메뉴 건너뛰기




Volumn 584, Issue 8, 2010, Pages 1591-1596

Confocal microscopy of giant vesicles supports the absence of HIV-1 neutralizing 2F5 antibody reactivity to plasma membrane phospholipids

Author keywords

2F5; Broadly neutralizing antibody; Gp41; HIV 1 neutralization; Membrane proximal external region; Passive immunotherapy; Peptide vaccine

Indexed keywords

EPITOPE; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; MEMBRANE PHOSPHOLIPID; MONOCLONAL ANTIBODY 2F5;

EID: 77951296711     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.03.021     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 27544481277 scopus 로고    scopus 로고
    • The membrane-proximal external region of HIV-1 gp41: a vaccine target worth exploring
    • Zwick M.B. The membrane-proximal external region of HIV-1 gp41: a vaccine target worth exploring. AIDS 2005, 19:1725-1737.
    • (2005) AIDS , vol.19 , pp. 1725-1737
    • Zwick, M.B.1
  • 2
    • 40849136223 scopus 로고    scopus 로고
    • The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design
    • Montero M., van Houten N.E., Wang X., Scott J.K. The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design. Microbiol. Mol. Biol. Rev. 2008, 72:54-84.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 54-84
    • Montero, M.1    van Houten, N.E.2    Wang, X.3    Scott, J.K.4
  • 3
    • 45449105978 scopus 로고    scopus 로고
    • Interfacial pre-transmembrane domains in viral proteins promoting membrane fusion and fission
    • Lorizate M., Huarte N., Saez-Cirion A., Nieva J.L. Interfacial pre-transmembrane domains in viral proteins promoting membrane fusion and fission. Biochim. Biophys. Acta 2008, 1778:1624-1639.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1624-1639
    • Lorizate, M.1    Huarte, N.2    Saez-Cirion, A.3    Nieva, J.L.4
  • 4
    • 0037394318 scopus 로고    scopus 로고
    • Therapeutic potential of neutralizing antibodies in the treatment of HIV-1 infection
    • Stiegler G., Katinger H. Therapeutic potential of neutralizing antibodies in the treatment of HIV-1 infection. J. Antimicrob. Chemother. 2003, 51:757-759.
    • (2003) J. Antimicrob. Chemother. , vol.51 , pp. 757-759
    • Stiegler, G.1    Katinger, H.2
  • 5
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    • Ofek G., Tang M., Sambor A., Katinger H., Mascola J.R., Wyatt R., Kwong P.D. Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J. Virol. 2004, 78:10724-10737.
    • (2004) J. Virol. , vol.78 , pp. 10724-10737
    • Ofek, G.1    Tang, M.2    Sambor, A.3    Katinger, H.4    Mascola, J.R.5    Wyatt, R.6    Kwong, P.D.7
  • 7
    • 50949104097 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5
    • Huarte N., Lorizate M., Maeso R., Kunert R., Arranz R., Valpuesta J.M., Nieva J.L. The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5. J. Virol. 2008, 82:8986-8996.
    • (2008) J. Virol. , vol.82 , pp. 8986-8996
    • Huarte, N.1    Lorizate, M.2    Maeso, R.3    Kunert, R.4    Arranz, R.5    Valpuesta, J.M.6    Nieva, J.L.7
  • 8
    • 67049156802 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface
    • Song L., et al. Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface. Proc. Natl. Acad. Sci. USA 2009, 106:9057-9062.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9057-9062
    • Song, L.1
  • 9
    • 70349272203 scopus 로고    scopus 로고
    • Stable docking of neutralizing human immunodeficiency virus type 1 gp41 membrane-proximal external region monoclonal antibodies 2F5 and 4E10 is dependent on the membrane immersion depth of their epitope regions
    • Dennison S.M., Stewart S.M., Stempel K.C., Liao H.X., Haynes B.F., Alam S.M. Stable docking of neutralizing human immunodeficiency virus type 1 gp41 membrane-proximal external region monoclonal antibodies 2F5 and 4E10 is dependent on the membrane immersion depth of their epitope regions. J. Virol. 2009, 83:10211-10223.
    • (2009) J. Virol. , vol.83 , pp. 10211-10223
    • Dennison, S.M.1    Stewart, S.M.2    Stempel, K.C.3    Liao, H.X.4    Haynes, B.F.5    Alam, S.M.6
