메뉴 건너뛰기




Volumn 125, Issue 6, 2015, Pages 2271-2274

Honing a harder-hitting hammerhead improves broadly neutralizing antibody breadth and potency

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; NEUTRALIZING ANTIBODY; COMPLEMENTARITY DETERMINING REGION; GLYCOPROTEIN GP 160; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY;

EID: 84930387857     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI82057     Document Type: Review
Times cited : (3)

References (33)
  • 1
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science. 2009;326(5950): 285-289.
    • (2009) Science , vol.326 , Issue.5950 , pp. 285-289
    • Walker, L.M.1
  • 2
    • 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 MD, 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. 2009;83(14): 7337-7348.
    • (2009) J Virol , vol.83 , Issue.14 , pp. 7337-7348
    • Simek, M.D.1
  • 3
    • 84863774072 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses
    • Burton DR, Poignard P, Stanfield RL, Wilson IA. Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses. Science. 2012;337(6091): 183-186.
    • (2012) Science , vol.337 , Issue.6091 , pp. 183-186
    • Burton, D.R.1    Poignard, P.2    Stanfield, R.L.3    Wilson, I.A.4
  • 4
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: Identification, structures, and B cell ontogenies
    • Kwong PD, Mascola JR. Human antibodies that neutralize HIV-1: Identification, structures, and B cell ontogenies. Immunity. 2012;37(3): 412-425.
    • (2012) Immunity , vol.37 , Issue.3 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 5
    • 84926453015 scopus 로고    scopus 로고
    • Comprehensive antigenic map of a cleaved soluble HIV-1 envelope trimer
    • Derking R, et al. Comprehensive antigenic map of a cleaved soluble HIV-1 envelope trimer. PLoS Pathog. 2015;11(3): E1004767.
    • (2015) PLoS Pathog , vol.11 , Issue.3 , pp. e1004767
    • Derking, R.1
  • 6
    • 84879302728 scopus 로고    scopus 로고
    • HIV-1 neutralizing antibodies: Understanding nature's pathways
    • Mascola JR, Haynes BF. HIV-1 neutralizing antibodies: Understanding nature's pathways. Immunol Rev. 2013;254(1): 225-244.
    • (2013) Immunol Rev , vol.254 , Issue.1 , pp. 225-244
    • Mascola, J.R.1    Haynes, B.F.2
  • 7
    • 84898538468 scopus 로고    scopus 로고
    • Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection
    • Derdeyn CA, Moore PL, Morris L. Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection. Curr Opin HIV AIDS. 2014;9(3): 210-216.
    • (2014) Curr Opin HIV AIDS , vol.9 , Issue.3 , pp. 210-216
    • Derdeyn, C.A.1    Moore, P.L.2    Morris, L.3
  • 8
    • 84930389498 scopus 로고    scopus 로고
    • Redesigned HIV antibodies exhibit enhanced neutralizing potency and breadth
    • Willis JR, et al. Redesigned HIV antibodies exhibit enhanced neutralizing potency and breadth. J Clin Invest. 2015;125(6): 2523-2531.
    • (2015) J Clin Invest , vol.125 , Issue.6 , pp. 2523-2531
    • Willis, J.R.1
  • 9
    • 84922982202 scopus 로고    scopus 로고
    • Improving neutralization potency and breadth by combining broadly reactive HIV-1 antibodies targeting major neutralization epitopes
    • Kong R, et al. Improving neutralization potency and breadth by combining broadly reactive HIV-1 antibodies targeting major neutralization epitopes. J Virol. 2015;89(5): 2659-2671.
    • (2015) J Virol , vol.89 , Issue.5 , pp. 2659-2671
    • Kong, R.1
  • 10
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien JP, et al. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science. 2013;342(6165): 1477-1483.
    • (2013) Science , vol.342 , Issue.6165 , pp. 1477-1483
    • Julien, J.P.1
  • 11
    • 84909640954 scopus 로고    scopus 로고
    • Structure and immune recognition of trimeric pre-fusion HIV-1 Env
    • Pancera M, et al. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature. 2014;514(7523): 455-461.
    • (2014) Nature , vol.514 , Issue.7523 , pp. 455-461
    • Pancera, M.1
  • 12
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis D, et al. Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science. 2013;342(6165): 1484-1490.
    • (2013) Science , vol.342 , Issue.6165 , pp. 1484-1490
    • Lyumkis, D.1
  • 13
    • 84878618663 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein structure
    • Merk A, Subramaniam S. HIV-1 envelope glycoprotein structure. Curr Opin Struct Biol. 2013;23(2): 268-276.
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.2 , pp. 268-276
    • Merk, A.1    Subramaniam, S.2
  • 14
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/ V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, et al. Structure of HIV-1 gp120 V1/ V2 domain with broadly neutralizing antibody PG9. Nature. 2011;480(7377): 336-343.
    • (2011) Nature , vol.480 , Issue.7377 , pp. 336-343
    • McLellan, J.S.1
  • 15
    • 77954982131 scopus 로고    scopus 로고
    • Crystal structure of PG16 and chimeric dissection with somatically related PG9: Structure-function analysis of two quaternary- specific antibodies that effectively neutralize HIV-1
    • Pancera M, et al. Crystal structure of PG16 and chimeric dissection with somatically related PG9: Structure-function analysis of two quaternary- specific antibodies that effectively neutralize HIV-1. J Virol. 2010;84(16): 8098-8110.
    • (2010) J Virol , vol.84 , Issue.16 , pp. 8098-8110
    • Pancera, M.1
  • 16
