메뉴 건너뛰기




Volumn 18, Issue 9, 2017, Pages 2175-2188

Vaccine Elicitation of High Mannose-Dependent Neutralizing Antibodies against the V3-Glycan Broadly Neutralizing Epitope in Nonhuman Primates

(35)  Saunders, Kevin O a   Nicely, Nathan I a   Wiehe, Kevin a   Bonsignori, Mattia a   Meyerhoff, R Ryan a   Parks, Robert a   Walkowicz, William E b   Aussedat, Baptiste b   Wu, Nelson R a   Cai, Fangping a   Vohra, Yusuf b   Park, Peter K b   Eaton, Amanda a   Go, Eden P f   Sutherland, Laura L a   Scearce, Richard M a   Barouch, Dan H i   Zhang, Ruijun a   Von Holle, Tarra a   Overman, R Glenn a   more..


Author keywords

glycan; HIV; long term immunization; V3 glycan; vaccination

Indexed keywords

AMINO ACID; EPITOPE; GLYCAN; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; MANNOSE; MANNOSE OLIGOSACCHARIDE; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; POLYSACCHARIDE; VACCINE; VIRUS ENVELOPE PROTEIN;

EID: 85014123206     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2017.02.003     Document Type: Article
Times cited : (60)

References (81)
  • 1
    • 78650062305 scopus 로고    scopus 로고
    • Yeast-elicited cross-reactive antibodies to HIV Env glycans efficiently neutralize virions expressing exclusively high-mannose N-linked glycans
    • Agrawal-Gamse, C., Luallen, R.J., Liu, B., Fu, H., Lee, F.H., Geng, Y., Doms, R.W., Yeast-elicited cross-reactive antibodies to HIV Env glycans efficiently neutralize virions expressing exclusively high-mannose N-linked glycans. J. Virol. 85 (2011), 470–480.
    • (2011) J. Virol. , vol.85 , pp. 470-480
    • Agrawal-Gamse, C.1    Luallen, R.J.2    Liu, B.3    Fu, H.4    Lee, F.H.5    Geng, Y.6    Doms, R.W.7
  • 3
    • 45749138808 scopus 로고    scopus 로고
    • A glycoconjugate antigen based on the recognition motif of a broadly neutralizing human immunodeficiency virus antibody, 2G12, is immunogenic but elicits antibodies unable to bind to the self glycans of gp120
    • Astronomo, R.D., Lee, H.K., Scanlan, C.N., Pantophlet, R., Huang, C.Y., Wilson, I.A., Blixt, O., Dwek, R.A., Wong, C.H., Burton, D.R., A glycoconjugate antigen based on the recognition motif of a broadly neutralizing human immunodeficiency virus antibody, 2G12, is immunogenic but elicits antibodies unable to bind to the self glycans of gp120. J. Virol. 82 (2008), 6359–6368.
    • (2008) J. Virol. , vol.82 , pp. 6359-6368
    • Astronomo, R.D.1    Lee, H.K.2    Scanlan, C.N.3    Pantophlet, R.4    Huang, C.Y.5    Wilson, I.A.6    Blixt, O.7    Dwek, R.A.8    Wong, C.H.9    Burton, D.R.10
  • 8
    • 84912062551 scopus 로고    scopus 로고
    • Nucleotide insertions and deletions complement point mutations to massively expand the diversity created by somatic hypermutation of antibodies
    • Bowers, P.M., Verdino, P., Wang, Z., da Silva Correia, J., Chhoa, M., Macondray, G., Do, M., Neben, T.Y., Horlick, R.A., Stanfield, R.L., et al. Nucleotide insertions and deletions complement point mutations to massively expand the diversity created by somatic hypermutation of antibodies. J. Biol. Chem. 289 (2014), 33557–33567.
