Aiming to induce broadly reactive neutralizing antibody responses with HIV-1 vaccine candidates

References

• Klausner R, Fauci A, Corey L et al. Medicine. The need for a global vaccine enterprise. Science5628, 2036–2039 (2003).
   Google Scholar
• Esparza J, Klausner Rl; the Coordinating Committee of the Global HIV/AIDS Vaccine Enterprise. The Global HIV/AIDS Vaccine Enterprise: Scientific Strategic Plan. 2, e25 (2005).
   Google Scholar
• Derived from Statistics in Global Summary of the AIDS Epidemic, ‘AIDS Epidemic Update’ UNAIDS. World Health Organization, December (2005).
   Google Scholar
• Letvin NL. Progress toward a HIV vaccine. Ann. Rev. Med.56, 213–223 (2005).
   PubMed Web of Science ®Google Scholar
• Gandhi R, Walker B. Immunologic control of HIV-1. Ann. Rev. Med.53, 149–172 (2002).
   PubMed Web of Science ®Google Scholar
• Mastro TD, Kitayaporn D. HIV type 1 transmission probabilities: estimates from epidemiologic studies. AIDS Res. Hum. Retrovir.14(Suppl. 3), S223–S227 (1998).
   Web of Science ®Google Scholar
• Quinn TC, Wawer JM, Sewankambo N et al. Viral load and heterosexual transmission of human immunodeficiency virus type 1. N. Engl. J. Med.342, 921–929 (2000).
   PubMed Web of Science ®Google Scholar
• Shibata R, Igarashi T, Haigwood N et al. Neutralizing antibody directed against the HIV-1 envelope glycoprotein can completely block HIV-1/SIV chimeric virus infections of macaque monkeys. Nat. Med.5, 204–210 (1999).
   PubMed Web of Science ®Google Scholar
• Mascola JR, Lewis GM, Stiegler G et al. Protection of macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J. Virol.73, 4009–4018 (1999).
   PubMed Web of Science ®Google Scholar
• Mascola JR, Stiegler G, VanCott TC et al. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nat. Med.6, 207–210 (2000).
   PubMed Web of Science ®Google Scholar
• Parren WHI, Marx AP, Hessell AJ et al. Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro. J. Virol.75, 8340–8347 (2001).
   PubMed Web of Science ®Google Scholar
• Ferrantelli F, Rasmussen RA, Buckley KA et al. Complete protection of neonatal macaques against oral challenge with pathogenic simian-human immunodeficiency virus by human anti-HIV monoclonal antibodies. J. Infect. Dis.189, 2167–2173 (2004).
   PubMed Web of Science ®Google Scholar
• Burton D, Stanfield R, Wilson I. Antibody vs HIV in a clash of evolutionary titans. Proc. Natl Acad. Sci. USA102, 14943–14948 (2005).
   PubMed Web of Science ®Google Scholar
• Haynes B, Moody A, Verkcozy L, Kelsoe G, Alam M. Polyspecificity and neutralization of HIV-1: an hypothesis. Human Antibodies14, 59–67 (2005).
   PubMedGoogle Scholar
• The rgp120 HIV Vaccine Study Group. Placebo-controlled Phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection. J. Infect. Dis.191, 654–665 (2006).
   Google Scholar
• Gilbert P, Ackers M, Berman P et al. HIV-1 virologic and immunologic progression and initiation of antiretroviral therapy among HIV-1-infected subjects in a trial of the efficacy of recombinant glycoprotein 120 vaccine. J. Infect. Dis.192, 974–983 (2005).
   PubMed Web of Science ®Google Scholar
• Levine A, Groshen S, Allen J et al. Initial studies on active immunization of HIV-infected subjects using a gp120-depleted HIV-1 immunogen: long-term follow-up. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol.11, 351–364 (1996).
   PubMedGoogle Scholar
• Lifson J, Rossio J, Piatak M et al. Evaluation of the safety, immunogenicity, and protective efficacy of whole inactivated simian immunodeficiency virus (SIV) vaccines with conformationally and functionally intact envelope glycoproteins. AIDS Res. Hum. Retrovir.20, 772–787 (2004).
   PubMedGoogle Scholar
• Whitney J, Ruprecht R. Live attenuated HIV vaccines: pitfalls and prospects. Curr. Opin. Infect. Dis.17, 17–16 (2004).
   PubMed Web of Science ®Google Scholar
• Koff W, Johnson P, Watkins D et al. HIV vaccine design: insights from live attenuated SIV vaccines. Nat. Immunol.7, 19–23 (2005).
   Google Scholar
• Derdeyn C, Decker J, Bibollet-Ruche F et al. Envelope-constrained neutralization-sensitive HIV-1 after heterosexual transmission. Science303, 2019–2022 (2004).
   PubMed Web of Science ®Google Scholar
• Frost S, Liu Y, Pond S, Chappey C et al. Characterization of human immunodeficiency virus type 1 (HIV-1) envelope variation and neutralizing antibody responses during transmission of HIV-1 subtype B. J. Virol.79, 6523–6527 (2005).
   PubMed Web of Science ®Google Scholar
• Chohan B, Lang D, Sagar M et al. Selection of human immunodeficiency virus type 1 envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viral RNA levels. J. Virol.79, 6528–6531 (2005).
   PubMed Web of Science ®Google Scholar
• Alfsen A, Iniguez P, Bouguyon E, Bomsel M. Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial trancytosis of HIV-1. J. Immunol.166, 6257–6265 (2001).
   PubMed Web of Science ®Google Scholar
• Devito C, Hinkula J, Kaul R et al. Cross-clade HIV-1-specific neutralizing IgA in mucosal and systemic compartments of HIV-1-exposed, persistently seronegative subjects. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol.30, 413–420 (2002).
   Google Scholar
• Yang X, Kurteva S, Ren X, Lee S, Sodroski J. Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus Type 1. J. Virol.79, 12132–12147 (2005).
   PubMed Web of Science ®Google Scholar
• Mascola J. Passive transfer studies to elucidate the role of antibody-mediated protection against HIV-1. Vaccine20, 1922–1925 (2002).
   PubMed Web of Science ®Google Scholar
• Mascola J. Defining the protective antibody response for HIV-1. Curr. Mol. Med.3, 209–216 (2003).
   PubMed Web of Science ®Google Scholar
• Kkusuhara H, Hohdatsu T, Okumura M et al. Dual-subtype vaccine (Fel-O-Vax FIV) Protects cats against contact challenge with heterologous subtype B FIV infected cats. Vet. Microbiol.108, 155–165 (2005).