  • 10
    • 21344434534 scopus 로고    scopus 로고
    • Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies
    • Haynes B.F., et al. Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science 2005, 308:1906-1908.
    • (2005) Science , vol.308 , pp. 1906-1908
    • Haynes, B.F.1
  • 11
    • 21744447837 scopus 로고    scopus 로고
    • Immunology. Close to the edge: neutralizing the HIV-1 envelope
    • Nabel G.J. Immunology. Close to the edge: neutralizing the HIV-1 envelope. Science 2005, 308:1878-1879.
    • (2005) Science , vol.308 , pp. 1878-1879
    • Nabel, G.J.1
  • 12
    • 37349086800 scopus 로고    scopus 로고
    • Reassessment of autoreactivity of the broadly neutralizing HIV antibodies 4E10 and 2F5 and retrospective analysis of clinical safety data
    • Vcelar B., et al. Reassessment of autoreactivity of the broadly neutralizing HIV antibodies 4E10 and 2F5 and retrospective analysis of clinical safety data. AIDS 2007, 21:2161-2170.
    • (2007) AIDS , vol.21 , pp. 2161-2170
    • Vcelar, B.1
  • 13
    • 37349058177 scopus 로고    scopus 로고
    • Difficulties in eliciting broadly neutralizing anti-HIV antibodies are not explained by cardiolipin autoreactivity
    • Scherer E.M., Zwick M.B., Teyton L., Burton D.R. Difficulties in eliciting broadly neutralizing anti-HIV antibodies are not explained by cardiolipin autoreactivity. AIDS 2007, 21:2131-2139.
    • (2007) AIDS , vol.21 , pp. 2131-2139
    • Scherer, E.M.1    Zwick, M.B.2    Teyton, L.3    Burton, D.R.4
  • 14
    • 43149113443 scopus 로고    scopus 로고
    • 4E10 and 2F5 monoclonal antibodies: binding specificities to phospholipids, tolerance, and clinical safety issues
    • Alving C.R. 4E10 and 2F5 monoclonal antibodies: binding specificities to phospholipids, tolerance, and clinical safety issues. AIDS 2008, 22:649-651.
    • (2008) AIDS , vol.22 , pp. 649-651
    • Alving, C.R.1
  • 15
    • 25144443228 scopus 로고    scopus 로고
    • Cellular lipidomics
    • van Meer G. Cellular lipidomics. EMBO J. 2005, 24:3159-3165.
    • (2005) EMBO J. , vol.24 , pp. 3159-3165
    • van Meer, G.1
  • 16
    • 34547614075 scopus 로고    scopus 로고
    • Bilayers as protein solvents: role of bilayer structure and elastic properties
    • McIntosh T.J., Simon S.A. Bilayers as protein solvents: role of bilayer structure and elastic properties. J. Gen. Physiol. 2007, 130:225-227.
    • (2007) J. Gen. Physiol. , vol.130 , pp. 225-227
    • McIntosh, T.J.1    Simon, S.A.2
  • 17
    • 77951884081 scopus 로고    scopus 로고
    • Membrane rafting: from apical sorting to phase segregation. FEBS Lett., doi:10.1016/j.febslet.2009.12.043.
    • Coskun, Ü. and Simons, K. (2010) Membrane rafting: from apical sorting to phase segregation. FEBS Lett., doi:10.1016/j.febslet.2009.12.043.
    • (2010)
    • Coskun, Ü.1    Simons, K.2
  • 18
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D., Simons K. Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 19
    • 0028155283 scopus 로고
    • Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization
    • Buchacher A., et al. Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization. AIDS Res. Hum. Retroviruses 1994, 10:359-369.
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , pp. 359-369
    • Buchacher, A.1
  • 20
    • 0034606680 scopus 로고    scopus 로고
    • Stable recombinant expression of the anti HIV-1 monoclonal antibody 2F5 after IgG3/IgG1 subclass switch in CHO cells
    • Kunert R., Steinfellner W., Purtscher M., Assadian A., Katinger H. Stable recombinant expression of the anti HIV-1 monoclonal antibody 2F5 after IgG3/IgG1 subclass switch in CHO cells. Biotechnol. Bioeng. 2000, 67:97-103.
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 97-103
    • Kunert, R.1    Steinfellner, W.2    Purtscher, M.3    Assadian, A.4    Katinger, H.5
  • 22
    • 34447255173 scopus 로고    scopus 로고
    • Pore formation by a Bax-derived peptide: effect on the line tension of the membrane probed by AFM