    • (2014) J. Biol. Chem. , vol.289 , pp. 33557-33567
    • Bowers, P.M.1    Verdino, P.2    Wang, Z.3    da Silva Correia, J.4    Chhoa, M.5    Macondray, G.6    Do, M.7    Neben, T.Y.8    Horlick, R.A.9    Stanfield, R.L.10
  • 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
  • 13
    • 33747890974 scopus 로고    scopus 로고
    • Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase I-independent fucosylation pathway
    • Crispin, M., Harvey, D.J., Chang, V.T., Yu, C., Aricescu, A.R., Jones, E.Y., Davis, S.J., Dwek, R.A., Rudd, P.M., Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase I-independent fucosylation pathway. Glycobiology 16 (2006), 748–756.
    • (2006) Glycobiology , vol.16 , pp. 748-756
    • Crispin, M.1    Harvey, D.J.2    Chang, V.T.3    Yu, C.4    Aricescu, A.R.5    Jones, E.Y.6    Davis, S.J.7    Dwek, R.A.8    Rudd, P.M.9
  • 14
    • 84930365226 scopus 로고    scopus 로고
    • Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site
    • Crooks, E.T., Tong, T., Chakrabarti, B., Narayan, K., Georgiev, I.S., Menis, S., Huang, X., Kulp, D., Osawa, K., Muranaka, J., et al. Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site. PLoS Pathog., 11, 2015, e1004932.
    • (2015) PLoS Pathog. , vol.11 , pp. e1004932
    • Crooks, E.T.1    Tong, T.2    Chakrabarti, B.3    Narayan, K.4    Georgiev, I.S.5    Menis, S.6    Huang, X.7    Kulp, D.8    Osawa, K.9    Muranaka, J.10
  • 16
    • 79955574923 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System
    • Schrödinger, LLC
    • DeLano, W.L., The PyMOL Molecular Graphics System. 2012, Schrödinger, LLC.
    • (2012)
    • DeLano, W.L.1
  • 17
    • 0028946178 scopus 로고
    • Antibodies to the Cryptococcus neoformans capsular glucuronoxylomannan are ubiquitous in serum from HIV+ and HIV- individuals
    • Deshaw, M., Pirofski, L.A., Antibodies to the Cryptococcus neoformans capsular glucuronoxylomannan are ubiquitous in serum from HIV+ and HIV- individuals. Clin. Exp. Immunol. 99 (1995), 425–432.
    • (1995) Clin. Exp. Immunol. , vol.99 , pp. 425-432
    • Deshaw, M.1    Pirofski, L.A.2
  • 18
    • 84959117772 scopus 로고    scopus 로고
    • The HIV glycan shield as a target for broadly neutralizing antibodies
    • Doores, K.J., The HIV glycan shield as a target for broadly neutralizing antibodies. FEBS J. 282 (2015), 4679–4691.
    • (2015) FEBS J. , vol.282 , pp. 4679-4691
    • Doores, K.J.1
  • 19
    • 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
  • 22
    • 84920771783 scopus 로고    scopus 로고
    • Two classes of broadly neutralizing antibodies within a single lineage directed to the high-mannose patch of HIV envelope
    • Doores, K.J., Kong, L., Krumm, S.A., Le, K.M., Sok, D., Laserson, U., Garces, F., Poignard, P., Wilson, I.A., Burton, D.R., Two classes of broadly neutralizing antibodies within a single lineage directed to the high-mannose patch of HIV envelope. J. Virol. 89 (2015), 1105–1118.
    • (2015) J. Virol. , vol.89 , pp. 1105-1118
    • Doores, K.J.1    Kong, L.2    Krumm, S.A.3    Le, K.M.4    Sok, D.5    Laserson, U.6    Garces, F.7    Poignard, P.8    Wilson, I.A.9    Burton, D.R.10
  • 25
    • 77956366187 scopus 로고    scopus 로고
    • Polysaccharide mimicry of the epitope of the broadly neutralizing anti-HIV antibody, 2G12, induces enhanced antibody responses to self oligomannose glycans
    • Dunlop, D.C., Bonomelli, C., Mansab, F., Vasiljevic, S., Doores, K.J., Wormald, M.R., Palma, A.S., Feizi, T., Harvey, D.J., Dwek, R.A., et al. Polysaccharide mimicry of the epitope of the broadly neutralizing anti-HIV antibody, 2G12, induces enhanced antibody responses to self oligomannose glycans. Glycobiology 20 (2010), 812–823.