   PubMedGoogle Scholar
• Beddows S, Lister S, Cheingsong R, Bruck C, Weber J. Comparison of the antibody repertoire generated in healthy volunteers following immunization with a monomeric recombinant gp120 construct derived from a CCR5/CXCR4-using human immunodeficiency virus type 1 isolate with sera from naturally infected individuals. J. Virol.73, 1740–1745 (1999).
   PubMedGoogle Scholar
• Bures RA, Gaitan T, Zhu C et al. Immunization with recombinant canarypox vectors expressing membrane-anchored gp120 followed by gp160 protein boosting fails to generate antibodies that neutralize R5 primary isolates of human immunodeficiency virus type 1. AIDS Res. Hum. Retrovir.,16, 2019–2035 (2000).
   PubMedGoogle Scholar
• Mascola JR, Snyder WS, Weislow OS et al. Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1. J. Infect. Dis.173, 340–348 (1996).
   PubMed Web of Science ®Google Scholar
• Belshe RB, Graham SB, Keefer MC et al. Neutralizing antibodies to HIV-1 in seronegative volunteers immunized with recombinant gp120 from the MN strain of HIV-1. JAMA272, 475–480 (1994).
   PubMed Web of Science ®Google Scholar
• Gorse GJ, McElrath JM, Matthews TJ et al. Modulation of immunologic responses to HIV-1MN recombinant gp160 vaccine by dose and schedule of administration. Vaccine16, 493–506 (1998).
   PubMedGoogle Scholar
• Evans TG, McElrath JM, Matthews T et al. QS-21 promotes an adjuvant effect allowing for reduced antigen dose during HIV-1 envelope subunit immunization in humans. Vaccine19, 2080–2091 (2001).
   PubMed Web of Science ®Google Scholar
• Gilbert PB, Peterson LM, Follman D et al. Correlation between immunologic responses to a recombinant glycoprotein 120 vaccine and incidence of HIV-1 infection in a Phase 3 HIV-1 preventive vaccine trial. J. Infect. Dis.191, 666–677 (2005).
   PubMed Web of Science ®Google Scholar
• Goepfert P, Horton J, McElrath S et al. High-dose recombinant canarypox vaccine expressing HIVI-1 protein in seronegative human subjects. J. Infect. Dis.192, 1249–1259 (2005).
   PubMed Web of Science ®Google Scholar
• Graham BS, Matthews JT, Belshe RB et al. and the NIAID AIDS Vaccine Clinical trials Network. Augmentation of human immunodeficiency virus type 1 neutralizing antibody by priming with gp160 recombinant vaccinia and boosting with rgp160 in vaccinia-naive adults. J. Infect. Dis.167, 533–537 (1993).
   PubMed Web of Science ®Google Scholar
• Evans TG, Keefer CM, Weinhold K et al. A canarypox vaccine expressing multiple HIV-1 genes given alone or with SF-2 rgp120 elicits broad and durable CTL responses in seronegative volunteers. J. Infect. Dis.180, 290–298 (1999).
   PubMed Web of Science ®Google Scholar
• Belshe RB, Gorse JG, Mulligan MJ et al. Induction of immune responses to HIV-1 canarypox virus (ALVAC) HIV-1 and gp120 SF-2 recombinant vaccines in uninfected volunteers. AIDS12, 2407–2415 (1998).
   PubMed Web of Science ®Google Scholar
• Corey L, Mulligan M, Goepfert P et al. Cellular and humoral immune responses to a canarypox vaccine containing human immunodeficiency virus type 1 Env, Gag, and Pro in combination with rgp120. J. Infect. Dis.183, 563–570 (2001).
   PubMedGoogle Scholar
• Russell ND, Graham SB, Keefer M et al. A qualifying Phase II study of an HIV-1 canarypox vaccine (vCP1452), alone and in combination with rgp120, fails to trigger a Phase III correlate of efficacy trial. J. Infect. Dis. submitted (2006).
   Google Scholar
• Ourmanov I, Bilska M, Hirsch VH, Montefiori DC. Recombinant modified vaccinia virus Ankara expressing the surface gp120 of simian immunodeficiency virus (SIV) primes for a rapid neutralizing antibody response to SIV infection in macaques. J. Virol.74, 2960–2965 (2000).
   PubMedGoogle Scholar
• Buckner C, Gines LG, Saunders CJ et al. Priming B cell-mediated anti-HIV envelope responses by vaccination allows for the long-term control of infection in macaques exposed to a R5-tropic SHIV. Virology320, 167–180 (2004).
   PubMed Web of Science ®Google Scholar
• Rose NF, Marx AP, Luckay A et al. An effective AIDS vaccine based on live attenuated vesicular stomatitis virus recombinants. Cell106, 539–549 (2001).
   PubMed Web of Science ®Google Scholar
• Amara RR, Villinger F, Altman JD et al. Control of a mucosal challenge and prevention of AIDS by a multiprotein DNA/MVA vaccine. Science292, 69–74 (2001).
   PubMed Web of Science ®Google Scholar
• Barouch DH, Santra S, Schmitz JE et al. Control of viremia and prevention of clinical AIDS in rhesus monkeys by cytokine-augmented DNA vaccination. Science290, 486–492 (2000).
   PubMed Web of Science ®Google Scholar
• Barouch DH, Santra S, Kuroda MJ et al. Reduction of simian-human immunodeficiency virus 89.6P viremia in rhesus monkeys by recombinant modified vaccinia Ankara (MVA) vaccination. J. Virol.75, 5151–5158 (2001).
   PubMedGoogle Scholar
• Davis NL, Caley IJ, Brown KW et al. Vaccination of macaques against pathogenic simian immunodeficiency virus with Venezuelan equine encephalitis virus replicon particles. J. Virol.74, 371–378 (2000).
   PubMed Web of Science ®Google Scholar
• Wang S, Arthos J, Lawrence MJ, van Ryk D et al. Enhanced immunogenicity of gp120 protein when combined with recombinant DNA priming to generate antibodies that neutralize the JR-FL primary isolate of human immunodeficiency virus type 1. J. Virol.79, 7933–7937 (2005).
   PubMed Web of Science ®Google Scholar
• Mascola JR, Sambor A, Beaudry K et al. Neutralizing antibodies elicited by immunization of monkeys with DNA plasmids and recombinant adenoviral vectors expressing human immunodeficiency virus type 1 proteins. J. Virol.79, 771–779 (2005).
