HIV-1 Env. Cell 162 (2015), 1379–1390.
    • (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
  • 57
    • 67650453747 scopus 로고    scopus 로고
    • HIV-1 elite neutralizers: individuals with broad and potent neutralizing activity identified using a high throughput neutralization assay together with an analytical selection algorithm
    • Simek, M.D., Rida, W., Priddy, F.H., Pung, P., Carrow, E., Laufer, D.S., Lehrman, J.K., Boaz, M., Tarragona-Fiol, T., Miiro, G., et al. HIV-1 elite neutralizers: individuals with broad and potent neutralizing activity identified using a high throughput neutralization assay together with an analytical selection algorithm. J. Virol. 83 (2009), 7337–7348.
    • (2009) J. Virol. , vol.83 , pp. 7337-7348
    • Simek, M.D.1    Rida, W.2    Priddy, F.H.3    Pung, P.4    Carrow, E.5    Laufer, D.S.6    Lehrman, J.K.7    Boaz, M.8    Tarragona-Fiol, T.9    Miiro, G.10
  • 58
    • 84888251984 scopus 로고    scopus 로고
    • The effects of somatic hypermutation on neutralization and binding in the PGT121 family of broadly neutralizing HIV antibodies
    • Sok, D., Laserson, U., Laserson, J., Liu, Y., Vigneault, F., Julien, J.-P., Briney, B., Ramos, A., Saye, K.F., Le, K., et al. The effects of somatic hypermutation on neutralization and binding in the PGT121 family of broadly neutralizing HIV antibodies. PLoS Pathog., 9, 2013, e1003754.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003754
    • Sok, D.1    Laserson, U.2    Laserson, J.3    Liu, Y.4    Vigneault, F.5    Julien, J.-P.6    Briney, B.7    Ramos, A.8    Saye, K.F.9    Le, K.10
  • 59
    • 84886780701 scopus 로고    scopus 로고
    • SnapShot: broadly neutralizing antibodies
    • 728–7e1
    • Sok, D., Moldt, B., Burton, D.R., SnapShot: broadly neutralizing antibodies. Cell, 155, 2013 728–7e1.
    • (2013) Cell , vol.155
    • Sok, D.1    Moldt, B.2    Burton, D.R.3
  • 62
    • 33847272713 scopus 로고    scopus 로고
    • Mutations in the V3 stem versus the V3 crown and C4 region have different effects on the binding and fusion steps of human immunodeficiency virus type 1 gp120 interaction with the CCR5 coreceptor
    • Suphaphiphat, P., Essex, M., Lee, T.-H., Mutations in the V3 stem versus the V3 crown and C4 region have different effects on the binding and fusion steps of human immunodeficiency virus type 1 gp120 interaction with the CCR5 coreceptor. Virology 360 (2007), 182–190.
    • (2007) Virology , vol.360 , pp. 182-190
    • Suphaphiphat, P.1    Essex, M.2    Lee, T.-H.3
  • 63
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali, M., Moore, J.P., Furman, C., Charles, M., Ho, D.D., Robinson, J., Sodroski, J., Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67 (1993), 3978–3988.
    • (1993) J. Virol. , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5    Robinson, J.6    Sodroski, J.7
  • 64
    • 36849031722 scopus 로고    scopus 로고
    • Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning
    • Tiller, T., Meffre, E., Yurasov, S., Tsuiji, M., Nussenzweig, M.C., Wardemann, H., Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning. J. Immunol. Methods 329 (2008), 112–124.
    • (2008) J. Immunol. Methods , vol.329 , pp. 112-124
    • Tiller, T.1    Meffre, E.2    Yurasov, S.3    Tsuiji, M.4    Nussenzweig, M.C.5    Wardemann, H.6
  • 68
    • 0032510757 scopus 로고    scopus 로고
    • CCR5 coreceptor utilization involves a highly conserved arginine residue of HIV type 1 gp120
    • Wang, W.K., Dudek, T., Zhao, Y.J., Brumblay, H.G., Essex, M., Lee, T.H., CCR5 coreceptor utilization involves a highly conserved arginine residue of HIV type 1 gp120. Proc. Natl. Acad. Sci. USA 95 (1998), 5740–5745.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5740-5745
    • Wang, W.K.1    Dudek, T.2    Zhao, Y.J.3    Brumblay, H.G.4    Essex, M.5    Lee, T.H.6
  • 70
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu, X., Zhou, T., Zhu, J., Zhang, B., Georgiev, I., Wang, C., Chen, X., Longo, N.S., Louder, M., McKee, K., et al., NISC Comparative Sequencing Program. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 333 (2011), 1593–1602.
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1    Zhou, T.2    Zhu, J.3    Zhang, B.4    Georgiev, I.5    Wang, C.6    Chen, X.7    Longo, N.S.8    Louder, M.9    McKee, K.10
  • 72
    • 84875186505 scopus 로고    scopus 로고
    • A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin
    • Xu, R., Krause, J.C., McBride, R., Paulson, J.C., Crowe, J.E. Jr., Wilson, I.A., A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin. Nat. Struct. Mol. Biol. 20 (2013), 363–370.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 363-370
    • Xu, R.1    Krause, J.C.2    McBride, R.3    Paulson, J.C.4    Crowe, J.E.5    Wilson, I.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.