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Volumn 405, Issue 2, 2010, Pages 513-523

Structure-guided design and immunological characterization of immunogens presenting the HIV-1 gp120 V3 loop on a CTB scaffold

Author keywords

447 52D; Cholera toxin B subunit; Gp120; HIV vaccine; HIV 1; Immunogen design; Neutralizing antibody; V3 loop

Indexed keywords

CHOLERA TOXIN B SUBUNIT; DNA; DNA VACCINE; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; MONOCLONAL ANTIBODY;

EID: 77955657135     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2010.06.027     Document Type: Article
Times cited : (39)

References (87)
  • 1
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan R., Totrov M. Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J. Mol. Biol. 1994, 235:983-1002.
    • (1994) J. Mol. Biol. , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 2
    • 84986522918 scopus 로고
    • ICM-a new method for protein modelling and design. Applications to docking and structure prediction from the distorted native conformation
    • Abagyan R., Totrov M., Kuznetsov D. ICM-a new method for protein modelling and design. Applications to docking and structure prediction from the distorted native conformation. J. Comp. Chem. 1994, 15:488-506.
    • (1994) J. Comp. Chem. , vol.15 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2    Kuznetsov, D.3
  • 3
    • 0027532369 scopus 로고
    • Envelope-binding domain in the cationic amino acid transporter determines the host range of ecotropic murine retroviruses
    • Albritton L.M., Kim J.W., Tseng L., Cunningham J.M. Envelope-binding domain in the cationic amino acid transporter determines the host range of ecotropic murine retroviruses. J. Virol. 1993, 67:2091-2096.
    • (1993) J. Virol. , vol.67 , pp. 2091-2096
    • Albritton, L.M.1    Kim, J.W.2    Tseng, L.3    Cunningham, J.M.4
  • 4
    • 0028109491 scopus 로고
    • Insertion of a HIV-1-neutralizing epitope in a surface-exposed internal region of the cholera toxin B-subunit
    • Backstrom M., Lebens M., Schodel F., Holmgren J. Insertion of a HIV-1-neutralizing epitope in a surface-exposed internal region of the cholera toxin B-subunit. Gene 1994, 149:211-217.
    • (1994) Gene , vol.149 , pp. 211-217
    • Backstrom, M.1    Lebens, M.2    Schodel, F.3    Holmgren, J.4
  • 6
    • 53349160053 scopus 로고    scopus 로고
    • Challenges in the development of an HIV-1 vaccine
    • Barouch D.H. Challenges in the development of an HIV-1 vaccine. Nature 2008, 455:613-619.
    • (2008) Nature , vol.455 , pp. 613-619
    • Barouch, D.H.1
  • 7
    • 0028839185 scopus 로고
    • Characterization of an internal permissive site in the cholera toxin B-subunit and insertion of epitopes from human immunodeficiency virus-1, hepatitis B virus and enterotoxigenic Escherichia coli
    • Backstrom M., Holmgren J., Schodel F., Lebens M. Characterization of an internal permissive site in the cholera toxin B-subunit and insertion of epitopes from human immunodeficiency virus-1, hepatitis B virus and enterotoxigenic Escherichia coli. Gene 1995, 165:163-171.
    • (1995) Gene , vol.165 , pp. 163-171
    • Backstrom, M.1    Holmgren, J.2    Schodel, F.3    Lebens, M.4
  • 9
    • 0027366163 scopus 로고
    • An endogenously synthesized decamer peptide efficiently primes cytotoxic T cells specific for the HIV-1 envelope glycoprotein
    • Bergmann C., Stohlmann S.A., McMillan M. An endogenously synthesized decamer peptide efficiently primes cytotoxic T cells specific for the HIV-1 envelope glycoprotein. Eur. J. Immunol. 1993, 23:2777-2781.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 2777-2781
    • Bergmann, C.1    Stohlmann, S.A.2    McMillan, M.3
  • 12
    • 70350714115 scopus 로고    scopus 로고
    • Structural basis of the cross-reactivity of genetically related human anti-HIV-1 mAbs: implications for design of V3-based immunogens
    • Burke V., Williams C., Sukumaran M., Kim S.S., Li H., Wang X.H., Gorny M.K., Zolla-Pazner S., Kong X.P. Structural basis of the cross-reactivity of genetically related human anti-HIV-1 mAbs: implications for design of V3-based immunogens. Structure 2009, 17:1538-1546.
