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Volumn 67, Issue , 2016, Pages 185-200

Broadly neutralizing antibodies against HIV: New insights to inform vaccine design

Author keywords

B cells; Broadly neutralizing antibodies; Env; HIV vaccine

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS VACCINE; NEUTRALIZING ANTIBODY; EPITOPE; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 84954553168     PISSN: 00664219     EISSN: 1545326X     Source Type: Book Series    
DOI: 10.1146/annurev-med-091014-090749     Document Type: Article
Times cited : (33)

References (88)
  • 1
    • 85158921979 scopus 로고    scopus 로고
    • Vaccine immunology
    • ed. SA Plotkin, WA Orenstein, PA Offit,. Philadelphia: Elsevier Saunders. 5th e.d
    • Siegrist CA. (2008). Vaccine immunology. Vaccines, ed. SA Plotkin, WA Orenstein, PA Offit, pp. 17-36. Philadelphia: Elsevier Saunders. 5th e.d
    • (2008) Vaccines , pp. 17-36
    • Siegrist, C.A.1
  • 2
    • 29444442970 scopus 로고    scopus 로고
    • Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection
    • Frost SDW, Wrin T, Smith DM, et al. (2005). Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection. PNAS 102(51): 18514-19
    • (2005) PNAS , vol.102 , Issue.51 , pp. 18514-18519
    • Frost, S.D.W.1    Wrin, T.2    Smith, D.M.3
  • 3
    • 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(1): 225-44
    • (2013) Immunol. Rev , vol.254 , Issue.1 , pp. 225-244
    • Mascola, J.R.1    Haynes, B.F.2
  • 4
    • 37549036732 scopus 로고    scopus 로고
    • Fc? Receptors as regulators of immune responses
    • Nimmerjahn F, Ravetch J. (2007). Fc? receptors as regulators of immune responses. Nat. Rev. Immunol. 8: 34-47
    • (2007) Nat. Rev. Immunol , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.2
  • 5
    • 80051737642 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein biosyn thesis, trafficking, and incorporation
    • Checkley MA, Luttge BG, Freed EO. (2011). HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation. J. Mol. Biol. 410(4): 582-608
    • (2011) J. Mol. Biol , vol.410 , Issue.4 , pp. 582-608
    • Checkley, M.A.1    Luttge, B.G.2    Freed, E.O.3
  • 6
    • 0031301825 scopus 로고    scopus 로고
    • Dynamics of HIV-1 and CD4+ lymphocytes in vivo
    • Suppl. A
    • Perelson AS, Essunger P, Ho DD. (1997). Dynamics of HIV-1 and CD4+ lymphocytes in vivo. AIDS 11(Suppl. A): S17-S24
    • (1997) AIDS , vol.11 , pp. S17-S24
    • Perelson, A.S.1    Essunger, P.2    Ho, D.D.3
  • 7
    • 0029967721 scopus 로고    scopus 로고
    • HIV-1 dynamics in vivo: Virion clearance rate, infected cell life-span, and viral generation time
    • Perelson AS, Neumann AU, Markowitz M, et al. (1996). HIV-1 dynamics in vivo: virion clearance rate, infected cell life-span, and viral generation time. Science 271(5255): 1582-86
    • (1996) Science , vol.271 , Issue.5255 , pp. 1582-1586
    • Perelson, A.S.1    Neumann, A.U.2    Markowitz, M.3
  • 8
    • 84898548356 scopus 로고    scopus 로고
    • Immunogen design to focus the B-cell repertoire
    • Sattentau QJ. (2014). Immunogen design to focus the B-cell repertoire. Curr. Opin. HIV AIDS 9(3): 217-23
    • (2014) Curr. Opin. HIV AIDS , vol.9 , Issue.3 , pp. 217-223
    • Sattentau, Q.J.1
  • 9
    • 84891799642 scopus 로고    scopus 로고
    • BNAber: Database of broadly neutralizing HIV antibodies
    • Database issue
    • Eroshkin AM, LeBlanc A, Weekes D, et al. (2014). BNAber: database of broadly neutralizing HIV antibodies. Nucleic Acids Res. 42(Database issue): D1133-39
    • (2014) Nucleic Acids Res , vol.42 , pp. D1133-D1139
    • Eroshkin, A.M.1    LeBlanc, A.2    Weekes, D.3
  • 10
    • 84899909771 scopus 로고    scopus 로고
    • Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike
    • Scharf L, Scheid JF, Lee JH, et al. (2014). Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike. Cell Rep. 7(3): 785-95
    • (2014) Cell Rep , vol.7 , Issue.3 , pp. 785-795
    • Scharf, L.1    Scheid, J.F.2    Lee, J.H.3
  • 11
    • 84921607768 scopus 로고    scopus 로고
    • Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface
    • Huang J, Kang BH, Pancera M, et al. (2014). Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface. Nature 515(7525): 138-42
    • (2014) Nature , vol.515 , Issue.7525 , pp. 138-142
    • Huang, J.1    Kang, B.H.2    Pancera, M.3
  • 12
    • 84875759341 scopus 로고    scopus 로고
    • Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization
    • Klein F, Diskin R, Scheid JF, et al. (2013). Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell 153(1): 126-38
    • (2013) Cell , vol.153 , Issue.1 , pp. 126-138
    • Klein, F.1    Diskin, R.2    Scheid, J.F.3
  • 13
    • 77957355961 scopus 로고    scopus 로고
    • Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation
    • Mouquet H, Scheid JF, Zoller MJ, et al. (2010). Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation. Nature 467(7315): 591-95
    • (2010) Nature , vol.467 , Issue.7315 , pp. 591-595
    • Mouquet, H.1    Scheid, J.F.2    Zoller, M.J.3
  • 14
    • 84937761089 scopus 로고    scopus 로고
    • Maturation and diversity of the VRC01-Antibody lineage over 15 years of chronic HIV-1 infection
    • Wu X, Zhang Z, Schramm CA, et al. (2015). Maturation and diversity of the VRC01-Antibody lineage over 15 years of chronic HIV-1 infection. Cell 161(3): 470-85
    • (2015) Cell , vol.161 , Issue.3 , pp. 470-485
    • Wu, X.1    Zhang, Z.2    Schramm, C.A.3
  • 15
    • 84866949036 scopus 로고    scopus 로고
    • Structural and genetic basis for development of broadly neutralizing influenza antibodies
    • Lingwood D, McTamney PM, Yassine HM, et al. (2012). Structural and genetic basis for development of broadly neutralizing influenza antibodies. Nature 489(7417): 566-70
    • (2012) Nature , vol.489 , Issue.7417 , pp. 566-570
    • Lingwood, D.1    McTamney, P.M.2    Yassine, H.M.3
  • 16
    • 84928485677 scopus 로고    scopus 로고
    • Ability to develop broadly neutralizing HIV-1 antibodies is not restricted by the germline Ig gene repertoire
    • Scheepers C, Shrestha RK, Lambson BE, et al. (2015). Ability to develop broadly neutralizing HIV-1 antibodies is not restricted by the germline Ig gene repertoire. J. Immunol. 194: 4371-78
    • (2015) J. Immunol , vol.194 , pp. 4371-4378
    • Scheepers, C.1    Shrestha, R.K.2    Lambson, B.E.3
  • 17
    • 79960220935 scopus 로고    scopus 로고
    • AID targeting in antibody diversity
    • Pavri R, Nussenzweig MC. (2011). AID targeting in antibody diversity. Adv. Immunol. 110: 1-26
    • (2011) Adv. Immunol , vol.110 , pp. 1-26
    • Pavri, R.1    Nussenzweig, M.C.2
  • 18
    • 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, et al. (2013). The effects of somatic hypermutation on neutralization and binding in the PGT121 family of broadly neutralizing HIV antibodies. PLoS Pathog. 9(11): e1003754
    • (2013) PLoS Pathog , vol.9 , Issue.11 , pp. e1003754
    • Sok, D.1    Laserson, U.2    Laserson, J.3
  • 19
    • 80555154835 scopus 로고    scopus 로고
    • HIV-1 N-glycan composition governs a balance between dendritic cell-mediated viral transmission and antigen presentation
    • vanMontfort T, Eggink D, Boot M, et al. (2011). HIV-1 N-glycan composition governs a balance between dendritic cell-mediated viral transmission and antigen presentation. J. Immunol. 187(9): 4676-85
    • (2011) J. Immunol , vol.187 , Issue.9 , pp. 4676-4685
    • Van Montfort, T.1    Eggink, D.2    Boot, M.3
  • 20
    • 79953316880 scopus 로고    scopus 로고
    • Comparison of antibody repertoires produced by HIV-1 infection, other chronic and acute infections, and systemic autoimmune disease
    • Breden F, Lepik C, Longo NS, et al. (2011). Comparison of antibody repertoires produced by HIV-1 infection, other chronic and acute infections, and systemic autoimmune disease. PLoS ONE 6(3): e16857
    • (2011) PLoS ONE , vol.6 , Issue.3 , pp. e16857
    • Breden, F.1    Lepik, C.2    Longo, N.S.3
  • 21
    • 84922479607 scopus 로고    scopus 로고
    • Recent strategies targeting HIV glycans in vaccine design
    • Horiya S, MacPherson IS, Krauss IJ. (2014). Recent strategies targeting HIV glycans in vaccine design. Nat. Chem. Biol. 10(12): 990-99
    • (2014) Nat. Chem. Biol , vol.10 , Issue.12 , pp. 990-999
    • Horiya, S.1    MacPherson, I.S.2    Krauss, I.J.3
  • 22
    • 84893352067 scopus 로고    scopus 로고
    • Antibodies VRC01 and 10E8 neutralize HIV-1 with high breadth and potency even with Ig-framework regions substantially reverted to germline
    • Georgiev IS, Rudicell RS, Saunders KO, et al. (2014). Antibodies VRC01 and 10E8 neutralize HIV-1 with high breadth and potency even with Ig-framework regions substantially reverted to germline. J. Immunol. 192(3): 1100-6
    • (2014) J. Immunol , vol.192 , Issue.3 , pp. 1100-1106