    • (2010) Glycobiology , vol.20 , pp. 812-823
    • Dunlop, D.C.1    Bonomelli, C.2    Mansab, F.3    Vasiljevic, S.4    Doores, K.J.5    Wormald, M.R.6    Palma, A.S.7    Feizi, T.8    Harvey, D.J.9    Dwek, R.A.10
  • 28
    • 84893570591 scopus 로고    scopus 로고
    • Ending AIDS–is an HIV vaccine necessary?
    • Fauci, A.S., Marston, H.D., Ending AIDS–is an HIV vaccine necessary?. N. Engl. J. Med. 370 (2014), 495–498.
    • (2014) N. Engl. J. Med. , vol.370 , pp. 495-498
    • Fauci, A.S.1    Marston, H.D.2
  • 31
    • 45549101708 scopus 로고    scopus 로고
    • Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes’ accessibility
    • Go, E.P., Irungu, J., Zhang, Y., Dalpathado, D.S., Liao, H.X., Sutherland, L.L., Alam, S.M., Haynes, B.F., Desaire, H., Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes’ accessibility. J. Proteome Res. 7 (2008), 1660–1674.
    • (2008) J. Proteome Res. , vol.7 , pp. 1660-1674
    • Go, E.P.1    Irungu, J.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.X.5    Sutherland, L.L.6    Alam, S.M.7    Haynes, B.F.8    Desaire, H.9
  • 32
    • 84874622598 scopus 로고    scopus 로고
    • Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins
    • Go, E.P., Liao, H.X., Alam, S.M., Hua, D., Haynes, B.F., Desaire, H., Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins. J. Proteome Res. 12 (2013), 1223–1234.
    • (2013) J. Proteome Res. , vol.12 , pp. 1223-1234
    • Go, E.P.1    Liao, H.X.2    Alam, S.M.3    Hua, D.4    Haynes, B.F.5    Desaire, H.6
  • 33
    • 84938149437 scopus 로고    scopus 로고
    • Comparative Analysis of the Glycosylation Profiles of Membrane-Anchored HIV-1 Envelope Glycoprotein Trimers and Soluble gp140
    • Go, E.P., Herschhorn, A., Gu, C., Castillo-Menendez, L., Zhang, S., Mao, Y., Chen, H., Ding, H., Wakefield, J.K., Hua, D., et al. Comparative Analysis of the Glycosylation Profiles of Membrane-Anchored HIV-1 Envelope Glycoprotein Trimers and Soluble gp140. J. Virol. 89 (2015), 8245–8257.
    • (2015) J. Virol. , vol.89 , pp. 8245-8257
    • Go, E.P.1    Herschhorn, A.2    Gu, C.3    Castillo-Menendez, L.4    Zhang, S.5    Mao, Y.6    Chen, H.7    Ding, H.8    Wakefield, J.K.9    Hua, D.10
  • 34
    • 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
  • 35
    • 33344479421 scopus 로고    scopus 로고
    • Antiviral antibody responses: the two extremes of a wide spectrum
    • Hangartner, L., Zinkernagel, R.M., Hengartner, H., Antiviral antibody responses: the two extremes of a wide spectrum. Nat. Rev. Immunol. 6 (2006), 231–243.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 231-243
    • Hangartner, L.1    Zinkernagel, R.M.2    Hengartner, H.3
  • 36
    • 84900317748 scopus 로고    scopus 로고
    • AIDS/HIV. Host controls of HIV neutralizing antibodies
    • Haynes, B.F., Verkoczy, L., AIDS/HIV. Host controls of HIV neutralizing antibodies. Science 344 (2014), 588–589.
    • (2014) Science , vol.344 , pp. 588-589
    • Haynes, B.F.1    Verkoczy, L.2
  • 37
    • 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., 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
  • 38
    • 0032096837 scopus 로고    scopus 로고
    • Continuum solvation model: computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation
    • Im, W., Beglov, D., Roux, B., Continuum solvation model: computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation. Comput. Phys. Commun. 111 (1998), 59–75.