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker LM, et al. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature. 2011;477(7365): 466-470.
    • (2011) Nature , vol.477 , Issue.7365 , pp. 466-470
    • Walker, L.M.1
  • 17
    • 0028865465 scopus 로고
    • Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG
    • Trkola A, et al. Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG. J Virol. 1995;69(11): 6609-6617.
    • (1995) J Virol , vol.69 , Issue.11 , pp. 6609-6617
    • Trkola, A.1
  • 18
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X, et al. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science. 2010;329(5993): 856-861.
    • (2010) Science , vol.329 , Issue.5993 , pp. 856-861
    • Wu, X.1
  • 19
    • 84866493348 scopus 로고    scopus 로고
    • Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    • Huang J, et al. Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature. 2012;491(7424): 406-412.
    • (2012) Nature , vol.491 , Issue.7424 , pp. 406-412
    • Huang, J.1
  • 20
    • 84900467984 scopus 로고    scopus 로고
    • Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers
    • Blattner C, et al. Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity. 2014;40(5): 669-680.
    • (2014) Immunity , vol.40 , Issue.5 , pp. 669-680
    • Blattner, C.1
  • 21
    • 84899909771 scopus 로고    scopus 로고
    • Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike
    • Scharf L, et al. Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike. Cell Rep. 2014;7(3): 785-795.
    • (2014) Cell Rep , vol.7 , Issue.3 , pp. 785-795
    • Scharf, L.1
  • 22
    • 84921607768 scopus 로고    scopus 로고
    • Broad and potent HIV-1 neutralization by a human antibody that binds the gp41- gp120 interface
    • Huang J, et al. Broad and potent HIV-1 neutralization by a human antibody that binds the gp41- gp120 interface. Nature. 2014;515(7525): 138-142.
    • (2014) Nature , vol.515 , Issue.7525 , pp. 138-142
    • Huang, J.1
  • 23
    • 84055181327 scopus 로고    scopus 로고
    • Rapid development of glycanspecific, broad, and potent anti-HIV-1 gp120 neutralizing antibodies in an R5 SIV/HIV chimeric virus infected macaque
    • Walker LM, et al. Rapid development of glycanspecific, broad, and potent anti-HIV-1 gp120 neutralizing antibodies in an R5 SIV/HIV chimeric virus infected macaque. Proc Natl Acad Sci U S A. 2011;108(50): 20125-20129.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.50 , pp. 20125-20129
    • Walker, L.M.1
  • 24
  • 25
    • 84875759341 scopus 로고    scopus 로고
    • Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization
    • Klein F, et al. Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell. 2013;153(1): 126-138.
    • (2013) Cell , vol.153 , Issue.1 , pp. 126-138
    • Klein, F.1
  • 26
    • 77954912140 scopus 로고    scopus 로고
    • Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1
    • Pejchal R, et al. Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1. Proc Natl Acad Sci U S A. 2010;107(25): 11483-11488.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.25 , pp. 11483-11488
    • Pejchal, R.1
  • 27
    • 84860706280 scopus 로고    scopus 로고
    • Human peripheral blood antibodies with long HCDR3s are established primarily at original recombination using a limited subset of germline genes
    • Briney BS, Willis JR, Crowe JE Jr. Human peripheral blood antibodies with long HCDR3s are established primarily at original recombination using a limited subset of germline genes. PLoS One. 2012;7(5): E36750.
    • (2012) PLoS One , vol.7 , Issue.5 , pp. e36750
    • Briney, B.S.1    Willis, J.R.2    Crowe, J.E.3
  • 28
    • 84875034460 scopus 로고    scopus 로고
    • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9
    • Julien JP, et al. Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. Proc Natl Acad Sci U S A. 2013;110(11): 4351-4356.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.11 , pp. 4351-4356
    • Julien, J.P.1
  • 29
    • 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 JP, 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. 2013;9(5): E1003342.
    • (2013) PLoS Pathog , vol.9 , Issue.5 , pp. e1003342
    • Julien, J.P.1
  • 30
    • 50649095790 scopus 로고    scopus 로고
    • Macromolecular modeling with rosetta
    • Das R, Baker D. Macromolecular modeling with rosetta. Annu Rev Biochem. 2008;77: 363-382.
    • (2008) Annu Rev Biochem , vol.77 , pp. 363-382
    • Das, R.1    Baker, D.2
  • 31
    • 84899991983 scopus 로고    scopus 로고
    • Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
    • Doria-Rose NA, et al. Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies. Nature. 2014;509(7498): 55-62.
    • (2014) Nature , vol.509 , Issue.7498 , pp. 55-62
    • Doria-Rose, N.A.1
  • 32
    • 84929247213 scopus 로고    scopus 로고
    • Immune system regulation in the induction of broadly neutralizing HIV-1 antibodies
    • Kelsoe G, Verkoczy L, Haynes BF. Immune system regulation in the induction of broadly neutralizing HIV-1 antibodies. Vaccines (Basel). 2014;2(1): 1-14.
    • (2014) Vaccines (Basel , vol.2 , Issue.1 , pp. 1-14
    • Kelsoe, G.1    Verkoczy, L.2    Haynes, B.F.3
  • 33
    • 84919430580 scopus 로고    scopus 로고
    • Polyreactivity and autoreactivity among HIV-1 antibodies
    • Liu M, et al. Polyreactivity and autoreactivity among HIV-1 antibodies. J Virol. 2015;89(1): 784-798.
    • (2015) J Virol , vol.89 , Issue.1 , pp. 784-798
    • Liu, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.