   PubMed Web of Science ®Google Scholar
• Evans TG, Frey S, Israel H et al. Long term memory B-cell responses in recipients of candidate human immunodeficiency virus type 1 vaccines. Vaccine222626–2630 (2004).
   PubMedGoogle Scholar
• Montefiori DC, Hill ST, Vo HTT, Walker DB, Rosenberg ES. Neutralizing antibodies associated with viremia control in a subset of individuals after treatment of acute human immunodeficiency virus type 1 infection. J. Virol.75, 10200–10207 (2001).
   PubMed Web of Science ®Google Scholar
• Montefiori DC, Altfeld M, Lee PK et al. Viremia control despite escape from a rapid and potent autologous neutralizing antibody response after treatment-cessation in an HIV-1-infected individual. J. Immunol.170, 3906–3914 (2003).
   PubMedGoogle Scholar
• Moore PL, Crooks TE, Porter L et al. The nature of non-functional envelope proteins on the surface of human immunodeficiency virus type 1. J. Virol.80(5), 2515–2528 (2006).
   PubMed Web of Science ®Google Scholar
• Montefiori DC. Role of complement and Fc receptors in the pathogenesis of HIV-1 infection. Springer Sem. Immunopathol.18, 371–390 (1997).
   PubMed Web of Science ®Google Scholar
• Forthal DN, Landucci G, Haubrich R Antibody-dependent cellular cytotoxicity independently predicts survival in severely immunocompromised human immunodeficiency virus-infected patients. J. Infect. Dis.180, 1338–1341 (1999).
   PubMedGoogle Scholar
• Forthal DN, Landucci G, Daar ES. Antibody from patients with acute human immunodeficiency virus (HIV) infection inhibits primary strains of HIV type 1 in the presence of natural-killer effector cells. J. Virol.75, 6953–6961 (2001).
   PubMed Web of Science ®Google Scholar
• Landucci G, Phan T, R Higa-Tanner, Gilbert P, Forthal D. Individuals homozygous for the V allele of FcγRIIIa may have increased risk of HIV infection following vaccination with recombinant gp120. AIDS Vaccine 2005, September 6–9, 2005. Montreal, Quebec, Canada. Abstract #119 (2005).
   Google Scholar
• Mascola JR, P D'Souza, Gilbert P et al. Recommendations for the design and use of standard virus panels to assess the neutralizing antibody response elicited by candidate human immunodeficiency virus type 1 vaccines. J. Virol.79, 10103–10107 (2005).
   PubMed Web of Science ®Google Scholar
• Li M, Gao F, Mascola JR et al. Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies. J. Virol.79, 10108–10125 (2005).
   PubMed Web of Science ®Google Scholar
• Chen B, Vogah E, Gong H, Skehel J, Wiley D, Harrison S. Structure of an unliganded simian immunodeficiency virus gp120 Core. Nature433, 834–841 (2005).
   PubMed Web of Science ®Google Scholar
• Eckert D, Kim P. Mechanisms of viral membrane fusion and its inhibition. Ann. Rev. Biochem.70, 777–810 (2001).
   PubMed Web of Science ®Google Scholar
• Matthews T, Salgo M, Greenberg M, Chung J, Demasi R, Bolognesi D. Efuvirtide: the first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes. Nat. Rev. Drug Discovery3, 215–225 (2004).
   PubMed Web of Science ®Google Scholar
• Wei X, Decker J, Wang S et al. Antibody neutralization and escape by HIV-1. Nature422, 307–312 (2003).
   PubMed Web of Science ®Google Scholar
• Richman D, Wrin T, Little S, Petropoulos C. Rapid evolution of the neutralizing antibody response to HIV Type 1 infection. Proc. Natl Acad. Sci. USA100, 4144–4149 (2003).
   PubMed Web of Science ®Google Scholar
• Frost S, Wrin T, Smith D et al. Neutralizing antibody responses drive the evolution of human immunodeficiency virus Type 1 envelope during recent HIV infection. Proc. Natl Acad. Sci. USA201, 18514–18519 (2005).
   Google Scholar
• Palker T, Matthews T, Langlois A et al. Polyvalent human immunodeficiency virus synthetic immunogen comprised of envelope gp120 T helper cell sites and B cell neutralization epitopes. J. Immunol.142, 3612–3619 (1989).
   PubMed Web of Science ®Google Scholar
• Korber B, MacInnes K, Smith R, Myers G. Mutational trends in V3 loop protein sequences observed in different genetic lineages of human immunodeficiency virus Type 1. J. Virol.68, 6730–6744 (1994).
   PubMedGoogle Scholar
• Kwong P, Doyle M, Casper D et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature420, 678–682 (2002).
   PubMed Web of Science ®Google Scholar
• Scanlan CN, Pantophlet R, Wormald MR et al. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of α1–2 mannose residues on the outer face of gp120. J. Virol.76, 7306–7321 (2002).
   PubMed Web of Science ®Google Scholar
• Scanlan CN, Pantophlet R, Wormald et al. The carbohydrate epitope of the neutralizing anti-HIV-1 antibody 2G12. Adv. Exp. Med. Biol.535, 205–218 (2003).
   PubMedGoogle Scholar
• Calarese DA, Lee HK, Huang CY et al. Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12. Proc. Natl Acad. Sci. USA102, 13372–13377 (2005).
   PubMed Web of Science ®Google Scholar
• Nara PL, Smit L, Dunlop N et al. Emergence of viruses resistant to neutralization by V3-specific antibodies in experimental human immunodeficiency virus type IIIb infection of chimpanzees.J. Virol.62, 3779–3791 (1990).
   Google Scholar
• Andeweg A, Boers P, Osterhaus A, Bosch M. Impact of natural sequences variation in the V2 region of the envelope protein of human immunodeficiency virus Type 1 on syncytium induction: a mutational analysis. J. Gen. Virol.76, 1901–1907 (1995).
   PubMedGoogle Scholar
• Wyatt R, Moore J, Accola M, Desjardin E, Robinson J, Sodroski J. Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus Type 1 gp120 epitopes induced by receptor binding. J. Virol.69, 5723–5733 (1995).
   PubMedGoogle Scholar
• Labrosse B, Treboute C, Brelot A, Alizon M. Cooperation of the V1/V2 andV3 domains of human immunodeficiency virus Type 1 gp120 for Interaction with the CXCR4 Receptor. J. Virol.75, 5457–5464 (2001).