    • Georgiev, I.S.1    Rudicell, R.S.2    Saunders, K.O.3
  • 23
    • 0027212854 scopus 로고
    • Length distribution of CDRH3 in antibodies
    • Wu TT, Johnson G, Kabat EA. (1993). Length distribution of CDRH3 in antibodies. Proteins 16(1): 1-7
    • (1993) Proteins , vol.16 , Issue.1 , pp. 1-7
    • Wu, T.T.1    Johnson, G.2    Kabat, E.A.3
  • 24
    • 0020619874 scopus 로고
    • Neutralization of poliovirus by a monoclonal antibody: Kinetics and stoichiometry
    • Icenogle J, Shiwen H, Duke G, et al. (1983). Neutralization of poliovirus by a monoclonal antibody: kinetics and stoichiometry. Virology 127(2): 412-25
    • (1983) Virology , vol.127 , Issue.2 , pp. 412-425
    • Icenogle, J.1    Shiwen, H.2    Duke, G.3
  • 25
    • 84878821153 scopus 로고    scopus 로고
    • Reshaping antibody diversity
    • Wang F, Ekiert DC, Ahmad I, et al. (2013). Reshaping antibody diversity. Cell 153(6): 1379-93
    • (2013) Cell , vol.153 , Issue.6 , pp. 1379-1393
    • Wang, F.1    Ekiert, D.C.2    Ahmad, I.3
  • 26
    • 0030732117 scopus 로고    scopus 로고
    • Variations in the neutralizing and haemagglutinationinhibiting activities of five influenza A virus-specific IgGs and their antibody fragments
    • Schofield DJ, Stephenson JR, Dimmock NJ. (1997). Variations in the neutralizing and haemagglutinationinhibiting activities of five influenza A virus-specific IgGs and their antibody fragments. J. Gen. Virol. 78(Pt 10): 2431-39
    • (1997) J. Gen. Virol , vol.78 , pp. 2431-2439
    • Schofield, D.J.1    Stephenson, J.R.2    Dimmock, N.J.3
  • 27
    • 84922224963 scopus 로고    scopus 로고
    • Intra-spike crosslinking overcomes antibody evasion by HIV-1
    • Galimidi RP, Klein JS, Politzer MS, et al. (2015). Intra-spike crosslinking overcomes antibody evasion by HIV-1. Cell 160(3): 433-46
    • (2015) Cell , vol.160 , Issue.3 , pp. 433-446
    • Galimidi, R.P.1    Klein, J.S.2    Politzer, M.S.3
  • 28
    • 84863769888 scopus 로고    scopus 로고
    • The development of CD4 binding site antibodies during HIV-1 infection
    • Lynch RM, Tran L, Louder MK, et al. (2012). The development of CD4 binding site antibodies during HIV-1 infection. J. Virol. 86(14): 7588-95
    • (2012) J. Virol , vol.86 , Issue.14 , pp. 7588-7595
    • Lynch, R.M.1    Tran, L.2    Louder, M.K.3
  • 29
    • 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. (2012). Human peripheral blood antibodies with long HCDR3s are established primarily at original recombination using a limited subset of germline genes. PLoS ONE 7(5): e36750
    • (2012) PLoS ONE , vol.7 , Issue.5 , pp. e36750
    • Briney, B.S.1    Willis, J.R.2    Crowe, J.E.3
  • 30
    • 58149399396 scopus 로고    scopus 로고
    • Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies
    • Doria-Rose NA, Klein RM, Manion MM, et al. (2009). Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies. J. Virol. 83(1): 188-99
    • (2009) J. Virol , vol.83 , Issue.1 , pp. 188-199
    • Doria-Rose, N.A.1    Klein, R.M.2    Manion, M.M.3
  • 31
    • 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, et al. (2009). Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J. Virol. 83(2): 757-69
    • (2009) J. Virol , vol.83 , Issue.2 , pp. 757-769
    • Sather, D.N.1    Armann, J.2    Ching, L.K.3
  • 32
    • 84924559557 scopus 로고    scopus 로고
    • Bone marrow plasma cells are a primary source of serum HIV-1-specific antibodies in chronically infected individuals
    • Montezuma-Rusca JM, Moir S, Kardava L, et al. (2015). Bone marrow plasma cells are a primary source of serum HIV-1-specific antibodies in chronically infected individuals. J. Immunol. 194(6): 2561-68
    • (2015) J. Immunol , vol.194 , Issue.6 , pp. 2561-2568
    • Montezuma-Rusca, J.M.1    Moir, S.2    Kardava, L.3
  • 33
    • 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, Walker LM, Stanfield RL, et al. (2010). Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1. PNAS 107(25): 11483-88
    • (2010) PNAS , vol.107 , Issue.25 , pp. 11483-11488
    • Pejchal, R.1    Walker, L.M.2    Stanfield, R.L.3
  • 34
    • 39649084660 scopus 로고    scopus 로고
    • Plasma cell development: From B-cell subsets to long-Term survival niches
    • Fairfax KA, Kallies A, Nutt SL, et al. (2008). Plasma cell development: from B-cell subsets to long-Term survival niches. Semin. Immunol. 20(1): 49-58
    • (2008) Semin. Immunol , vol.20 , Issue.1 , pp. 49-58