    • (1998) Comput. Phys. Commun. , vol.111 , pp. 59-75
    • Im, W.1    Beglov, D.2    Roux, B.3
  • 39
    • 47149096704 scopus 로고    scopus 로고
    • CHARMM-GUI: a web-based graphical user interface for CHARMM
    • Jo, S., Kim, T., Iyer, V.G., Im, W., CHARMM-GUI: a web-based graphical user interface for CHARMM. J. Comput. Chem. 29 (2008), 1859–1865.
    • (2008) J. Comput. Chem. , vol.29 , pp. 1859-1865
    • Jo, S.1    Kim, T.2    Iyer, V.G.3    Im, W.4
  • 40
    • 48449099381 scopus 로고    scopus 로고
    • PBEQ-Solver for online visualization of electrostatic potential of biomolecules
    • Jo, S., Vargyas, M., Vasko-Szedlar, J., Roux, B., Im, W., PBEQ-Solver for online visualization of electrostatic potential of biomolecules. Nucleic Acids Res. 36 (2008), W270–W275.
    • (2008) Nucleic Acids Res. , vol.36 , pp. W270-W275
    • Jo, S.1    Vargyas, M.2    Vasko-Szedlar, J.3    Roux, B.4    Im, W.5
  • 43
    • 85000360533 scopus 로고    scopus 로고
    • Reconstructing a B-cell clonal lineage. I. Statistical inference of unobserved ancestors
    • Kepler, T.B., Reconstructing a B-cell clonal lineage. I. Statistical inference of unobserved ancestors. F1000Res., 2, 2013, 103.
    • (2013) F1000Res. , vol.2 , pp. 103
    • Kepler, T.B.1
  • 47
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard, C.K., Spellman, M.W., Riddle, L., Harris, R.J., Thomas, J.N., Gregory, T.J., Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265 (1990), 10373–10382.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 50
    • 84875771414 scopus 로고    scopus 로고
    • Antigenicity and immunogenicity of transmitted/founder, consensus, and chronic envelope glycoproteins of human immunodeficiency virus type 1
    • Liao, H.X., Tsao, C.Y., Alam, S.M., Muldoon, M., Vandergrift, N., Ma, B.J., Lu, X., Sutherland, L.L., Scearce, R.M., Bowman, C., et al. Antigenicity and immunogenicity of transmitted/founder, consensus, and chronic envelope glycoproteins of human immunodeficiency virus type 1. J. Virol. 87 (2013), 4185–4201.
    • (2013) J. Virol. , vol.87 , pp. 4185-4201
    • Liao, H.X.1    Tsao, C.Y.2    Alam, S.M.3    Muldoon, M.4    Vandergrift, N.5    Ma, B.J.6    Lu, X.7    Sutherland, L.L.8    Scearce, R.M.9    Bowman, C.10
  • 51
    • 84967148279 scopus 로고    scopus 로고
    • Early Antibody Lineage Diversification and Independent Limb Maturation Lead to Broad HIV-1 Neutralization Targeting the Env High-Mannose Patch
    • MacLeod, D.T., Choi, N.M., Briney, B., Garces, F., Ver, L.S., Landais, E., Murrell, B., Wrin, T., Kilembe, W., Liang, C.H., et al., IAVI Protocol C Investigators & The IAVI African HIV Research Network. Early Antibody Lineage Diversification and Independent Limb Maturation Lead to Broad HIV-1 Neutralization Targeting the Env High-Mannose Patch. Immunity 44 (2016), 1215–1226.
    • (2016) Immunity , vol.44 , pp. 1215-1226
    • MacLeod, D.T.1    Choi, N.M.2    Briney, B.3    Garces, F.4    Ver, L.S.5    Landais, E.6    Murrell, B.7    Wrin, T.8    Kilembe, W.9    Liang, C.H.10
  • 52
    • 84879302728 scopus 로고    scopus 로고
    • HIV-1 neutralizing antibodies: understanding nature's pathways
    • Mascola, J.R., Haynes, B.F., HIV-1 neutralizing antibodies: understanding nature's pathways. Immunol. Rev. 254 (2013), 225–244.