   PubMedGoogle Scholar
• Okamoto Y, Shiosaki K, Eda Y et al. Father-to-mother-to-infant transmission of HIV-1: clonally transmitted isolate of infant mutates more rapidly than that of the mother and rapidly loses reactivity with neutralizing antibody. Microbiol. Immunol.41, 131–138 (1997).
   PubMedGoogle Scholar
• Palker T, Clark M, Langlois A et al. Type-specific neutralization of the human immunodeficiency virus with antibodies to Env-coded synthetic peptides. Proc. Natl Acad. Sci. USA85, 1932–1936 (1988).
   PubMed Web of Science ®Google Scholar
• Gorny M, Revesz K, Williams C et al. The V3 loop is accessible on the surface of most human immunlodeficiency virus type 1 primary isolates and serves as a neutralization epitope. J. Virol.78, 2394–2404 (2004).
   PubMedGoogle Scholar
• Zolla-Pazner S. Identifying epitopes of HIV-1 that induce protective antibodies. Nat. Rev. Immunol.4, 199–210 (2004).
   PubMed Web of Science ®Google Scholar
• Rusche J, Javaherian K, McDanal C et al. Antibodies that inhibit fusion of human immunodeficiency virus-infected cells bind a 24-amino acid sequence of the viral envelope, gp120. Proc. Natl Acad. Sci. USA85, 3198–3202 (1988).
   PubMed Web of Science ®Google Scholar
• Javaherian K, Langlois A, LaRosa G et al. Broadly neutralizing antibodies elicited by the hyupervariable neutralizing determinant of HIV-1. Science250, 1590–1593 (1990).
   PubMed Web of Science ®Google Scholar
• Looney D, Fisher A. Putney S et al. Type-restricted neutralization of molecular clones of human immunodeficiency virus. Science241, 357–359 (1988).
   PubMed Web of Science ®Google Scholar
• Golding H, D’Souza M, Bradac J, Mathieson B, Fast P. Neutralization of HIV-1. AIDS Res. Hum. Retrovir.10, 633–643 (1994).
   PubMedGoogle Scholar
• Matthews T. Dilemma of neutralization resistance of HIV-1 field isolates and vaccine development. AIDS Res. Hum. Retrovir.10, 631–632 (1994).
   PubMedGoogle Scholar
• Bou-Habib DC, Roderiquez G, Oravecz T, Berman PW, Lusso P, Norcross MA. Cryptic nature of envelope V3 region epitopes protects primary monocytotropic human immunodeficiency virus type 1 from antibody neutralization. J. Virol.68, 6006–6013 (1994).
   PubMed Web of Science ®Google Scholar
• Haynes B, Ma B, Montefiori D et al. Analysis of HIV-1 subtype B third variable region peptide motifs for induction of neutralizing antibodies against HIV-1 primary isolates. Virology345, 44–55 (2005).
   PubMedGoogle Scholar
• Binley J, Wrin T, Korber B et al. Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies. J. Virol.78, 13232–13252 (2004).
   PubMed Web of Science ®Google Scholar
• Krachmarov C, Pinter A, Honnen W et al. Antibodies that are cross-reactive for human immunodeficiency virus type 1 Clade A and B v3 domains are common in patient sera from Cameroon, but their neutralization activity is usually restricted by epitope masking. J. Virol.79, 780–790 (2005).
   PubMedGoogle Scholar
• Gaschen B, Taylor KJ, Yusim K et al. Diversity of considerations in HIV-1 vaccine selection. Science296, 2354–2360 (2003).
   Google Scholar
• Liao, H-X. Sutherland LL, Xia S-M et al. A group M consensus envelope glycoprotein induces antibodies that neutralize subsets of subtype B and C primary viruses. Virology (2006) (In Press).
   Google Scholar
• Huang C, Tang M, Zhang M et al. Structure of V3-containing HIV-1 gp120 core. Science310, 1025–1028 (2005).
   PubMed Web of Science ®Google Scholar
• Nara PL, Robey WG, Pyle SW et al. Purified envelope glycoproteins from human immunodeficiency virus type 1 induce individuals type-specific neutralizing antibodies. J. Virol.62, 2622–2628 (1988).
   PubMedGoogle Scholar
• Kohler H, Gouldsmit J, Nara P. Clonal antibody dominance in HIB-1 infection: cause for a limited failing immune response. J. Acquir. Immun. Defic. Syndr.5, 1158–1168 (1992).
   PubMedGoogle Scholar
• Herrera C, Klasse P, Michael E et al. The impact of envelope glycoprotein cleavage on the antigenicity, infectivity, and neutralization sensitivity of env-pseudotyped human immunodeficiency virus type 1 particles. Virology338, 154–172 (2005).
   PubMedGoogle Scholar
• Pinter A, Honnen W, D’AGostino P, Gorny M, Zolla-Pazner S, Kayman S. The C108g epitope in the V2 domain of gp120 functions as a potent neutralization target when introduced into envelope proteins derived from human immunodeficiency virus type 1 primary isolates. J. Virol.79, 6909–6917 (2005).
   PubMedGoogle Scholar
• Edinger A, Ahuja M, Sung T et al. Characterization and epitope mapping of neutralizing monoclonal antibodies produced by immunization with oligomeric simian immunodeficiency virus envelope protein. J. Virol.74, 7922–7935 (2000).
   PubMedGoogle Scholar
• Pinter A, Honnen W, Kayman S, Trochev O, Wu Z. Potent neutralization of primary HIV-1 isolates by antibodies directed against epitopes present in the V1/V2 domain of HIV-1 gp120. Vaccine16, 1803–1811 (1998).
   PubMed Web of Science ®Google Scholar
• Wu Z, Kayman S, Honnen W et al. Characterization of neutralization epitopes in the V2 region of human immunodeficiency virus type 1 gp120: role of glycosylation in the correct folding of the V1/V2 domain. J. Virol.69, 2271–2278 (1995).
   PubMedGoogle Scholar
• Skott P, Achour A, Norin M, Thorstensson R, Bjorling E.Characterization of neutralization sites in the second variable and fourth variable region in gp125 and a conserved region in gp36 of human immunodeficiency virus type 2. Viral Immunol.12, 79–88 (1999).
   PubMedGoogle Scholar
• Bolmstedt A, Sjolander S, Hansen J et al. Influence of N-linked glycans in V4-V5 region of human immunodeficiency virus type 1 glycoprotein gp160 on induction of a virus-neutralizing humoral response. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol.12, 213–220 (1996).