    • (2009) Structure , vol.17 , pp. 1538-1546
    • Burke, V.1    Williams, C.2    Sukumaran, M.3    Kim, S.S.4    Li, H.5    Wang, X.H.6    Gorny, M.K.7    Zolla-Pazner, S.8    Kong, X.P.9
  • 14
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D.C., Fass D., Berger J.M., Kim P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997, 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 16
    • 4644279789 scopus 로고    scopus 로고
    • Different immune response of mice immunized with conjugates containing multiple copies of either consensus or mixotope versions of the V3 loop peptide from human immunodeficiency virus type 1
    • Cruz L.J., Iglesias E., Aguilar J.C., Cabrales A., Reyes O., Andreu D. Different immune response of mice immunized with conjugates containing multiple copies of either consensus or mixotope versions of the V3 loop peptide from human immunodeficiency virus type 1. Bioconjug. Chem. 2004, 15:1110-1117.
    • (2004) Bioconjug. Chem. , vol.15 , pp. 1110-1117
    • Cruz, L.J.1    Iglesias, E.2    Aguilar, J.C.3    Cabrales, A.4    Reyes, O.5    Andreu, D.6
  • 18
    • 0024565465 scopus 로고
    • Oral administration of a streptococcal antigen coupled to cholera toxin B subunit evokes strong antibody responses in salivary glands and extramucosal tissues
    • Czerkinsky C., Russell M.W., Lycke N., Lindblad M., Holmgren J. Oral administration of a streptococcal antigen coupled to cholera toxin B subunit evokes strong antibody responses in salivary glands and extramucosal tissues. Infect. Immun. 1989, 57:1072-1077.
    • (1989) Infect. Immun. , vol.57 , pp. 1072-1077
    • Czerkinsky, C.1    Russell, M.W.2    Lycke, N.3    Lindblad, M.4    Holmgren, J.5
  • 21
    • 0029812316 scopus 로고    scopus 로고
    • Immunogenic presentation of a conserved gp41 epitope of human immunodeficiency virus type 1 on recombinant surface antigen of hepatitis B virus
    • Eckhart L., Raffelsberger W., Ferko B., Klima A., Purtscher M., Katinger H., Ruker F. Immunogenic presentation of a conserved gp41 epitope of human immunodeficiency virus type 1 on recombinant surface antigen of hepatitis B virus. J. Gen. Virol. 1996, 77(Pt 9):2001-2008.
    • (1996) J. Gen. Virol. , vol.77 , Issue.PT 9 , pp. 2001-2008
    • Eckhart, L.1    Raffelsberger, W.2    Ferko, B.3    Klima, A.4    Purtscher, M.5    Katinger, H.6    Ruker, F.7
  • 22
    • 0037378940 scopus 로고    scopus 로고
    • Cholera toxin and its B subunit promote dendritic cell vaccination with different influences on Th1 and Th2 development
    • Eriksson K., Fredriksson M., Nordstrom I., Holmgren J. Cholera toxin and its B subunit promote dendritic cell vaccination with different influences on Th1 and Th2 development. Infect. Immun. 2003, 71:1740-1747.
    • (2003) Infect. Immun. , vol.71 , pp. 1740-1747
    • Eriksson, K.1    Fredriksson, M.2    Nordstrom, I.3    Holmgren, J.4
  • 24
    • 0027508019 scopus 로고
    • Immunological characterization of a rotavirus-neutralizing epitope fused to the cholera toxin B subunit
    • Gonzalez R.A., Sanchez J., Holmgren J., Lopez S., Arias C.F. Immunological characterization of a rotavirus-neutralizing epitope fused to the cholera toxin B subunit. Gene 1993, 133:227-232.