    • Fairfax, K.A.1    Kallies, A.2    Nutt, S.L.3
  • 35
    • 63849131879 scopus 로고    scopus 로고
    • Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
    • Scheid JF, Mouquet H, Feldhahn N, et al. (2009). Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 458(7238): 636-40
    • (2009) Nature , vol.458 , Issue.7238 , pp. 636-640
    • Scheid, J.F.1    Mouquet, H.2    Feldhahn, N.3
  • 36
    • 21344434534 scopus 로고    scopus 로고
    • Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies
    • Haynes BF, Fleming J, St Clair EW, et al. (2005). Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science 308(5730): 1906-8
    • (2005) Science , vol.308 , Issue.5730 , pp. 1906-1908
    • Haynes, B.F.1    Fleming, J.2    St Clair, E.W.3
  • 37
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid JF, Mouquet H, Ueberheide B, et al. (2011). Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 333(6049): 1633-37
    • (2011) Science , vol.333 , Issue.6049 , pp. 1633-1637
    • Scheid, J.F.1    Mouquet, H.2    Ueberheide, B.3
  • 38
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, Phogat SK, Chan-Hui P-Y, et al. (2009). Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326(5950): 285-89
    • (2009) Science , vol.326 , Issue.5950 , pp. 285-289
    • Walker, L.M.1    Phogat, S.K.2    Chan-Hui, P.-Y.3
  • 39
    • 84919430580 scopus 로고    scopus 로고
    • Polyreactivity and autoreactivity among HIV-1 antibodies
    • Liu M, Yang G, Wiehe K, et al. (2015). Polyreactivity and autoreactivity among HIV-1 antibodies. J. Virol. 89(1): 784-98
    • (2015) J. Virol , vol.89 , Issue.1 , pp. 784-798
    • Liu, M.1    Yang, G.2    Wiehe, K.3
  • 40
    • 84884991510 scopus 로고    scopus 로고
    • Isolation of human monoclonal antibodies from peripheral blood B cells
    • Huang J, Doria-Rose NA, Longo NS, et al. (2013). Isolation of human monoclonal antibodies from peripheral blood B cells. Nat. Protoc. 8(10): 1907-15
    • (2013) Nat. Protoc , vol.8 , Issue.10 , pp. 1907-1915
    • Huang, J.1    Doria-Rose, N.A.2    Longo, N.S.3
  • 41
    • 84859717525 scopus 로고    scopus 로고
    • Germinal center selection and the development of memory B and plasma cells
    • Shlomchik MJ, Weisel F. (2012). Germinal center selection and the development of memory B and plasma cells. Immunol. Rev. 247(1): 52-63
    • (2012) Immunol. Rev , vol.247 , Issue.1 , pp. 52-63
    • Shlomchik, M.J.1    Weisel, F.2
  • 42
    • 76249083814 scopus 로고    scopus 로고
    • Autoreactivity in an HIV-1 broadly reactive neutralizing antibody variable region heavy chain induces immunologic tolerance
    • Verkoczy L, Diaz M, Holl TM, et al. (2010). Autoreactivity in an HIV-1 broadly reactive neutralizing antibody variable region heavy chain induces immunologic tolerance. PNAS 107(1): 181-86
    • (2010) PNAS , vol.107 , Issue.1 , pp. 181-186
    • Verkoczy, L.1    Diaz, M.2    Holl, T.M.3
  • 43
    • 80053529030 scopus 로고    scopus 로고
    • Rescue of HIV-1 broad neutralizing antibodyexpressing B cells in 2F5 VH'VL knockin mice reveals multiple tolerance controls
    • Verkoczy L, Chen Y, Bouton-Verville H, et al. (2011). Rescue of HIV-1 broad neutralizing antibodyexpressing B cells in 2F5 VH'VL knockin mice reveals multiple tolerance controls. J. Immunol. 187(7): 3785-97
    • (2011) J. Immunol , vol.187 , Issue.7 , pp. 3785-3797
    • Verkoczy, L.1    Chen, Y.2    Bouton-Verville, H.3
  • 44
    • 84880667257 scopus 로고    scopus 로고
    • Common tolerance mechanisms, but distinct cross-reactivities associated with gp41 and lipids, limit production of HIV-1 broad neutralizing antibodies 2F5 and 4E10
    • Chen Y, Zhang J, Hwang K-K, et al. (2013). Common tolerance mechanisms, but distinct cross-reactivities associated with gp41 and lipids, limit production of HIV-1 broad neutralizing antibodies 2F5 and 4E10. J. Immunol. 191(3): 1260-75
    • (2013) J. Immunol , vol.191 , Issue.3 , pp. 1260-1275
    • Chen, Y.1    Zhang, J.2    Hwang, K.-K.3
  • 45
    • 39649094515 scopus 로고    scopus 로고
    • Follicular dendritic cell networks of primary follicles and germinal centers: Phenotype and function
    • Allen CDC, Cyster JG. (2008). Follicular dendritic cell networks of primary follicles and germinal centers: phenotype and function. Semin. Immunol. 20(1): 14-25
    • (2008) Semin. Immunol , vol.20 , Issue.1 , pp. 14-25
    • Allen, C.D.C.1    Cyster, J.G.2