   PubMedGoogle Scholar
• Pinter A, Honnen W, He Y, Gorney M, Zolla-Pazner S, Kayman S. The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection. J. Virol.78, 5205–5215 (2004).
   PubMed Web of Science ®Google Scholar
• Ren X, Sodroski J, Yang X. An unrelated monoclonal antibody neutralizes human immunodeficiency virus type 1 by binding to an artificial epitope engineered in a functionally neutral region of the viral envelope glycoproteins. J. Virol.79, 5616–5624 (2005).
   PubMedGoogle Scholar
• Burton D, Pyati R, Koduri S et al. Efficient neutralization of primary isolates of HIV-1 by recombinant human monoclonal antibody. Science266, 1024 (1994).
   PubMed Web of Science ®Google Scholar
• Haynes B, Fleming J, St Clair E et al. Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science308, 1906 (2005).
   PubMed Web of Science ®Google Scholar
• Pantophlet R, Burton D. Immunofocusing: antigen engineering to promote the induction of HIV-neutralizing antibodies. Trends Mol. Med.9, 468–473 (2003).
   PubMed Web of Science ®Google Scholar
• Pantophlet R, Wilson I, Burton D. Improved design of an antigen with enhanced specificity for the broadly HIV-neutralizing antibody b12. Prot. Eng. Design Selection17, 749–758 (2004).
   PubMedGoogle Scholar
• Selvarjah S, Puffer B, Pantophlet R, Law M, Doms R, Burton D. Comparing antigenicity and immunogenicity of engineered gp120. J. Virol.79, 12148–12163 (2005).
   PubMedGoogle Scholar
• Decker J, Bibollet-Ruche F, Wei X et al. Antigenic conservation and immunogenicity of the HIV coreceptor binding site. J. Exp. Med.201, 1407–1419 (2005).
   PubMed Web of Science ®Google Scholar
• Labrijn A, Poignard P, Raja A et al. Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J. Virol.77, 10557–10565 (2003).
   PubMed Web of Science ®Google Scholar
• LaBranche C, Hoffman T, Romano J et al. Determinants of CD4 independence for a human immunodeficiency virus type 1 variant map outside regions required for coreceptor specificity. J. Virol.73, 10310–10319 (1999).
   PubMedGoogle Scholar
• Edwards T, Hoffman T, Baribaud F et al. Relationships between CD4 independence, neutralization sensitivity, and exposure of a CD4-induced epitope in a human immunodeficiency virus type 1 envelope protein. J. Virol.75, 5230–5239 (2001).
   PubMed Web of Science ®Google Scholar
• Conley A, Kessler A, Boots L et al. Neutralization of divergent human immunodeficiency virus type 1 variants and primary isolates by IAM-41–2F5, an anti-gp41 human monoclonal antibody. Proc. Natl Acad. Sci. USA91, 3348 (1994).
   PubMedGoogle Scholar
• Stiegler G, Kunert R, Purtscher M et al. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retrovir.17, 1757 (2001).
   PubMed Web of Science ®Google Scholar
• Roben P, Moore J, Thali M, Sodroski J, Barbas C, Burton D. Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. J. Virol.68, 4821 (1994).
   PubMed Web of Science ®Google Scholar
• Muster T, Stindl F, Purtscher M et al. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J. Virol.67, 6642 (1993).
   PubMed Web of Science ®Google Scholar
• Zwick MB, Labrijn AF, Wang M et al. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J. Virol.75, 10892–10905 (2001).
   PubMed Web of Science ®Google Scholar
• Ofek G, Tang M, Sambor A et al. Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J. Virol.78, 10724 (2004).
   PubMed Web of Science ®Google Scholar
• Cardoso R, Zwick M, Stanfield R et al. Broadly neutralzing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity22, 163 (2005).
   PubMed Web of Science ®Google Scholar
• Burton D, Desrosiers R. Doms R et al. HIV vaccine design and the neutralizing antibody problem. Nat. Immunol.5, 233 (2004).
   PubMed Web of Science ®Google Scholar
• Bibollet-Ruche F, Li H, Decker M et al.Detection of novel neutralizing antibody reactivities against the membrane proximal external region (MPER) of gp41 in HIV-1 infected humans. AIDS Vaccine (2005) Meeting (September 6–9, 2005), Montreal, Canada, Abstract 71 (2005).
   Google Scholar
• Walmsley SK, Katlama HC, Nelson M et al. Enfuvirtide (T-20) cross-reactive glycoprotein 41 antiobdy does not impair the efficacy or safety of enfuvirtide. J. Infect. Diseases188, 1827–1833 (2003).
   PubMed Web of Science ®Google Scholar
• Zwick M, Jensen R, Church W et al. Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial studies in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1. J. Virol.79, 1252 (2005).
   PubMed Web of Science ®Google Scholar
• Earl P, Broder C, Doms R, Moss B. Epitope map of human immunodeficiency virus gype 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol.71, 2674 (1997).
   PubMedGoogle Scholar
• Golding H, Zaitseva M, de Rosny E et al. Dissection of human immunodeficiency virus type 1 entry with neutralizing antibodies to gp41 fusion intermediates. J. Virol.76, 6780–6790 (2002).
   PubMedGoogle Scholar
• Maksyutov AZ, Bachinskii AG, Bazhan SI et al. Exclusion of HIV epitopes shared with human proteins is prerequisite for designing safer AIDS vaccines. J. Clin. Virol.1(Suppl.), S26–38 (2004).
   Google Scholar
• Su TT, Guo B, Wei B, Braun J, Rawlings DJ. Signaling in transitional type 2 B cells is critical for peripheral B-cell development. Immunol. Rev.197, 161–78 (2004).
   PubMed Web of Science ®Google Scholar
• Tsuiji M, Yurasov S, Velinzon K, Thomas S, Nussenzweig MC, Wardemann H. A checkpoint for autoreactivity in human IgM+ memory B cell development. J. Exp. Med.203, 393–400 (2006).
   PubMed Web of Science ®Google Scholar
• Meffre E, Milili M, Blanco-Betancourt C, Antunes H, Nussenzweig MC, Schiff C. Immunoglobulin heavy chain expression shapes the B cell receptro repertor in human B cell development. J. Clin. Invest.108, 879–886 (2001).
   Google Scholar
• Lopalco L, Barassi C, Paolucci C et al. Predictive value of anti-cell and anti-human immunodeficiency virus (HIV) humoral responses in HIV-1-exposed seronegative cohorts of European and Asian origin. J. Gen. Virol.86, 339–348 (2005).