    • Garcia-Saez A.J., Chiantia S., Salgado J., Schwille P. Pore formation by a Bax-derived peptide: effect on the line tension of the membrane probed by AFM. Biophys. J. 2007, 93:103-112.
    • (2007) Biophys. J. , vol.93 , pp. 103-112
    • Garcia-Saez, A.J.1    Chiantia, S.2    Salgado, J.3    Schwille, P.4
  • 23
    • 36348937414 scopus 로고    scopus 로고
    • Effect of line tension on the lateral organization of lipid membranes
    • Garcia-Saez A.J., Chiantia S., Schwille P. Effect of line tension on the lateral organization of lipid membranes. J. Biol. Chem. 2007, 282:33537-33544.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33537-33544
    • Garcia-Saez, A.J.1    Chiantia, S.2    Schwille, P.3
  • 24
    • 33646394886 scopus 로고    scopus 로고
    • Specific phospholipid recognition by human immunodeficiency virus type-1 neutralizing anti-gp41 2F5 antibody
    • Sanchez-Martinez S., Lorizate M., Hermann K., Kunert R., Basanez G., Nieva J.L. Specific phospholipid recognition by human immunodeficiency virus type-1 neutralizing anti-gp41 2F5 antibody. FEBS Lett. 2006, 580:2395-2399.
    • (2006) FEBS Lett. , vol.580 , pp. 2395-2399
    • Sanchez-Martinez, S.1    Lorizate, M.2    Hermann, K.3    Kunert, R.4    Basanez, G.5    Nieva, J.L.6
  • 25
    • 33947635198 scopus 로고    scopus 로고
    • The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes
    • Alam S.M., et al. The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes. J. Immunol. 2007, 178:4424-4435.
    • (2007) J. Immunol. , vol.178 , pp. 4424-4435
    • Alam, S.M.1
  • 26
    • 60549089534 scopus 로고    scopus 로고
    • Lipid binding properties of 4E10, 2F5, and WR304 monoclonal antibodies that neutralize HIV-1
    • Matyas G.R., Beck Z., Karasavvas N., Alving C.R. Lipid binding properties of 4E10, 2F5, and WR304 monoclonal antibodies that neutralize HIV-1. Biochim. Biophys. Acta 2009, 1788:660-665.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 660-665
    • Matyas, G.R.1    Beck, Z.2    Karasavvas, N.3    Alving, C.R.4
  • 27
    • 11144227042 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1
    • Zwick M.B., Jensen R., Church S., Wang M., Stiegler G., Kunert R., Katinger H., Burton D.R. Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1. J. Virol. 2005, 79:1252-1261.
    • (2005) J. Virol. , vol.79 , pp. 1252-1261
    • Zwick, M.B.1    Jensen, R.2    Church, S.3    Wang, M.4    Stiegler, G.5    Kunert, R.6    Katinger, H.7    Burton, D.R.8
  • 28
    • 43949135190 scopus 로고    scopus 로고
    • Importance of the membrane-perturbing properties of the membrane-proximal external region of human immunodeficiency virus type 1 gp41 to viral fusion
    • Vishwanathan S.A., Hunter E. Importance of the membrane-perturbing properties of the membrane-proximal external region of human immunodeficiency virus type 1 gp41 to viral fusion. J. Virol. 2008, 82:5118-5126.
    • (2008) J. Virol. , vol.82 , pp. 5118-5126
    • Vishwanathan, S.A.1    Hunter, E.2
  • 29
    • 47749109057 scopus 로고    scopus 로고
    • Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence
    • Schon P., Garcia-Saez A.J., Malovrh P., Bacia K., Anderluh G., Schwille P. Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence. Biophys. J. 2008, 95:691-698.
    • (2008) Biophys. J. , vol.95 , pp. 691-698
    • Schon, P.1    Garcia-Saez, A.J.2    Malovrh, P.3    Bacia, K.4    Anderluh, G.5    Schwille, P.6
  • 30
    • 0242331729 scopus 로고    scopus 로고
    • Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension
    • Baumgart T., Hess S.T., Webb W.W. Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension. Nature 2003, 425:821-824.
    • (2003) Nature , vol.425 , pp. 821-824
    • Baumgart, T.1    Hess, S.T.2    Webb, W.W.3
  • 31
    • 69249215233 scopus 로고    scopus 로고
    • Biomimetic membrane systems to study cellular organization
    • Loose M., Schwille P. Biomimetic membrane systems to study cellular organization. J. Struct. Biol. 2009, 168:143-151.
    • (2009) J. Struct. Biol. , vol.168 , pp. 143-151
    • Loose, M.1    Schwille, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.