    • (1993) Gene , vol.133 , pp. 227-232
    • Gonzalez, R.A.1    Sanchez, J.2    Holmgren, J.3    Lopez, S.4    Arias, C.F.5
  • 29
    • 0027311936 scopus 로고
    • Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120
    • Gorny M.K., Xu J.Y., Karwowska S., Buchbinder A., Zolla-Pazner S. Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120. J. Immunol. 1993, 150:635-643.
    • (1993) J. Immunol. , vol.150 , pp. 635-643
    • Gorny, M.K.1    Xu, J.Y.2    Karwowska, S.3    Buchbinder, A.4    Zolla-Pazner, S.5
  • 30
    • 33846148643 scopus 로고    scopus 로고
    • Clinical experience with plasmid DNA- and modified vaccinia virus Ankara-vectored human immunodeficiency virus type 1 clade A vaccine focusing on T-cell induction
    • Hanke T., Goonetilleke N., McMichael A.J., Dorrell L. Clinical experience with plasmid DNA- and modified vaccinia virus Ankara-vectored human immunodeficiency virus type 1 clade A vaccine focusing on T-cell induction. J. Gen. Virol. 2007, 88:1-12.
    • (2007) J. Gen. Virol. , vol.88 , pp. 1-12
    • Hanke, T.1    Goonetilleke, N.2    McMichael, A.J.3    Dorrell, L.4
  • 31
    • 1842331564 scopus 로고    scopus 로고
    • Envelope glycoproteins from human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus can use human CCR5 as a coreceptor for viral entry and make direct CD4-dependent interactions with this chemokine receptor
    • Hill C.M., Deng H., Unutmaz D., Kewalramani V.N., Bastiani L., Gorny M.K., Zolla-Pazner S., Littman D.R. Envelope glycoproteins from human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus can use human CCR5 as a coreceptor for viral entry and make direct CD4-dependent interactions with this chemokine receptor. J. Virol. 1997, 71:6296-6304.
    • (1997) J. Virol. , vol.71 , pp. 6296-6304
    • Hill, C.M.1    Deng, H.2    Unutmaz, D.3    Kewalramani, V.N.4    Bastiani, L.5    Gorny, M.K.6    Zolla-Pazner, S.7    Littman, D.R.8
  • 32
    • 70649105392 scopus 로고    scopus 로고
    • The use of immune complex vaccines to enhance antibody responses against neutralizing epitopes on HIV-1 envelope gp120
    • Hioe C.E., Visciano M.L., Kumar R., Liu J., Mack E.A., Simon R.E., Levy D.N., Tuen M. The use of immune complex vaccines to enhance antibody responses against neutralizing epitopes on HIV-1 envelope gp120. Vaccine 2009, 28:352-360.
    • (2009) Vaccine , vol.28 , pp. 352-360
    • Hioe, C.E.1    Visciano, M.L.2    Kumar, R.3    Liu, J.4    Mack, E.A.5    Simon, R.E.6    Levy, D.N.7    Tuen, M.8
  • 34
    • 33846556067 scopus 로고    scopus 로고
    • Type-specific epitopes targeted by monoclonal antibodies with exceptionally potent neutralizing activities for selected strains of human immunodeficiency virus type 1 map to a common region of the V2 domain of gp120 and differ only at single positions from the clade B consensus sequence
    • Honnen W.J., Krachmarov C., Kayman S.C., Gorny M.K., Zolla-Pazner S., Pinter A. Type-specific epitopes targeted by monoclonal antibodies with exceptionally potent neutralizing activities for selected strains of human immunodeficiency virus type 1 map to a common region of the V2 domain of gp120 and differ only at single positions from the clade B consensus sequence. J. Virol. 2007, 81:1424-1432.