   PubMedGoogle Scholar
• Montefiori DC, Safrit TJ, SL Lydy et al. Induction of neutralizing antibodies and Gag-specific cellular immune responses to an R5 primary isolate of human immunodeficiency virus type 1 in vaccinated rhesus macaques. J. Virol.75, 5939–5948 (2001).
   PubMedGoogle Scholar
• Berkower I M, Raymond J, Muller A, Spadaccini A. Aberseen. Assembly, structure, and antigenic properties of virus-like particles rich in HIV-1 envelope gp120. Virology321, 75–86 (2004).
   PubMedGoogle Scholar
• Grundner C, Mirzabekov T, Sodroski J, Wyatt R. Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins. J. Virol.76, 3511–3521 (2002).
   PubMed Web of Science ®Google Scholar
• Sakaue G, Hiroi T, Nakagawa Y et al. HIV mucosal vaccine: nasal immunization with gp160-encapsulated hemagglutinating virus of Japan-liposome induces antigen-specific CTLs and neutralizing antibody responses. J. Immunol.170, 495–502 (2003).
   PubMed Web of Science ®Google Scholar
• Arthur LO, Bess WJ, Chertova EN Jr. Chemical inactivation of retroviral infectivity by targeting nucleocapsid protein zinc fingers: a candidate SIV vaccine. AIDS Res. Hum. Retrovir.14(Suppl. 3), S311–S319 (1998).
   PubMedGoogle Scholar
• Rossio JL, Esser TM, Suryanarayana K. Inactivation of human immunodeficiency virus type 1 infectivity with preservation of conformational and functional integrity of virion surface proteins. J. Virol.72, 7992–8001 (1998).
   PubMed Web of Science ®Google Scholar
• Montefiori DC, Hirsch MV, Johnson PR. AIDS response. (Scientific Correspondence). Nature,354, 439–440 (1991).
   PubMedGoogle Scholar
• Langlois AJ, Weinhold JK, Matthews JT, Greenberg ML, Bolognesi DP. Detection of anti-human cell antibodies in sera from macaques immunized with whole inactivated virus. AIDS Res. Hum. Retrovir.8, 1641–1652 (2005).
   Google Scholar
• Hammonds J, Chen X, Fouts T, DeVico A, Montefiori D, Spearman P. Induction of neutralizing antibodies against human immunodeficiency virus type 1 primary isolates by Gag-Env pseudovirion immunization. J. Virol.79, 14804–14814 (1992).
   Google Scholar
• Sanders RW, Vesanen M, Schuelke N. Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J. Virol.76, 8875–8889 (2002).
   PubMed Web of Science ®Google Scholar
• Yang X, Farzan M, Wyatt R, Sodroski J. Characterization of stable, soluble trimers containing complete ectodomains of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol.74, 5716–5725 (2000).
   PubMedGoogle Scholar
• Yang X, Florin L, M Farzan P et al. Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution. J. Virol.74, 4746–4654 (2000).
   PubMed Web of Science ®Google Scholar
• Beddows S, Schulke N, M Kirschner et al. Evaluating the immunogenicity of a disulfide-stabilized, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J. Virol.79, 8812–8827 (2005).
   PubMed Web of Science ®Google Scholar
• Yang X, Wyatt R, Sodroski J. Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers. J. Virol.75, 1165–1171 (2001).
   PubMed Web of Science ®Google Scholar
• Kim M, Qiao Z, Montefiori CD, Haynes BF, Reinherz LE, Liao H-X. Comparison of HIV type 1 ADA gp120 monomers versus gp140 trimers as immunogens for the induction of neutralizing antibodies. AIDS Res. Hum. Retrovir.,21, 58–67 (2005).
   PubMed Web of Science ®Google Scholar
• Bolmstedt A, Hinkula J, Rowcliffe E, Biller M, Wahren B, Olofsson S. Enhanced immunogenicity of a human immunodeficiency virus type 1 env DNA vaccine by manipulating N-glycosylation signals: Effects of elimination of the V3 N306 glycan. Vaccine20, 397–405 (2002).
   Google Scholar
• Quinones-Kochs MI, Buonocore L, Rose JK. Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response. J. Virol.76, 4199–4211 (2002).
   PubMed Web of Science ®Google Scholar
• Reitter JN, Means ER, Desrosiers RC. A role for carbohydrates in immune evasion in AIDS. Nat. Med.4, 679–684 (1998).
   PubMed Web of Science ®Google Scholar
• Mori K, Sugimoto C, Ohgimoto S et al. Influence of glycosylation on the efficacy of an Env-based vaccine against simian immunodeficiency virus SIVmac239 in a macaque AIDS model. J. Virol.79, 10386–10396 (2005).
   PubMed Web of Science ®Google Scholar
• Barnett SW, Lu S, Sravastava I et al. The ability of an oligomeric human immunodeficiency virus type 1 (HIV-1) envelope antigen to elicit neutralizing antibodies against primary HIV-1 isolates is improved following partial deletion of the second hypervariable region. J. Virol.75, 5526–5540 (2001).
   PubMed Web of Science ®Google Scholar
• Cherpelis S, Shrivastava I, Gettie A, Jin X, Ho DD, Barnett SW. DNA vaccination with the human immunodeficiency virus type 1 SF162ΕV2 envelope elicits immune responses that offer partial protection from simian/human immunodeficiency virus infection to CD8+ T cell- depleted rhesus macaques. J. Virol.75, 1547–1550 (2001).
   PubMed Web of Science ®Google Scholar
• Gzyl J, Bolesta E, Wierzbicki A et al. Effect of partial and complete variable loop deletions of the human immunodeficiency virus type 1 envelope glycoprotein on the breadth of gp160-specific immune responses. Virology318, 493–506 (2004).
   PubMedGoogle Scholar
• Kim YB, Han PD, Cao C, Cho MW. Immunogenicity and ability of variable loop-deleted human immunodeficiency virus type 1 envelope glycoproteins to elicit neutralizing antibodies. Virology305, 124–137 (2003).
   PubMedGoogle Scholar
• Srivastava IK, VanDorsten K, Vojtech L, Barnett WS, Stomatatos L. Changes in the immunogenic properties of soluble gp140 human immunodeficiency virus envelope constructs upon partial deletion of the second hypervariable region. J. Virol.77, 2310–2320 (2003).