    • (2013) Immunol. Rev. , vol.254 , pp. 225-244
    • Mascola, J.R.1    Haynes, B.F.2
  • 53
    • 77952311370 scopus 로고    scopus 로고
    • The role of antibodies in HIV vaccines
    • Mascola, J.R., Montefiori, D.C., The role of antibodies in HIV vaccines. Annu. Rev. Immunol. 28 (2010), 413–444.
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 413-444
    • Mascola, J.R.1    Montefiori, D.C.2
  • 58
    • 84921564277 scopus 로고    scopus 로고
    • Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy
    • Murin, C.D., Julien, J.P., Sok, D., Stanfield, R.L., Khayat, R., Cupo, A., Moore, J.P., Burton, D.R., Wilson, I.A., Ward, A.B., Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy. J. Virol. 88 (2014), 10177–10188.
    • (2014) J. Virol. , vol.88 , pp. 10177-10188
    • Murin, C.D.1    Julien, J.P.2    Sok, D.3    Stanfield, R.L.4    Khayat, R.5    Cupo, A.6    Moore, J.P.7    Burton, D.R.8    Wilson, I.A.9    Ward, A.B.10
  • 60
    • 0035222608 scopus 로고    scopus 로고
    • The antiviral activity of antibodies in vitro and in vivo
    • Parren, P.W., Burton, D.R., The antiviral activity of antibodies in vitro and in vivo. Adv. Immunol. 77 (2001), 195–262.
    • (2001) Adv. Immunol. , vol.77 , pp. 195-262
    • Parren, P.W.1    Burton, D.R.2
  • 62
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves, P.J., Callewaert, N., Contreras, R., Khorana, H.G., Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl. Acad. Sci. USA 99 (2002), 13419–13424.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 65
    • 34247636624 scopus 로고    scopus 로고
    • Exploiting the defensive sugars of HIV-1 for drug and vaccine design
    • Scanlan, C.N., Offer, J., Zitzmann, N., Dwek, R.A., Exploiting the defensive sugars of HIV-1 for drug and vaccine design. Nature 446 (2007), 1038–1045.
    • (2007) Nature , vol.446 , pp. 1038-1045
    • Scanlan, C.N.1    Offer, J.2    Zitzmann, N.3    Dwek, R.A.4
  • 67
    • 67650453747 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 elite neutralizers: individuals with broad and potent neutralizing activity identified by 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. Human immunodeficiency virus type 1 elite neutralizers: individuals with broad and potent neutralizing activity identified by 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
  • 69
    • 84990856306 scopus 로고    scopus 로고
    • A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans
    • Sok, D., Pauthner, M., Briney, B., Lee, J.H., Saye-Francisco, K.L., Hsueh, J., Ramos, A., Le, K.M., Jones, M., Jardine, J.G., et al. A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans. Immunity 45 (2016), 31–45.
    • (2016) Immunity , vol.45 , pp. 31-45
    • Sok, D.1    Pauthner, M.2    Briney, B.3    Lee, J.H.4    Saye-Francisco, K.L.5    Hsueh, J.6    Ramos, A.7    Le, K.M.8    Jones, M.9    Jardine, J.G.10
  • 71
    • 84986300672 scopus 로고    scopus 로고
    • Induction of HIV Neutralizing Antibody Lineages in Mice with Diverse Precursor Repertoires
    • Tian, M., Cheng, C., Chen, X., Duan, H., Cheng, H.L., Dao, M., Sheng, Z., Kimble, M., Wang, L., Lin, S., et al. Induction of HIV Neutralizing Antibody Lineages in Mice with Diverse Precursor Repertoires. Cell 166 (2016), 1471–1484.