    • (2007) J. Virol. , vol.81 , pp. 1424-1432
    • Honnen, W.J.1    Krachmarov, C.2    Kayman, S.C.3    Gorny, M.K.4    Zolla-Pazner, S.5    Pinter, A.6
  • 37
    • 0028097964 scopus 로고
    • Presentation of native epitopes in the V1/V2 and V3 regions of human immunodeficiency virus type 1 gp120 by fusion glycoproteins containing isolated gp120 domains
    • Kayman S.C., Wu Z., Revesz K., Chen H., Kopelman R., Pinter A. Presentation of native epitopes in the V1/V2 and V3 regions of human immunodeficiency virus type 1 gp120 by fusion glycoproteins containing isolated gp120 domains. J. Virol. 1994, 68:400-410.
    • (1994) J. Virol. , vol.68 , pp. 400-410
    • Kayman, S.C.1    Wu, Z.2    Revesz, K.3    Chen, H.4    Kopelman, R.5    Pinter, A.6
  • 38
    • 11144233210 scopus 로고    scopus 로고
    • Antibodies that are cross-reactive for human immunodeficiency virus type 1 clade a and clade B V3 domains are common in patient sera from Cameroon, but their neutralization activity is usually restricted by epitope masking
    • Krachmarov C., Pinter A., Honnen W.J., Gorny M.K., Nyambi P.N., Zolla-Pazner S., Kayman S.C. Antibodies that are cross-reactive for human immunodeficiency virus type 1 clade a and clade B V3 domains are common in patient sera from Cameroon, but their neutralization activity is usually restricted by epitope masking. J. Virol. 2005, 79:780-790.
    • (2005) J. Virol. , vol.79 , pp. 780-790
    • Krachmarov, C.1    Pinter, A.2    Honnen, W.J.3    Gorny, M.K.4    Nyambi, P.N.5    Zolla-Pazner, S.6    Kayman, S.C.7
  • 39
    • 33745796735 scopus 로고    scopus 로고
    • Factors determining the breadth and potency of neutralization by V3-specific human monoclonal antibodies derived from subjects infected with clade A or clade B strains of human immunodeficiency virus type 1
    • Krachmarov C.P., Honnen W.J., Kayman S.C., Gorny M.K., Zolla-Pazner S., Pinter A. Factors determining the breadth and potency of neutralization by V3-specific human monoclonal antibodies derived from subjects infected with clade A or clade B strains of human immunodeficiency virus type 1. J. Virol. 2006, 80:7127-7135.
    • (2006) J. Virol. , vol.80 , pp. 7127-7135
    • Krachmarov, C.P.1    Honnen, W.J.2    Kayman, S.C.3    Gorny, M.K.4    Zolla-Pazner, S.5    Pinter, A.6
  • 40
    • 0035701793 scopus 로고    scopus 로고
    • V3-specific polyclonal antibodies affinity purified from sera of infected humans effectively neutralize primary isolates of human immunodeficiency virus type 1
    • Krachmarov C.P., Kayman S.C., Honnen W.J., Trochev O., Pinter A. V3-specific polyclonal antibodies affinity purified from sera of infected humans effectively neutralize primary isolates of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses 2001, 17:1737-1748.
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 1737-1748
    • Krachmarov, C.P.1    Kayman, S.C.2    Honnen, W.J.3    Trochev, O.4    Pinter, A.5
  • 43
    • 0035000767 scopus 로고    scopus 로고
    • Cooperation of the V1/V2 and V3 domains of human immunodeficiency virus type 1 gp120 for interaction with the CXCR4 receptor
    • Labrosse B., Treboute C., Brelot A., Alizon M. Cooperation of the V1/V2 and V3 domains of human immunodeficiency virus type 1 gp120 for interaction with the CXCR4 receptor. J. Virol. 2001, 75:5457-5464.
    • (2001) J. Virol. , vol.75 , pp. 5457-5464
    • Labrosse, B.1    Treboute, C.2    Brelot, A.3    Alizon, M.4
  • 45
    • 34247166722 scopus 로고    scopus 로고
    • Antigenic and immunogenic study of membrane-proximal external region-grafted gp120 antigens by a DNA prime-protein boost immunization strategy
    • Law M., Cardoso R.M., Wilson I.A., Burton D.R. Antigenic and immunogenic study of membrane-proximal external region-grafted gp120 antigens by a DNA prime-protein boost immunization strategy. J. Virol. 2007, 81:4272-4285.