  • 46
    • 84919949772 scopus 로고    scopus 로고
    • HIV-1 envelope gp41 antibodies can originate from terminal ileum B cells that share cross-reactivity with commensal bacteria
    • Trama AM, Moody MA, Alam SM, et al. (2014). HIV-1 envelope gp41 antibodies can originate from terminal ileum B cells that share cross-reactivity with commensal bacteria. Cell HostMicrobe 16(2): 215-26
    • (2014) Cell HostMicrobe , vol.16 , Issue.2 , pp. 215-226
    • Trama, A.M.1    Moody, M.A.2    Alam, S.M.3
  • 47
    • 84861692916 scopus 로고    scopus 로고
    • B cell receptor signal transduction in the GC is shortcircuited by high phosphatase activity
    • Khalil AM, Cambier JC, Shlomchik MJ. (2012). B cell receptor signal transduction in the GC is shortcircuited by high phosphatase activity. Science 336(6085): 1178-81
    • (2012) Science , vol.336 , Issue.6085 , pp. 1178-1181
    • Khalil, A.M.1    Cambier, J.C.2    Shlomchik, M.J.3
  • 48
    • 0034255034 scopus 로고    scopus 로고
    • Energetics of the HIV gp120-CD4 binding reaction
    • Myszka DG, Sweet RW, Hensley P, et al. (2000). Energetics of the HIV gp120-CD4 binding reaction. PNAS 97(16): 9026-31
    • (2000) PNAS , vol.97 , Issue.16 , pp. 9026-9031
    • Myszka, D.G.1    Sweet, R.W.2    Hensley, P.3
  • 49
    • 84901644301 scopus 로고    scopus 로고
    • Clonal selection in the germinal centre by regulated proliferation and hypermutation
    • Gitlin AD, Shulman Z, Nussenzweig MC. (2014). Clonal selection in the germinal centre by regulated proliferation and hypermutation. Nature 509(7502): 637-40
    • (2014) Nature , vol.509 , Issue.7502 , pp. 637-640
    • Gitlin, A.D.1    Shulman, Z.2    Nussenzweig, M.C.3
  • 50
    • 0037069682 scopus 로고    scopus 로고
    • HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    • Kwong PD, Doyle ML, Casper DJ, et al. (2002). HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 420(6916): 678-82
    • (2002) Nature , vol.420 , Issue.6916 , pp. 678-682
    • Kwong, P.D.1    Doyle, M.L.2    Casper, D.J.3
  • 51
    • 70450182950 scopus 로고    scopus 로고
    • Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120
    • Chen L, Kwon YD, Zhou T, et al. (2009). Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science 326(5956): 1123-27
    • (2009) Science , vol.326 , Issue.5956 , pp. 1123-1127
    • Chen, L.1    Kwon, Y.D.2    Zhou, T.3
  • 52
    • 79952675131 scopus 로고    scopus 로고
    • Follicular helper CD4 T cells (TFH
    • Crotty S. (2011). Follicular helper CD4 T cells (TFH). Annu. Rev. Immunol. 29: 621-63
    • (2011) Annu. Rev. Immunol , vol.29 , pp. 621-663
    • Crotty, S.1
  • 53
    • 84876797103 scopus 로고    scopus 로고
    • Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
    • Liao H-X, Lynch R, Zhou T, et al. (2013). Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature 496(7446): 469-76
    • (2013) Nature , vol.496 , Issue.7446 , pp. 469-476
    • Liao, H.-X.1    Lynch, R.2    Zhou, T.3
  • 54
    • 84878257992 scopus 로고    scopus 로고
    • The good, the bad and the ugly-TFH cells in human health and disease
    • Tangye SG, Ma CS, Brink R, et al. (2013). The good, the bad and the ugly-TFH cells in human health and disease. Nat. Rev. Immunol. 13(6): 412-26
    • (2013) Nat. Rev. Immunol , vol.13 , Issue.6 , pp. 412-426
    • Tangye, S.G.1    Ma, C.S.2    Brink, R.3
  • 55
    • 84908148200 scopus 로고    scopus 로고
    • T follicular helper cell differentiation, function, and roles in disease
    • Crotty S. (2014). T follicular helper cell differentiation, function, and roles in disease. Immunity 41(4): 529-42
    • (2014) Immunity , vol.41 , Issue.4 , pp. 529-542
    • Crotty, S.1
  • 56
    • 84925236503 scopus 로고    scopus 로고
    • Independent evolution of Fc-And Fab-mediated HIV-1-specific antiviral antibody activity following acute infection
    • Dugast A-S, Stamatatos L, Tonelli A, et al. (2014). Independent evolution of Fc-And Fab-mediated HIV-1-specific antiviral antibody activity following acute infection. Eur. J. Immunol. 44: 2925-37
    • (2014) Eur. J. Immunol , vol.44 , pp. 2925-2937
    • Dugast, A.-S.1    Stamatatos, L.2    Tonelli, A.3
  • 57
    • 84908391100 scopus 로고    scopus 로고
    • Emergence of broadly neutralizing antibodies and viral coevolution in two subjects during the early stages of infection with human immunodeficiency virus type 1
