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Volumn 89, Issue 2, 2015, Pages 1105-1118

Two classes of broadly neutralizing antibodies within a single lineage directed to the high-mannose patch of HIV envelope

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BROADLY NEUTRALIZING ANTIBODY; ENVELOPE PROTEIN; ENVELOPE PROTEIN HIGH MANNOSE PATCH; EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; MANNOSE; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

EID: 84920771783     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02905-14     Document Type: Article
Times cited : (75)

References (47)
  • 4
    • 77958115264 scopus 로고    scopus 로고
    • A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals
    • Walker LM, Simek MD, Priddy F, Gach JS, Wagner D, Zwick MB, Phogat SK, Poignard P, Burton DR. 2010. A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals. PLoS Pathog 6:e1001028. http://dx.doi.org/10.1371/journal.ppat.1001028.
    • (2010) PLoS Pathog , vol.6
    • 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
  • 8
    • 80051677678 scopus 로고    scopus 로고
    • The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade
    • Bonomelli C, Doores KJ, Dunlop DC, Thaney V, Dwek RA, Burton DR, Crispin M, Scanlan CN. 2011. The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade. PLoS One 6:e23521. http://dx.doi.org/10.1371/journal.pone.0023521.
    • (2011) PLoS One , vol.6
    • Bonomelli, C.1    Doores, K.J.2    Dunlop, D.C.3    Thaney, V.4    Dwek, R.A.5    Burton, D.R.6    Crispin, M.7    Scanlan, C.N.8
  • 10
    • 0023811767 scopus 로고
    • Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120
    • Geyer H, Holschbach C, Hunsmann G, Schneider J. 1988. Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120. J Biol Chem 263:11760-11767.
    • (1988) J Biol Chem , vol.263 , pp. 11760-11767
    • Geyer, H.1    Holschbach, C.2    Hunsmann, G.3    Schneider, J.4
  • 11
    • 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
  • 12
    • 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
  • 22
    • 63149142646 scopus 로고    scopus 로고
    • B cells in HIV infection and disease
    • Moir S, Fauci AS. 2009. B cells in HIV infection and disease. Nat Rev Immunol 9:235-245. http://dx.doi.org/10.1038/nri2524.
    • (2009) Nat Rev Immunol , vol.9 , pp. 235-245
    • Moir, S.1    Fauci, A.S.2
  • 23
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores KJ, Burton DR. 2010. Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J Virol 84:10510-10521. http://dx.doi.org/10.1128/JVI.00552-10.
    • (2010) J Virol , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 24
    • 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
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326. http://dx.doi.org/10.1016/S0076-6879(97)76066-X.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 84896690177 scopus 로고    scopus 로고
    • Diverse recombinant HIV-1 Envs fail to activate B cells expressing the germline B cell receptors of the broadly neutralizing anti-HIV-1 antibodies PG9 and 447-52D
    • McGuire AT, Glenn JA, Lippy A, Stamatatos L. 2014. Diverse recombinant HIV-1 Envs fail to activate B cells expressing the germline B cell receptors of the broadly neutralizing anti-HIV-1 antibodies PG9 and 447-52D. J Virol 88:2645-2657. http://dx.doi.org/10.1128/JVI.03228-13.
    • (2014) J Virol , vol.88 , pp. 2645-2657
    • McGuire, A.T.1    Glenn, J.A.2    Lippy, A.3    Stamatatos, L.4
  • 34
    • 70449701456 scopus 로고    scopus 로고
    • Germline-like predecessors of broadly neutralizing antibodies lack measurable binding to HIV-1 envelope glycoproteins: implications for evasion of immune responses and design of vaccine immunogens
    • Xiao X, Chen W, Feng Y, Zhu Z, Prabakaran P, Wang Y, Zhang MY, Longo NS, Dimitrov DS. 2009. Germline-like predecessors of broadly neutralizing antibodies lack measurable binding to HIV-1 envelope glycoproteins: implications for evasion of immune responses and design of vaccine immunogens. Biochem Biophys Res Commun 390:404-409. http://dx.doi.org/10.1016/j.bbrc.2009.09.029.
    • (2009) Biochem Biophys Res Commun , vol.390 , pp. 404-409
    • Xiao, X.1    Chen, W.2    Feng, Y.3    Zhu, Z.4    Prabakaran, P.5    Wang, Y.6    Zhang, M.Y.7    Longo, N.S.8    Dimitrov, D.S.9
  • 35
    • 77957201600 scopus 로고    scopus 로고
    • Very few substitutions in a germ line antibody are required to initiate significant domain exchange
    • Huber M, Le KM, Doores KJ, Fulton Z, Stanfield RL, Wilson IA, Burton DR. 2010. Very few substitutions in a germ line antibody are required to initiate significant domain exchange. J Virol 84:10700-10707. http://dx.doi.org/10.1128/JVI.01111-10.
    • (2010) J Virol , vol.84 , pp. 10700-10707
    • Huber, M.1    Le, K.M.2    Doores, K.J.3    Fulton, Z.4    Stanfield, R.L.5    Wilson, I.A.6    Burton, D.R.7
  • 36
    • 84904327067 scopus 로고    scopus 로고
    • Conservation, compensation, and evolution of Nlinked glycans in the HIV-1 group M subtypes and circulating recombinant forms
    • 823605
    • Travers SA. 2012. Conservation, compensation, and evolution of Nlinked glycans in the HIV-1 group M subtypes and circulating recombinant forms. ISRN AIDS 2012:823605. http://dx.doi.org/10.5402/2012/823605.
    • (2012) ISRN AIDS , vol.2012
    • Travers, S.A.1
  • 38
    • 0030589039 scopus 로고    scopus 로고
    • Structural families in loops of homologous proteins: automatic classification, modelling and application to antibodies
    • Martin AC, Thornton JM. 1996. Structural families in loops of homologous proteins: automatic classification, modelling and application to antibodies. J Mol Biol 263:800-815. http://dx.doi.org/10.1006/jmbi.1996.0617.
    • (1996) J Mol Biol , vol.263 , pp. 800-815
    • Martin, A.C.1    Thornton, J.M.2
  • 39
    • 84879302728 scopus 로고    scopus 로고
    • HIV-1 neutralizing antibodies: understanding nature's pathways
    • Mascola JR, Haynes BF. 2013. HIV-1 neutralizing antibodies: understanding nature's pathways. Immunol Rev 254:225-244. http://dx.doi.org/10.1111/imr.12075.
    • (2013) Immunol Rev , vol.254 , pp. 225-244
    • Mascola, J.R.1    Haynes, B.F.2
  • 42
    • 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
  • 47
    • 84894173514 scopus 로고    scopus 로고
    • Structural insights on the role of antibodies in HIV-1 vaccine and therapy
    • West AP, Jr, Scharf L, Scheid JF, Klein F, Bjorkman PJ, Nussenzweig MC. 2014. Structural insights on the role of antibodies in HIV-1 vaccine and therapy. Cell 156:633-648. http://dx.doi.org/10.1016/j.cell.2014.01.052.
    • (2014) Cell , vol.156 , pp. 633-648
    • West, A.P.1    Scharf, L.2    Scheid, J.F.3    Klein, F.4    Bjorkman, P.J.5    Nussenzweig, M.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.