    • (2007) J. Virol. , vol.81 , pp. 4272-4285
    • Law, M.1    Cardoso, R.M.2    Wilson, I.A.3    Burton, D.R.4
  • 46
    • 25144458435 scopus 로고    scopus 로고
    • Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM, LA-UR 06-0680, T. Leitner, F.B., B. Hahn, P. Marx, F. McCutchan, J. Mellors, S. Wolinsky, B. Korber (Eds.)
    • HIV Sequence Compendium 2005, Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM, LA-UR 06-0680. T. Leitner, F.B., B. Hahn, P. Marx, F. McCutchan, J. Mellors, S. Wolinsky, B. Korber (Eds.).
    • (2005) HIV Sequence Compendium
  • 48
    • 0025770262 scopus 로고
    • Intranasal immunization using the B subunit of the Escherichia coli heat-labile toxin fused to an epitope of the Bordetella pertussis P.69 antigen
    • Lipscombe M., Charles I.G., Roberts M., Dougan G., Tite J., Fairweather N.F. Intranasal immunization using the B subunit of the Escherichia coli heat-labile toxin fused to an epitope of the Bordetella pertussis P.69 antigen. Mol. Microbiol. 1991, 5:1385-1392.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1385-1392
    • Lipscombe, M.1    Charles, I.G.2    Roberts, M.3    Dougan, G.4    Tite, J.5    Fairweather, N.F.6
  • 51
    • 0035158926 scopus 로고    scopus 로고
    • Recombinant antigen-enterotoxin A2/B chimeric mucosal immunogens differentially enhance antibody responses and B7-dependent costimulation of CD4(+) T cells
    • Martin M., Hajishengallis G., Metzger D.J., Michalek S.M., Connell T.D., Russell M.W. Recombinant antigen-enterotoxin A2/B chimeric mucosal immunogens differentially enhance antibody responses and B7-dependent costimulation of CD4(+) T cells. Infect. Immun. 2001, 69:252-261.
    • (2001) Infect. Immun. , vol.69 , pp. 252-261
    • Martin, M.1    Hajishengallis, G.2    Metzger, D.J.3    Michalek, S.M.4    Connell, T.D.5    Russell, M.W.6
  • 52
    • 33646872613 scopus 로고    scopus 로고
    • Humoral immune responses by prime-boost heterologous route immunizations with CTB-MPR (649-684), a mucosal subunit HIV/AIDS vaccine candidate
    • Matoba N., Geyer B.C., Kilbourne J., Alfsen A., Bomsel M., Mor T.S. Humoral immune responses by prime-boost heterologous route immunizations with CTB-MPR (649-684), a mucosal subunit HIV/AIDS vaccine candidate. Vaccine 2006, 24:5047-5055.
    • (2006) Vaccine , vol.24 , pp. 5047-5055
    • Matoba, N.1    Geyer, B.C.2    Kilbourne, J.3    Alfsen, A.4    Bomsel, M.5    Mor, T.S.6
  • 54
    • 0034904098 scopus 로고    scopus 로고
    • Effect of soluble CD4 on exposure of epitopes on primary, intact, native human immunodeficiency virus type 1 virions of different genetic clades
    • Mbah H.A., Burda S., Gorny M.K., Williams C., Revesz K., Zolla-Pazner S., Nyambi P.N. Effect of soluble CD4 on exposure of epitopes on primary, intact, native human immunodeficiency virus type 1 virions of different genetic clades. J. Virol. 2001, 75:7785-7788.
    • (2001) J. Virol. , vol.75 , pp. 7785-7788
    • Mbah, H.A.1    Burda, S.2    Gorny, M.K.3    Williams, C.4    Revesz, K.5    Zolla-Pazner, S.6    Nyambi, P.N.7
  • 55
    • 55849141268 scopus 로고    scopus 로고
    • Viral sequence diversity: challenges for AIDS vaccine designs
    • McBurney S.P., Ross T.M. Viral sequence diversity: challenges for AIDS vaccine designs. Expert Rev. Vaccin. 2008, 7:1405-1417.