   PubMed Web of Science ®Google Scholar
• LaCasse RA, Follis KE, Trahey M, Scarborough JD, Littman DR, Nunberg JH. Fusion-competent vaccines: broad neutralization of primary isolates of HIV. Science283(5570), 1025 (2002).
   Google Scholar
• Nunberg, JH (2002). Retraction of "LaCasse RA, Follis EK, Trahey M, Scarborough DJ, Littman RD, Nunberg JH. Fusion-competent vaccines: broad neutralization of primary isolates of HIV. Science283, 357–362." Retraction in Science 296, 1025(1999).
   Google Scholar
• Fouts TR, Tuskan R, Godfrey K et al. Expression and characterization of a single-chain polypeptide analogue of the human immunodeficiency virus type 1 gp120-CD4 receptor complex. J. Virol.74, 11427–11436 (2000).
   PubMed Web of Science ®Google Scholar
• DeVico A, Silver A, Thornton MA, Sarngadharan GM, Pal R. Covalently crosslinked complexes of human immunodeficiency virus type 1 (HIV-1) gp120 and CD4 receptor elicit a neutralizing immune response that includes antibodies selective for primary virus isolates. Virology218, 258–263 (1996).
   PubMedGoogle Scholar
• Fouts T, Godfrey K, Bobb K et al. Crosslinked HIV-1 envelope-CD4 receptor complexes elicit broadly cross-reactive neutralizing antibodies in rhesus macaques. Proc. Natl Acad. Sci. USA99, 11842–11847 (2002).
   PubMed Web of Science ®Google Scholar
• Varadarajan R, Sharma D, Chakraborty K et al. Characterization of gp120 and its single-chain derivatives, gp120-CD4D12 and gp120-M9: Implications for targeting the CD4i epitope in human immunodeficiency virus vaccine design. J. Virol.79, 1713–1723 (2005).
   PubMedGoogle Scholar
• Wyatt R, Moore J, Accola M, Desjardin E, Robinson J, Sodroski J. Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J. Virol.69, 5723–5733 (1995).
   PubMedGoogle Scholar
• Liao H-X, S Munir Alam, Mascola JR et al. Immunogenicity of constrained monoclonal antibody A32-human immunodeficiency virus (HIV) Env gp120 complexes compared to that of recombinant HIV type 1 gp120 envelope glycoprotein. J. Virol.78, 5270–5278 (2004).
   PubMedGoogle Scholar
• Sullivan N, Sun Y, Sattentau Q et al. CD4-induced conformational changes in the human immunodeficiency virus type 1 gp120 glycoprotein: consequences for virus entry and neutralization. J. Virol.72, 4694–4703 (1998).
   PubMed Web of Science ®Google Scholar
• Coëffier E, Clément J-M, Cussac V et al. Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein. Vaccine 19, 684–693 (2001).
   Google Scholar
• Eckhart L, Raffelsberger W, Ferko B et al. Immunogenic presentation of a conserved gp41 epitope of human immunodeficiency virus type 1 on recombinant surface antigen of hepatitis B virus. J. Gen. Virol.77, 2001–2008 (1996).
   PubMed Web of Science ®Google Scholar
• Joyce JG, Hurni MW, Bogusky MJ et al. Enhancement of -helicity in the HIV-1 inhibitory peptide DP178 leads to an increased affinity for human monoclonal antibody 2F5 but does not elicit neutralizing responses in vitro: implications for vaccine design. J. Biol. Chem.277, 45811–45820 (2002).
   PubMed Web of Science ®Google Scholar
• Liang X, Munshi S, Shendure J et al. Epitope insertion into variable loops of HIV-1 gp120 as a potential means to improve immunogenicity of viral envelope protein. Vaccine17, 2862–2872 (1999).
   PubMed Web of Science ®Google Scholar
• McGaughey GB, Citron M, Danzeisen RC et al. HIV-1 vaccine development: constrained peptide immunogens show improved binding to the anti-HIV-1 gp41 MAb. Biochemisty42, 3214–3223 (2003).
   PubMedGoogle Scholar
• Zwick MB, Bonnycastle A, Menendez MB et al. Identification and characterization of a peptide that specifically binds the human, broadly neutralizing anti-human immunodeficiency virus type 1 antibody b12. J. Virol.75, 6692–6699 (2001).
   PubMed Web of Science ®Google Scholar
• Bures R, Morris L, Williamson C et al. Regional clustering of shared neutralization determinants on primary isolates of Clade C human immunodeficiency virus type 1 from South Africa. J. Virol.76, 2233–2244 (2002).
   PubMed Web of Science ®Google Scholar
• McKeating JA, Cordell J, Dean JC, Balfe P. Synergistic interaction between ligands binding to the CD4 binding site and V3 domain of human immunodeficiency virus type 1 gp120. Virology191, 732–742 (1992).
   PubMedGoogle Scholar
• Tilley SA, Honnen JW, Racho EM, Chou T-C, Pinter A. Synergistic neutralization of HIV-1 by human monoclonal antibodies against the V3 loop and the CD4-binding site of gp120. AIDS Res. Hum. Retrovir.8, 461–467 (1992).
   PubMedGoogle Scholar
• Potts BJ, Field GK, Wu Y, Posner M, Cavacini L, White-Scharf M. Synergistic inhibition of HIV-1 by CD4 binding domain reagents and V3-directed monoclonal antibodies. Virology197, 415–419 (1993).
   PubMedGoogle Scholar
• Montefiori DC, Graham SB, JT Zhou et al; and the NIH AIDS Vaccine Clinical Trials Network. V3-specific neutralizing antibodies in sera from HIV-1 gp160-immunized volunteers block virus fusion and act synergistically with human monoclonal antibody to the conformation-dependent CD4 binding region of gp120. J. Clin. Invest.92, 840–847 (1993).
   PubMed Web of Science ®Google Scholar
• Mascola JR, Louder KM, VanCott TC et al. Potent and synergistic neutralization of human immunodeficiency virus (HIV) type 1 primary isolates by hyperimmune anti-HIV immunoglobulin combined with monoclonal antibodies 2F5 and 2G12. J. Virol.71, 7198–7206 (1997).
   PubMed Web of Science ®Google Scholar
• Zwick MB, Wang M, Poignard P et al. Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies. J. Virol.75, 12198–12208 (2001).
   PubMed Web of Science ®Google Scholar
• Xu W, BA Smith-Franklin, Li P-L et al. Potent neutralization of primary human immunodeficiency virus Clade C isolates with a synergistic combination of human monoclonal antibodies raised against Clade B. J. Hum. Virol.4, 55–61 (2001).