    • (2016) Cell , vol.166 , pp. 1471-1484
    • Tian, M.1    Cheng, C.2    Chen, X.3    Duan, H.4    Cheng, H.L.5    Dao, M.6    Sheng, Z.7    Kimble, M.8    Wang, L.9    Lin, S.10
  • 72
    • 32544437698 scopus 로고    scopus 로고
    • SoDA: implementation of a 3D alignment algorithm for inference of antigen receptor recombinations
    • Volpe, J.M., Cowell, L.G., Kepler, T.B., SoDA: implementation of a 3D alignment algorithm for inference of antigen receptor recombinations. Bioinformatics 22 (2006), 438–444.
    • (2006) Bioinformatics , vol.22 , pp. 438-444
    • Volpe, J.M.1    Cowell, L.G.2    Kepler, T.B.3
  • 74
    • 77958115264 scopus 로고    scopus 로고
    • A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals
    • Walker, L.M., Simek, M.D., Priddy, F., Gach, J.S., Wagner, D., Zwick, M.B., Phogat, S.K., Poignard, P., Burton, D.R., A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals. PLoS Pathog., 6, 2010, e1001028.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001028
    • Walker, L.M.1    Simek, M.D.2    Priddy, F.3    Gach, J.S.4    Wagner, D.5    Zwick, M.B.6    Phogat, S.K.7    Poignard, P.8    Burton, D.R.9
  • 76
    • 41649109652 scopus 로고    scopus 로고
    • Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN
    • Wang, S.K., Liang, P.H., Astronomo, R.D., Hsu, T.L., Hsieh, S.L., Burton, D.R., Wong, C.H., Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN. Proc. Natl. Acad. Sci. USA 105 (2008), 3690–3695.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3690-3695
    • Wang, S.K.1    Liang, P.H.2    Astronomo, R.D.3    Hsu, T.L.4    Hsieh, S.L.5    Burton, D.R.6    Wong, C.H.7
  • 78
    • 84918548024 scopus 로고    scopus 로고
    • Antibody light-chain-restricted recognition of the site of immune pressure in the RV144 HIV-1 vaccine trial is phylogenetically conserved
    • Wiehe, K., Easterhoff, D., Luo, K., Nicely, N.I., Bradley, T., Jaeger, F.H., Dennison, S.M., Zhang, R., Lloyd, K.E., Stolarchuk, C., et al. Antibody light-chain-restricted recognition of the site of immune pressure in the RV144 HIV-1 vaccine trial is phylogenetically conserved. Immunity 41 (2014), 909–918.
    • (2014) Immunity , vol.41 , pp. 909-918
    • Wiehe, K.1    Easterhoff, D.2    Luo, K.3    Nicely, N.I.4    Bradley, T.5    Jaeger, F.H.6    Dennison, S.M.7    Zhang, R.8    Lloyd, K.E.9    Stolarchuk, C.10
  • 79
    • 84941747254 scopus 로고    scopus 로고
    • Antibodies elicited by yeast glycoproteins recognize HIV-1 virions and potently neutralize virions with high mannose N-glycans
    • Zhang, H., Fu, H., Luallen, R.J., Liu, B., Lee, F.H., Doms, R.W., Geng, Y., Antibodies elicited by yeast glycoproteins recognize HIV-1 virions and potently neutralize virions with high mannose N-glycans. Vaccine 33 (2015), 5140–5147.
    • (2015) Vaccine , vol.33 , pp. 5140-5147
    • Zhang, H.1    Fu, H.2    Luallen, R.J.3    Liu, B.4    Lee, F.H.5    Doms, R.W.6    Geng, Y.7
  • 81
    • 84882589754 scopus 로고    scopus 로고
    • Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies
    • Zhou, T., Zhu, J., Wu, X., Moquin, S., Zhang, B., Acharya, P., Georgiev, I.S., Altae-Tran, H.R., Chuang, G.Y., Joyce, M.G., et al., NISC Comparative Sequencing Program. Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies. Immunity 39 (2013), 245–258.
    • (2013) Immunity , vol.39 , pp. 245-258
    • Zhou, T.1    Zhu, J.2    Wu, X.3    Moquin, S.4    Zhang, B.5    Acharya, P.6    Georgiev, I.S.7    Altae-Tran, H.R.8    Chuang, G.Y.9    Joyce, M.G.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.