    • (2008) Expert Rev. Vaccin. , vol.7 , pp. 1405-1417
    • McBurney, S.P.1    Ross, T.M.2
  • 56
    • 0021165561 scopus 로고
    • Cholera toxin B subunit as a carrier protein to stimulate a mucosal immune response
    • McKenzie S.J., Halsey J.F. Cholera toxin B subunit as a carrier protein to stimulate a mucosal immune response. J. Immunol. 1984, 133:1818-1824.
    • (1984) J. Immunol. , vol.133 , pp. 1818-1824
    • McKenzie, S.J.1    Halsey, J.F.2
  • 57
    • 0032500378 scopus 로고    scopus 로고
    • The 1.25 Å resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site
    • Merritt E.A., Kuhn P., Sarfaty S., Erbe J.L., Holmes R.K., Hol W.G. The 1.25 Å resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site. J. Mol. Biol. 1998, 282:1043-1059.
    • (1998) J. Mol. Biol. , vol.282 , pp. 1043-1059
    • Merritt, E.A.1    Kuhn, P.2    Sarfaty, S.3    Erbe, J.L.4    Holmes, R.K.5    Hol, W.G.6
  • 59
    • 0028235930 scopus 로고
    • Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS
    • Muster T., Guinea R., Trkola A., Purtscher M., Klima A., Steindl F., Palese P., Katinger H. Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS. J. Virol. 1994, 68:4031-4034.
    • (1994) J. Virol. , vol.68 , pp. 4031-4034
    • Muster, T.1    Guinea, R.2    Trkola, A.3    Purtscher, M.4    Klima, A.5    Steindl, F.6    Palese, P.7    Katinger, H.8
  • 60
    • 34547778364 scopus 로고    scopus 로고
    • Prediction of MHC class II binding affinity using SMM-align, a novel stabilization matrix alignment method
    • Nielsen M., Lundegaard C., Lund O. Prediction of MHC class II binding affinity using SMM-align, a novel stabilization matrix alignment method. BMC Bioinform. 2007, 8:238.
    • (2007) BMC Bioinform. , vol.8 , pp. 238
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3
  • 61
    • 58149116578 scopus 로고    scopus 로고
    • Neutralization patterns and evolution of sequential HIV type 1 envelope sequences in HIV type 1 subtype B-infected drug-naive individuals
    • Nyambi P., Burda S., Urbanski M., Heyndrickx L., Janssens W., Vanham G., Nadas A. Neutralization patterns and evolution of sequential HIV type 1 envelope sequences in HIV type 1 subtype B-infected drug-naive individuals. AIDS Res. Hum. Retroviruses 2008, 24:1507-1519.
    • (2008) AIDS Res. Hum. Retroviruses , vol.24 , pp. 1507-1519
    • Nyambi, P.1    Burda, S.2    Urbanski, M.3    Heyndrickx, L.4    Janssens, W.5    Vanham, G.6    Nadas, A.7
  • 62
    • 34250027638 scopus 로고    scopus 로고
    • Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesis
    • Pantophlet R., Aguilar-Sino R.O., Wrin T., Cavacini L.A., Burton D.R. Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesis. Virology 2007, 364:441-453.
    • (2007) Virology , vol.364 , pp. 441-453
    • Pantophlet, R.1    Aguilar-Sino, R.O.2    Wrin, T.3    Cavacini, L.A.4    Burton, D.R.5
  • 63
    • 54949111659 scopus 로고    scopus 로고
    • Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity
    • Pantophlet R., Wrin T., Cavacini L.A., Robinson J.E., Burton D.R. Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity. Virology 2008, 381:251-260.