   PubMedGoogle Scholar
• Zhang M-Y, Shu Y, Rudolph D et al. Improved breadth and potency of an HIV-1 neutralizing human single-chain antibody by random mutagenesis and sequential antigen panning. J. Mol. Biol.335, 209–219 (2004).
   PubMed Web of Science ®Google Scholar
• Barbas CF III, Hu D, Dunlop N et al.In vitro evolution of a neutralizing human antibody to HIV-1 to enhance affinity and broaden strain cross-reactivity. Proc. Natl Acad. Sci. USA91, 3809–3813 (1994).
   PubMed Web of Science ®Google Scholar
• Yang WP, Green K, Pinz-Sweeney S, Briones TA, Burton RD, Barbas CF III. CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J. Mol. Biol.254, 392–403 (1995).
   PubMed Web of Science ®Google Scholar
• Cho MW, Kim BY, Lee MK et al. Polyvalent envelope glycoprotein vaccine elicits a broader neutralizing antibody response but is unable to provide sterilizing protection against heterologous simian/human immunodeficiency virus infection in pigtailed macaques. J. Virol.75, 2224–2234 (2001).
   PubMed Web of Science ®Google Scholar
• Rollman E, Hinkula J, Arteaga J et al. Multi-subtype gp160 DNA immuinization induces broadly neutralizing anti-HIV antibodies. Gen. Ther.1–9 (2004).
   PubMedGoogle Scholar
• Pal R, Wang S, Kalyanaraman V et al. Polyvalent DNA prime and envelope protein boost HIV-1 vaccine elicits humoral and cellular responses and controls plasma viremia in rhesus macaques following rectal challenge with an R5 SHIV isolate. AIDS Res. Hum. Retrovir.14(Suppl. 3), 226–236 (2005).
   Google Scholar
• Zhan X, Martin LN, Slobod KS et al. Multi-envelope HIV-1 vaccine devoid of SIV components controls disease in macaques challenged with heterologous pathogenic SHIV. Vaccine23, 5306–20 (2005).
   PubMedGoogle Scholar
• Nickle DC, Jensen AM, GS Gottlieb et al. Consensus and ancestral state HIV vaccines. Science299, 1515–1518 (2003).
   PubMed Web of Science ®Google Scholar
• Doria-Rose N, Learn HG, Rodrigo AG et al. Human immunodeficiency virus Type 1 subtype B ancestral envelope protein is functional and elicits neutralizing antibodies in rabbits similar to those elicited by a native contemporary subtype B envelope. J. Virol.79, 11214–11224 (2005).
   PubMed Web of Science ®Google Scholar
• Gao F, Weaver AE, Lu Z et al. Antigenicity and immunogenicity of a synthetic human immunodeficiency virus type 1 group M consensus envelope glycoprotein. J. Virol.79, 1154–1163 (2005).
   PubMed Web of Science ®Google Scholar
• Pantophlet R, Wilson AI, Burton DR. Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design. J. Virol.77, 5889–5910 (2003).
   PubMed Web of Science ®Google Scholar
• Nara PL, Garrity R. Deceptive imprinting: a cosmopolitan strategy for complicating vaccination. Vaccine16, 1780–1787 (1998).
   Google Scholar
• Garrity RR, Rimmelzwaan G, Minassian A et al. Refocusing neutralizing antibody responses by targeted dampening of an immunodominant epitope. J. Immunol.77, 5589–5910 (1997).
   Google Scholar
• Selvarajah S, Puffer B, Pantophlet R, Law M, Doms R, Burton D. Evaluating antigenicity and immunogenicity of engineered gp120s. AIDS Vaccine 2005, September 6–9, 2005. Montreal, Quebec, Canada. Abstract #72 (2005).
   Google Scholar
• Sanders RW, Schiffner L, Master A et al. Variable-loop deleted variants of the human immunogenicity virus type 1 envelope glycoprotein can be stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits. J. Virol.74, 5091–5100 (2000).
   PubMedGoogle Scholar
• Srivastava IK, Stamatatos L, Kan E. Purification, characterization, and immunogenicity of a soluble trimeric envelope protein containing a partial deletion of the V2 loop derived from SF162, an R5-tropic human immunodeficiency virus type 1 isolate. J. Virol.77, 11244–11259 (2003).
   PubMed Web of Science ®Google Scholar
• Jiang ZH, Koganty RR. Synthetic vaccines: the role of adjuvants in immune targeting. Curr. Med. Chem.10, 1423–1439 (2003).
   PubMedGoogle Scholar
• Kaisho T, Akira, S Regulation of dendritic cell function through toll-like receptors. Curr. Mol. Med.3, 759–771 (2003).
   PubMed Web of Science ®Google Scholar
• Takeshita F, Gursel I, Ishii KJ, Suzuki K, Gursel M, Klinman DM. Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9. Sem. Immunol.16, 17–22 (2004).
   PubMed Web of Science ®Google Scholar
• Baldridge JR, McGowan P, Evans JT et al. Taking a toll on human disease: Toll-like receptor 4 agonists as vaccine adjuvants and monotherapeutic agents. Expert Opin. Biol. Ther.4, 1129–1138 (2004).
   PubMed Web of Science ®Google Scholar
• Kaisho T, Akira, S Pleiotropic function of Toll-like receptors. Microb. Infect.6, 1388–1394 (2004).
   PubMed Web of Science ®Google Scholar
• Vollmer J. Progress in drug development of immunostimulatory CpG oligodeoxynucleotide ligands for TLR9. Expert Opin. Biol. Ther.5, 673–682 (2005).
   PubMed Web of Science ®Google Scholar
• Gluck R, Burri KG, Metcalfe I. Adjuvant and antigen delivery properties of virosomes. Curr. Drug Deliv.2, 395–400 (2005).
   PubMedGoogle Scholar
• Brown LE, Jackson DC. Lipid-based self-adjuvanting vaccines. Curr. Drug Deliv.2, 383–393 (2005).
   PubMedGoogle Scholar
• Graham BS. New Approaches to Vaccine Adjuvants: Inhibiting the Inhibitor. PLoS Med.3, e57 (2006).
   PubMed Web of Science ®Google Scholar
• Moore AC, Gallimore A, Draper SJ, Watkins KR, Gilbert SC, Hill AV. Anti-CD25 antibody enhancement of vaccine-induced immunogenicity: increased durable cellular immunity with reduced immunodominance. J. Immunol.175, 7264–7273 (2005).
   PubMed Web of Science ®Google Scholar