메뉴 건너뛰기




Volumn 90, Issue 22, 2016, Pages 10220-10235

Structure of an N276-dependent HIV-1 neutralizing antibody targeting a rare V5 glycan hole adjacent to the CD4 binding site

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CD4 ANTIGEN; EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; BLOCKING ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; POLYSACCHARIDE;

EID: 84995377829     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01357-16     Document Type: Article
Times cited : (27)

References (71)
  • 2
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • Richman DD, Wrin T, Little SJ, Petropoulos CJ. 2003. Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc Natl Acad Sci U S A 100:4144-4149. http://dx.doi.org/10.1073/pnas.0630530100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4144-4149
    • Richman, D.D.1    Wrin, T.2    Little, S.J.3    Petropoulos, C.J.4
  • 4
    • 49149118421 scopus 로고    scopus 로고
    • Autologous neutralizing humoral immunity and evolution of the viral envelope in the course of subtype B human immunodeficiency virus type 1 infection
    • Bunnik EM, Pisas L, van Nuenen AC, Schuitemaker H. 2008. Autologous neutralizing humoral immunity and evolution of the viral envelope in the course of subtype B human immunodeficiency virus type 1 infection. J Virol 82:7932-7941. http://dx.doi.org/10.1128/JVI.00757-08.
    • (2008) J Virol , vol.82 , pp. 7932-7941
    • Bunnik, E.M.1    Pisas, L.2    van Nuenen, A.C.3    Schuitemaker, H.4
  • 5
    • 38849090714 scopus 로고    scopus 로고
    • The C3-V4 region is a major target of autologous neutralizing antibodies in human immunodeficiency virus type 1 subtype C infection
    • Moore PL, Gray ES, Choge IA, Ranchobe N, Mlisana K, Abdool Karim SS, Williamson C, Morris L. 2008. The C3-V4 region is a major target of autologous neutralizing antibodies in human immunodeficiency virus type 1 subtype C infection. J Virol 82:1860-1869. http://dx.doi.org/10.1128/JVI.02187-07.
    • (2008) J Virol , vol.82 , pp. 1860-1869
    • Moore, P.L.1    Gray, E.S.2    Choge, I.A.3    Ranchobe, N.4    Mlisana, K.5    Abdool Karim, S.S.6    Williamson, C.7    Morris, L.8
  • 7
    • 33846552274 scopus 로고    scopus 로고
    • Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection
    • Rong R, Bibollet-Ruche F, Mulenga J, Allen S, Blackwell JL, Derdeyn CA. 2007. Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection. J Virol 81:1350-1359. http://dx.doi.org/10.1128/JVI.01839-06.
    • (2007) J Virol , vol.81 , pp. 1350-1359
    • Rong, R.1    Bibollet-Ruche, F.2    Mulenga, J.3    Allen, S.4    Blackwell, J.L.5    Derdeyn, C.A.6
  • 10
    • 58149487645 scopus 로고    scopus 로고
    • Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection
    • Sather DN, Armann J, Ching LK, Mavrantoni A, Sellhorn G, Caldwell Z, Yu X, Wood B, Self S, Kalams S, Stamatatos L. 2009. Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J Virol 83:757-769. http://dx.doi.org/10.1128/JVI.02036-08.
    • (2009) J Virol , vol.83 , pp. 757-769
    • Sather, D.N.1    Armann, J.2    Ching, L.K.3    Mavrantoni, A.4    Sellhorn, G.5    Caldwell, Z.6    Yu, X.7    Wood, B.8    Self, S.9    Kalams, S.10    Stamatatos, L.11
  • 13
    • 77749306129 scopus 로고    scopus 로고
    • Cross-reactive neutralizing humoral immunity does not protect from HIV type 1 disease progression
    • Euler Z, van Gils MJ, Bunnik EM, Phung P, Schweighardt B, Wrin T, Schuitemaker H. 2010. Cross-reactive neutralizing humoral immunity does not protect from HIV type 1 disease progression. J Infect Dis 201: 1045-1053. http://dx.doi.org/10.1086/651144.
    • (2010) J Infect Dis , vol.201 , pp. 1045-1053
    • Euler, Z.1    van Gils, M.J.2    Bunnik, E.M.3    Phung, P.4    Schweighardt, B.5    Wrin, T.6    Schuitemaker, H.7
  • 14
    • 84928569654 scopus 로고    scopus 로고
    • HIV broadly neutralizing antibody targets
    • Wibmer CK, Moore PL, Morris L. 2015. HIV broadly neutralizing antibody targets. Curr Opin HIV AIDS 10:135-143. http://dx.doi.org/10.1097/COH.0000000000000153.
    • (2015) Curr Opin HIV AIDS , vol.10 , pp. 135-143
    • Wibmer, C.K.1    Moore, P.L.2    Morris, L.3
  • 19
    • 84898538468 scopus 로고    scopus 로고
    • Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection
    • Derdeyn CA, Moore PL, Morris L. 2014. Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection. Curr Opin HIV AIDS 9:210-216. http://dx.doi.org/10.1097/COH.0000000000000057.
    • (2014) Curr Opin HIV AIDS , vol.9 , pp. 210-216
    • Derdeyn, C.A.1    Moore, P.L.2    Morris, L.3
  • 33
    • 84880431984 scopus 로고    scopus 로고
    • The N276 glycosylation site is required for HIV-1 neutralization by the CD4 binding site specific HJ16 monoclonal antibody
    • Balla-Jhagjhoorsingh SS, Corti D, Heyndrickx L, Willems E, Vereecken K, Davis D, Vanham G. 2013. The N276 glycosylation site is required for HIV-1 neutralization by the CD4 binding site specific HJ16 monoclonal antibody. PLoS One 8:e68863. http://dx.doi.org/10.1371/journal.pone.0068863.
    • (2013) PLoS One , vol.8
    • Balla-Jhagjhoorsingh, S.S.1    Corti, D.2    Heyndrickx, L.3    Willems, E.4    Vereecken, K.5    Davis, D.6    Vanham, G.7
  • 36
    • 84887270287 scopus 로고    scopus 로고
    • Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes
    • Wibmer CK, Bhiman JN, Gray ES, Tumba N, Abdool Karim SS, Williamson C, Morris L, Moore PL. 2013. Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes. PLoS Pathog 9:e1003738. http://dx.doi.org/10.1371/journal.ppat.1003738.
    • (2013) PLoS Pathog , vol.9
    • Wibmer, C.K.1    Bhiman, J.N.2    Gray, E.S.3    Tumba, N.4    Abdool Karim, S.S.5    Williamson, C.6    Morris, L.7    Moore, P.L.8
  • 37
    • 19944423187 scopus 로고    scopus 로고
    • Evaluating neutralizing antibodies against HIV, SIV and SHIV in luciferase reporter gene assays
    • Coligan JE, Kruisbeek AM, Margulies DH, Shevach EM, Strober W, Coico R (ed), John Wiley&Sons, Chichester, United Kingdom
    • Montefiori DC. 2004. Evaluating neutralizing antibodies against HIV, SIV and SHIV in luciferase reporter gene assays, p 12.11.1-12.11.15. In Coligan JE, Kruisbeek AM, Margulies DH, Shevach EM, Strober W, Coico R (ed), Current protocols in immunology. John Wiley&Sons, Chichester, United Kingdom.
    • (2004) Current protocols in immunology , pp. 12.11.1-12.11.15
    • Montefiori, D.C.1
  • 39
    • 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 MC, Wardemann H. 2008. Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning. J Immunol Methods 329:112-124. http://dx.doi.org/10.1016/j.jim.2007.09.017.
    • (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
  • 40
    • 84055200527 scopus 로고    scopus 로고
    • Accurate sampling and deep sequencing of the HIV-1 protease gene using a Primer ID
    • Jabara CB, Jones CD, Roach J, Anderson JA, Swanstrom R. 2011. Accurate sampling and deep sequencing of the HIV-1 protease gene using a Primer ID. Proc Natl Acad SciUSA108:20166-20171. http://dx.doi.org/10.1073/pnas.1110064108.
    • (2011) Proc Natl Acad SciUSA , vol.108 , pp. 20166-20171
    • Jabara, C.B.1    Jones, C.D.2    Roach, J.3    Anderson, J.A.4    Swanstrom, R.5
  • 41
    • 84905049901 scopus 로고    scopus 로고
    • Trimmomatic: a flexible trimmer for Illumina sequence data
    • Bolger AM, Lohse M, Usadel B. 2014. Trimmomatic: a flexible trimmer for Illumina sequence data. Bioinformatics 30:2114-2120. http://dx.doi.org/10.1093/bioinformatics/btu170.
    • (2014) Bioinformatics , vol.30 , pp. 2114-2120
    • Bolger, A.M.1    Lohse, M.2    Usadel, B.3
  • 42
    • 84897676120 scopus 로고    scopus 로고
    • PEAR: a fast and accurate Illumina paired-end read merger
    • Zhang J, Kobert K, Flouri T, Stamatakis A. 2014. PEAR: a fast and accurate Illumina paired-end read merger. Bioinformatics 30:614-620. http://dx.doi.org/10.1093/bioinformatics/btt593.
    • (2014) Bioinformatics , vol.30 , pp. 614-620
    • Zhang, J.1    Kobert, K.2    Flouri, T.3    Stamatakis, A.4
  • 43
    • 84875619226 scopus 로고    scopus 로고
    • MAFFT multiple sequence alignment software version 7: improvements in performance and usability
    • Katoh K, Standley DM. 2013. MAFFT multiple sequence alignment software version 7: improvements in performance and usability. Mol Biol Evol 30:772-780. http://dx.doi.org/10.1093/molbev/mst010.
    • (2013) Mol Biol Evol , vol.30 , pp. 772-780
    • Katoh, K.1    Standley, D.M.2
  • 44
    • 84938099470 scopus 로고    scopus 로고
    • Primer ID validates template sampling depth and greatly reduces the error rate of nextgeneration sequencing of HIV-1 genomic RNA populations