    • Sather DN, Carbonetti S, Malherbe DC, et al. (2014). Emergence of broadly neutralizing antibodies and viral coevolution in two subjects during the early stages of infection with human immunodeficiency virus type 1. J. Virol. 88(22): 12968-81
    • (2014) J. Virol , vol.88 , Issue.22 , pp. 12968-12981
    • Sather, D.N.1    Carbonetti, S.2    Malherbe, D.C.3
  • 58
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1 V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, Pancera M, Carrico C, et al. (2011). Structure of HIV-1 gp120 V1 V2 domain with broadly neutralizing antibody PG9. Nature 480(7377): 336-43
    • (2011) Nature , vol.480 , Issue.7377 , pp. 336-343
    • McLellan, J.S.1    Pancera, M.2    Carrico, C.3
  • 59
    • 84906968862 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies suppress HIV in the persistent viral reservoir
    • Chun T-W, Murray D, Justement JS, et al. (2014). Broadly neutralizing antibodies suppress HIV in the persistent viral reservoir. PNAS 111(36): 13151-56
    • (2014) PNAS , vol.111 , Issue.36 , pp. 13151-13156
    • Chun, T.-W.1    Murray, D.2    Justement, J.S.3
  • 60
    • 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, et al. (2015). HIV-1 fitness cost associated with escape from the VRC01 class of CD4 binding site neutralizing antibodies. J. Virol. 89: 4201-13
    • (2015) J. Virol , vol.89 , pp. 4201-4213
    • Lynch, R.M.1    Wong, P.2    Tran, L.3
  • 61
    • 84904361849 scopus 로고    scopus 로고
    • Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains
    • Fera D, Schmidt AG, Haynes BF, et al. (2014). Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains. PNAS 111(28): 10275-80
    • (2014) PNAS , vol.111 , Issue.28 , pp. 10275-10280
    • Fera, D.1    Schmidt, A.G.2    Haynes, B.F.3
  • 62
    • 84899991983 scopus 로고    scopus 로고
    • Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
    • Doria-Rose NA, Schramm CA, Gorman J, et al. (2014). Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies. Nature 509(7498): 55-62
    • (2014) Nature , vol.509 , Issue.7498 , pp. 55-62
    • Doria-Rose, N.A.1    Schramm, C.A.2    Gorman, J.3
  • 63
    • 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, et al. (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(5): 2645-57
    • (2014) J. Virol , vol.88 , Issue.5 , pp. 2645-2657
    • McGuire, A.T.1    Glenn, J.A.2    Lippy, A.3
  • 64
    • 63749100579 scopus 로고    scopus 로고
    • A method for identification of HIV gp140 binding memory B cells in human blood
    • Scheid JF, Mouquet H, Feldhahn N, et al. (2009). A method for identification of HIV gp140 binding memory B cells in human blood. J. Immunol. Methods 343(2): 65-67
    • (2009) J. Immunol. Methods , vol.343 , Issue.2 , pp. 65-67
    • Scheid, J.F.1    Mouquet, H.2    Feldhahn, N.3
  • 65
    • 84878626061 scopus 로고    scopus 로고
    • Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies
    • McGuire AT, Hoot S, Dreyer AM, et al. (2013). Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies. J. Exp. Med. 210(4): 655-63
    • (2013) J. Exp. Med , vol.210 , Issue.4 , pp. 655-663
    • McGuire, A.T.1    Hoot, S.2    Dreyer, A.M.3
  • 66
    • 84907527916 scopus 로고    scopus 로고
    • Structural evolution of glycan recognition by a family of potent HIV antibodies
    • Garces F, Sok D, Kong L, et al. (2014). Structural evolution of glycan recognition by a family of potent HIV antibodies. Cell 159(1): 69-79
    • (2014) Cell , vol.159 , Issue.1 , pp. 69-79
    • Garces, F.1    Sok, D.2    Kong, L.3
  • 67
    • 84917691102 scopus 로고    scopus 로고
    • Antigen modification regulates competition of broad and narrow neutralizing HIV antibodies
    • McGuire AT, Dreyer AM, Carbonetti S, et al. (2014). Antigen modification regulates competition of broad and narrow neutralizing HIV antibodies. Science 346(6215): 1380-83
    • (2014) Science , vol.346 , Issue.6215 , pp. 1380-1383
    • McGuire, A.T.1    Dreyer, A.M.2    Carbonetti, S.3
  • 68
    • 0036333661 scopus 로고    scopus 로고
    • Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1
    • Sanders RW, Vesanen M, Schuelke N, et al. (2002). Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J. Virol. 76(17): 8875-89
    • (2002) J. Virol , vol.76 , Issue.17 , pp. 8875-8889
    • Sanders, R.W.1    Vesanen, M.2    Schuelke, N.3
  • 69
    • 79960974710 scopus 로고    scopus 로고
    • Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures
    • Harris A, Borgnia MJ, Shi D, et al. (2011). Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures. PNAS 108(28): 11440-45
    • (2011) PNAS , vol.108 , Issue.28 , pp. 11440-11445
    • Harris, A.1    Borgnia, M.J.2    Shi, D.3
  • 70
    • 21644445378 scopus 로고    scopus 로고
    • Evaluating the immunogenicity of a disulfide-stabilized, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1
    • Beddows S, Schulke N, Kirschner M, et al. (2005). Evaluating the immunogenicity of a disulfide-stabilized, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J. Virol. 79(14): 8812-27
    • (2005) J. Virol , vol.79 , Issue.14 , pp. 8812-8827
    • Beddows, S.1    Schulke, N.2    Kirschner, M.3
  • 71
    • 84884678235 scopus 로고    scopus 로고
    • A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies
    • Sanders RW, Derking R, Cupo A, et al. (2013). A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies. PLoS Pathog. 9(9): e1003618
    • (2013) PLoS Pathog , vol.9 , Issue.9 , pp. e1003618
    • Sanders, R.W.1    Derking, R.2    Cupo, A.3
  • 72
    • 84928583366 scopus 로고    scopus 로고
    • Cleavage-independentHIV-1 Env trimers engineered as soluble native spike mimetics for vaccine design
    • Sharma SK, de Val N, Bale S, et al. (2015). Cleavage-independentHIV-1 Env trimers engineered as soluble native spike mimetics for vaccine design. Cell Rep. 11(4): 539-50
    • (2015) Cell Rep , vol.11 , Issue.4 , pp. 539-550
    • Sharma, S.K.1    De Val, N.2    Bale, S.3
  • 73
    • 34548577658 scopus 로고    scopus 로고
    • A comparative immunogenicity study of HIV-1 virus-like particles bearing various forms of envelope proteins, particles bearing no envelope and solublemonomeric gp120
    • Crooks ET, Moore PL, Franti M, et al. (2007). A comparative immunogenicity study of HIV-1 virus-like particles bearing various forms of envelope proteins, particles bearing no envelope and solublemonomeric gp120. Virology 366(2): 245-62
    • (2007) Virology , vol.366 , Issue.2 , pp. 245-262
    • Crooks, E.T.1    Moore, P.L.2    Franti, M.3
  • 74
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected
    • Crooks ET, Tong T, Osawa K, et al. (2011). Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected. J. Virol. 85(12): 5825-39
    • (2011) J. Virol , vol.85 , Issue.12 , pp. 5825-5839
    • Crooks, E.T.1    Tong, T.2    Osawa, K.3
  • 75
    • 84901653387 scopus 로고    scopus 로고
    • HIV-1 envelope gp41 broadly neutralizing antibodies: Hurdles for vaccine development
    • Verkoczy L, Kelsoe G, Haynes BF. (2014). HIV-1 envelope gp41 broadly neutralizing antibodies: hurdles for vaccine development. PLoS Pathog. 10(5): e1004073
    • (2014) PLoS Pathog , vol.10 , Issue.5 , pp. e1004073
    • Verkoczy, L.1    Kelsoe, G.2    Haynes, B.F.3
  • 76
    • 84922225958 scopus 로고    scopus 로고
    • Rapid development of broadly influenza neutralizing antibodies through redundant mutations
    • Pappas L, Foglierini M, Piccoli L, et al. (2014). Rapid development of broadly influenza neutralizing antibodies through redundant mutations. Nature 516(7531): 418-22
    • (2014) Nature , vol.516 , Issue.7531 , pp. 418-422
    • Pappas, L.1    Foglierini, M.2    Piccoli, L.3
  • 77
    • 84877609579 scopus 로고    scopus 로고
    • Rational HIV immunogen design to target specific germline B cell receptors
    • Jardine J, Julien J-P, Menis S, et al. (2013). Rational HIV immunogen design to target specific germline B cell receptors. Science 340(6133): 711-16
    • (2013) Science , vol.340 , Issue.6133 , pp. 711-716
    • Jardine, J.1    Julien, J.-P.2    Menis, S.3
  • 78
    • 84865997747 scopus 로고    scopus 로고
    • Expansion of HIV-specific T follicular helper cells in chronic HIV infection
    • Lindqvist M, van Lunzen J, Soghoian DZ, et al. (2012). Expansion of HIV-specific T follicular helper cells in chronic HIV infection. J. Clin. Invest. 122(9): 3271-80
    • (2012) J. Clin. Invest , vol.122 , Issue.9 , pp. 3271-3280
    • Lindqvist, M.1    Van Lunzen, J.2    Soghoian, D.Z.3
  • 79
    • 84874519282 scopus 로고    scopus 로고
    • Follicular helper T cells serve as the major CD4 T cell compartment for HIV-1 infection, replication, and production
    • Perreau M, Savoye A-L, De Crignis E, et al. (2013). Follicular helper T cells serve as the major CD4 T cell compartment for HIV-1 infection, replication, and production. J. Exp. Med. 210(1): 143-56