    • (2008) Virology , vol.381 , pp. 251-260
    • Pantophlet, R.1    Wrin, T.2    Cavacini, L.A.3    Robinson, J.E.4    Burton, D.R.5
  • 69
    • 34548695901 scopus 로고    scopus 로고
    • Standardized assessment of NAb responses elicited in rhesus monkeys immunized with single- or multi-clade HIV-1 envelope immunogens
    • Seaman M.S., Leblanc D.F., Grandpre L.E., Bartman M.T., Montefiori D.C., Letvin N.L., Mascola J.R. Standardized assessment of NAb responses elicited in rhesus monkeys immunized with single- or multi-clade HIV-1 envelope immunogens. Virology 2007, 367:175-186.
    • (2007) Virology , vol.367 , pp. 175-186
    • Seaman, M.S.1    Leblanc, D.F.2    Grandpre, L.E.3    Bartman, M.T.4    Montefiori, D.C.5    Letvin, N.L.6    Mascola, J.R.7
  • 70
    • 0037317611 scopus 로고    scopus 로고
    • Alternative conformations of HIV-1 V3 loops mimic beta hairpins in chemokines, suggesting a mechanism for coreceptor selectivity
    • Sharon M., Kessler N., Levy R., Zolla-Pazner S., Gorlach M., Anglister J. Alternative conformations of HIV-1 V3 loops mimic beta hairpins in chemokines, suggesting a mechanism for coreceptor selectivity. Structure 2003, 11:225-236.
    • (2003) Structure , vol.11 , pp. 225-236
    • Sharon, M.1    Kessler, N.2    Levy, R.3    Zolla-Pazner, S.4    Gorlach, M.5    Anglister, J.6
  • 71
    • 0026754683 scopus 로고
    • Small amino acid changes in the V3 hypervariable region of gp120 can affect the T-cell-line and macrophage tropism of human immunodeficiency virus type 1
    • Shioda T., Levy J.A., Cheng-Mayer C. Small amino acid changes in the V3 hypervariable region of gp120 can affect the T-cell-line and macrophage tropism of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:9434-9438.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 9434-9438
    • Shioda, T.1    Levy, J.A.2    Cheng-Mayer, C.3
  • 72
    • 1242351232 scopus 로고    scopus 로고
    • Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D
    • Stanfield R.L., Gorny M.K., Williams C., Zolla-Pazner S., Wilson I.A. Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D. Structure 2004, 12:193-204.
    • (2004) Structure , vol.12 , pp. 193-204
    • Stanfield, R.L.1    Gorny, M.K.2    Williams, C.3    Zolla-Pazner, S.4    Wilson, I.A.5
  • 73
    • 33744933182 scopus 로고    scopus 로고
    • Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity
    • Stanfield R.L., Gorny M.K., Zolla-Pazner S., Wilson I.A. Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity. J. Virol. 2006, 80:6093-6105.
    • (2006) J. Virol. , vol.80 , pp. 6093-6105
    • Stanfield, R.L.1    Gorny, M.K.2    Zolla-Pazner, S.3    Wilson, I.A.4
  • 77
    • 33746651142 scopus 로고    scopus 로고
    • Polyvalent HIV-1 Env vaccine formulations delivered by the DNA priming plus protein boosting approach are effective in generating neutralizing antibodies against primary human immunodeficiency virus type 1 isolates from subtypes A, B, C, D and E
    • Wang S., Pal R., Mascola J.R., Chou T.H., Mboudjeka I., Shen S., Liu Q., Whitney S., Keen T., Nair B.C., Kalyanaraman V.S., Markham P., Lu S. Polyvalent HIV-1 Env vaccine formulations delivered by the DNA priming plus protein boosting approach are effective in generating neutralizing antibodies against primary human immunodeficiency virus type 1 isolates from subtypes A, B, C, D and E. Virology 2006, 350:34-47.
    • (2006) Virology , vol.350 , pp. 34-47
    • Wang, S.1    Pal, R.2    Mascola, J.R.3    Chou, T.H.4    Mboudjeka, I.5    Shen, S.6    Liu, Q.7    Whitney, S.8    Keen, T.9    Nair, B.C.10    Kalyanaraman, V.S.11    Markham, P.12    Lu, S.13
  • 79
    • 33744470143 scopus 로고    scopus 로고
    • Cross-clade recognition and neutralization by the V3 region from clade C human immunodeficiency virus-1 envelope
    • Wu L., Yang Z.Y., Xu L., Welcher B., Winfrey S., Shao Y., Mascola J.R., Nabel G.J. Cross-clade recognition and neutralization by the V3 region from clade C human immunodeficiency virus-1 envelope. Vaccine 2006, 24:4995-5002.