    • Zhou S, Jones C, Mieczkowski P, Swanstrom R. 2015. Primer ID validates template sampling depth and greatly reduces the error rate of nextgeneration sequencing of HIV-1 genomic RNA populations. J Virol 89: 8540-8555. http://dx.doi.org/10.1128/JVI.00522-15.
    • (2015) J Virol , vol.89 , pp. 8540-8555
    • Zhou, S.1    Jones, C.2    Mieczkowski, P.3    Swanstrom, R.4
  • 47
    • 84923164032 scopus 로고    scopus 로고
    • Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env
    • Guttman M, Cupo A, Julien JP, Sanders RW, Wilson IA, Moore JP, Lee KK. 2015. Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env. Nat Commun 6:6144. http://dx.doi.org/10.1038/ncomms7144.
    • (2015) Nat Commun , vol.6 , pp. 6144
    • Guttman, M.1    Cupo, A.2    Julien, J.P.3    Sanders, R.W.4    Wilson, I.A.5    Moore, J.P.6    Lee, K.K.7
  • 51
    • 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 CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ. 1990. 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 265:10373-10382.
    • (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
  • 52
    • 0034687168 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells
    • Zhu X, Borchers C, Bienstock RJ, Tomer KB. 2000. Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells. Biochemistry 39:11194-11204. http://dx.doi.org/10.1021/bi000432m.
    • (2000) Biochemistry , vol.39 , pp. 11194-11204
    • Zhu, X.1    Borchers, C.2    Bienstock, R.J.3    Tomer, K.B.4
  • 53
    • 84874622598 scopus 로고    scopus 로고
    • Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins
    • Go EP, Liao HX, Alam SM, Hua D, Haynes BF, Desaire H. 2013. Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins. J Proteome Res 12: 1223-1234. http://dx.doi.org/10.1021/pr300870t.
    • (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
  • 56
    • 80052502584 scopus 로고    scopus 로고
    • Epitopes immediately below the base of the V3 loop of gp120 as targets for the initial autologous neutralizing antibody response in two HIV-1 sub-type B-infected individuals
    • Tang H, Robinson JE, Gnanakaran S, Li M, Rosenberg ES, Perez LG, Haynes BF, Liao HX, Labranche CC, Korber BT, Montefiori DC. 2011. Epitopes immediately below the base of the V3 loop of gp120 as targets for the initial autologous neutralizing antibody response in two HIV-1 sub-type B-infected individuals. J Virol 85:9286-9299. http://dx.doi.org/10.1128/JVI.02286-10.
    • (2011) J Virol , vol.85 , pp. 9286-9299
    • Tang, H.1    Robinson, J.E.2    Gnanakaran, S.3    Li, M.4    Rosenberg, E.S.5    Perez, L.G.6    Haynes, B.F.7    Liao, H.X.8    Labranche, C.C.9    Korber, B.T.10    Montefiori, D.C.11
  • 58
    • 16244419386 scopus 로고    scopus 로고
    • Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles
    • Gorny MK, Stamatatos L, Volsky B, Revesz K, Williams C, Wang XH, Cohen S, Staudinger R, Zolla-Pazner S. 2005. Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles. J Virol 79:5232-5237. http://dx.doi.org/10.1128/JVI.79.8.5232-5237.2005.
    • (2005) J Virol , vol.79 , pp. 5232-5237
    • Gorny, M.K.1    Stamatatos, L.2    Volsky, B.3    Revesz, K.4    Williams, C.5    Wang, X.H.6    Cohen, S.7    Staudinger, R.8    Zolla-Pazner, S.9
  • 61
    • 84879538530 scopus 로고    scopus 로고
    • Computational analysis of anti-HIV-1 antibody neutralization panel data to identify potential functional epitope residues
    • 10 June
    • West AP, Jr, Scharf L, Horwitz J, Klein F, Nussenzweig MC, Bjorkman PJ. 10 June 2013. Computational analysis of anti-HIV-1 antibody neutralization panel data to identify potential functional epitope residues. Proc Natl Acad Sci U S A http://dx.doi.org/10.1073/pnas.1309215110.
    • (2013) Proc Natl Acad Sci U S A
    • West, A.P.1    Scharf, L.2    Horwitz, J.3    Klein, F.4    Nussenzweig, M.C.5    Bjorkman, P.J.6
  • 69
    • 84925431182 scopus 로고    scopus 로고
    • HIV-1 fitness cost associated with escape from the VRC01 class of CD4 binding site neutralizing antibodies
    • Lynch RM, Wong P, Tran L, O'Dell S, Nason MC, Li Y, Wu X, Mascola JR. 2015. HIV-1 fitness cost associated with escape from the VRC01 class of CD4 binding site neutralizing antibodies. J Virol 89:4201-4213. http://dx.doi.org/10.1128/JVI.03608-14.
    • (2015) J Virol , vol.89 , pp. 4201-4213
    • Lynch, R.M.1    Wong, P.2    Tran, L.3    O'Dell, S.4    Nason, M.C.5    Li, Y.6    Wu, X.7    Mascola, J.R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.