    • (2013) J. Exp. Med , vol.210 , Issue.1 , pp. 143-156
    • Perreau, M.1    Savoye, A.-L.2    De Crignis, E.3
  • 80
    • 84885743368 scopus 로고    scopus 로고
    • Human circulating PD-1+CXCR3-CXCR5+memory Tfh cells are highly functional and correlate with broadly neutralizing HIV antibody responses
    • Locci M, Havenar-Daughton C, Landais E, et al. (2013). Human circulating PD-1+CXCR3-CXCR5+memory Tfh cells are highly functional and correlate with broadly neutralizing HIV antibody responses. Immunity 39(4): 758-69
    • (2013) Immunity , vol.39 , Issue.4 , pp. 758-769
    • Locci, M.1    Havenar-Daughton, C.2    Landais, E.3
  • 81
    • 84908377312 scopus 로고    scopus 로고
    • Early preservation of CXCR5+ PD-1+ helper T cells and B cell activation predict the breadth of neutralizing antibody responses in chronic HIV-1 infection
    • Cohen K, Altfeld M, Alter G, et al. (2014). Early preservation of CXCR5+ PD-1+ helper T cells and B cell activation predict the breadth of neutralizing antibody responses in chronic HIV-1 infection. J. Virol. 88(22): 13310-21
    • (2014) J. Virol , vol.88 , Issue.22 , pp. 13310-13321
    • Cohen, K.1    Altfeld, M.2    Alter, G.3
  • 82
    • 84907200998 scopus 로고    scopus 로고
    • Circulating CXCR5+PD-1+ response predicts influenza vaccine antibody responses in young adults but not elderly adults
    • Herati RS, Reuter MA, Dolfi DV, et al. (2014). Circulating CXCR5+PD-1+ response predicts influenza vaccine antibody responses in young adults but not elderly adults. J. Immunol. 193(7): 3528-37
    • (2014) J. Immunol , vol.193 , Issue.7 , pp. 3528-3537
    • Herati, R.S.1    Reuter, M.A.2    Dolfi, D.V.3
  • 83
    • 77149142640 scopus 로고    scopus 로고
    • IL-21 regulates germinal center B cell differentiation and proliferation through a B cell-intrinsic mechanism
    • Zotos D, Coquet JM, Zhang Y, et al. (2010). IL-21 regulates germinal center B cell differentiation and proliferation through a B cell-intrinsic mechanism. J. Exp. Med. 207(2): 365-78
    • (2010) J. Exp. Med , vol.207 , Issue.2 , pp. 365-378
    • Zotos, D.1    Coquet, J.M.2    Zhang, Y.3
  • 84
    • 70450265288 scopus 로고    scopus 로고
    • Early commitment of naïve human CD4+ T cells to the T follicular helper (TFH) cell lineage is induced by IL-12
    • Ma CS, Suryani S, Avery DT, et al. (2009). Early commitment of naïve human CD4+ T cells to the T follicular helper (TFH) cell lineage is induced by IL-12. Immunol. Cell Biol. 87(8): 590-600
    • (2009) Immunol. Cell Biol , vol.87 , Issue.8 , pp. 590-600
    • Ma, C.S.1    Suryani, S.2    Avery, D.T.3
  • 85
    • 18844447818 scopus 로고    scopus 로고
    • The role of April and BAFF in lymphocyte activation
    • Schneider P. (2005). The role of APRIL and BAFF in lymphocyte activation. Curr. Opin. Immunol. 17(3): 282-89
    • (2005) Curr. Opin. Immunol , vol.17 , Issue.3 , pp. 282-289
    • Schneider, P.1
  • 86
    • 84892546134 scopus 로고    scopus 로고
    • Local BLyS production by T follicular cells mediates retention of high affinity B cells during affinity maturation
    • Goenka R, Matthews AH, Zhang B, et al. (2014). Local BLyS production by T follicular cells mediates retention of high affinity B cells during affinity maturation. J. Exp. Med. 211(1): 45-56
    • (2014) J. Exp. Med , vol.211 , Issue.1 , pp. 45-56
    • Goenka, R.1    Matthews, A.H.2    Zhang, B.3
  • 87
    • 84879492157 scopus 로고    scopus 로고
    • An HIV-1 envelope glycoprotein trimer with an embedded IL-21 domain activates human B cells
    • Isik G, Chung NPY, van Montfort T, et al. (2013). An HIV-1 envelope glycoprotein trimer with an embedded IL-21 domain activates human B cells. PLoS ONE 8(6): e67309
    • (2013) PLoS ONE , vol.8 , Issue.6 , pp. e67309
    • Isik, G.1    Chung, N.P.Y.2    Van Montfort, T.3
  • 88
    • 84929636240 scopus 로고    scopus 로고
    • DNA vaccine molecular adjuvants SP-D-BAFF and SP-DAPRIL enhance anti-gp120 immune response and increase HIV-1 neutralizing antibody titers
    • Gupta S, Clark ES, Termini JM, et al. (2015). DNA vaccine molecular adjuvants SP-D-BAFF and SP-DAPRIL enhance anti-gp120 immune response and increase HIV-1 neutralizing antibody titers. J. Virol. 89(8): 4158-69
    • (2015) J. Virol , vol.89 , Issue.8 , pp. 4158-4169
    • Gupta, S.1    Clark, E.S.2    Termini, J.M.3


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