    • (2006) Vaccine , vol.24 , pp. 4995-5002
    • Wu, L.1    Yang, Z.Y.2    Xu, L.3    Welcher, B.4    Winfrey, S.5    Shao, Y.6    Mascola, J.R.7    Nabel, G.J.8
  • 80
    • 53249113124 scopus 로고    scopus 로고
    • Soluble CD4 broadens neutralization of V3-directed monoclonal antibodies and guinea pig vaccine sera against HIV-1 subtype B and C reference viruses
    • Wu X., Sambor A., Nason M.C., Yang Z.Y., Wu L., Zolla-Pazner S., Nabel G.J., Mascola J.R. Soluble CD4 broadens neutralization of V3-directed monoclonal antibodies and guinea pig vaccine sera against HIV-1 subtype B and C reference viruses. Virology 2008, 380:285-295.
    • (2008) Virology , vol.380 , pp. 285-295
    • Wu, X.1    Sambor, A.2    Nason, M.C.3    Yang, Z.Y.4    Wu, L.5    Zolla-Pazner, S.6    Nabel, G.J.7    Mascola, J.R.8
  • 82
    • 1842432386 scopus 로고    scopus 로고
    • Selective modification of variable loops alters tropism and enhances immunogenicity of human immunodeficiency virus type 1 envelope
    • Yang Z.Y., Chakrabarti B.K., Xu L., Welcher B., Kong W.P., Leung K., Panet A., Mascola J.R., Nabel G.J. Selective modification of variable loops alters tropism and enhances immunogenicity of human immunodeficiency virus type 1 envelope. J. Virol. 2004, 78:4029-4036.
    • (2004) J. Virol. , vol.78 , pp. 4029-4036
    • Yang, Z.Y.1    Chakrabarti, B.K.2    Xu, L.3    Welcher, B.4    Kong, W.P.5    Leung, K.6    Panet, A.7    Mascola, J.R.8    Nabel, G.J.9
  • 84
    • 33646744353 scopus 로고    scopus 로고
    • Improving on nature: focusing the immune response on the V3 loop
    • Zolla-Pazner S. Improving on nature: focusing the immune response on the V3 loop. Hum. Antibodies 2005, 14:69-72.
    • (2005) Hum. Antibodies , vol.14 , pp. 69-72
    • Zolla-Pazner, S.1
  • 85
    • 69249210887 scopus 로고    scopus 로고
    • Cross-clade neutralizing antibodies against HIV-1 induced in rabbits by focusing the immune response on a neutralizing epitope
    • Zolla-Pazner S., Cohen S., Pinter A., Krachmarov C., Wrin T., Wang S., Lu S. Cross-clade neutralizing antibodies against HIV-1 induced in rabbits by focusing the immune response on a neutralizing epitope. Virology 2009, 392:82-93.
    • (2009) Virology , vol.392 , pp. 82-93
    • Zolla-Pazner, S.1    Cohen, S.2    Pinter, A.3    Krachmarov, C.4    Wrin, T.5    Wang, S.6    Lu, S.7
  • 86
    • 39449107834 scopus 로고    scopus 로고
    • Focusing the immune response on the V3 loop, a neutralizing epitope of the HIV-1 gp120 envelope
    • Zolla-Pazner S., Cohen S.S., Krachmarov C., Wang S., Pinter A., Lu S. Focusing the immune response on the V3 loop, a neutralizing epitope of the HIV-1 gp120 envelope. Virology 2008, 372:233-246.
    • (2008) Virology , vol.372 , pp. 233-246
    • Zolla-Pazner, S.1    Cohen, S.S.2    Krachmarov, C.3    Wang, S.4    Pinter, A.5    Lu, S.6
  • 87


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