HIV molecular immunology database
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|HXB2 Location||Env||Env Epitope Map|
|Ab Type||gp120 CD4BS|
|Keywords||antibody generation, binding affinity, review|
Showing 3 of 3 notes.
Showing 4 of 4 references.
Burton1991 D. R. Burton, C. F. Barbas III, M. A. Persson, S. Koenig, R. M. Chanock, and R. A. Lerner. A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc. Natl. Acad. Sci. U.S.A., 88:10134-10137, 1991. A panel of human monoclonal antibody Fab fragments was generated against the surface of the gp120 glycoprotein of HIV-1 by antigen selection from a random combinatorial library prepared from 5 ml of bone marrow from an asymptomatic individual who had been HIV-positive for 6 years. These Fab variable regions were sequenced and were found to be diverse. Binding constants were measured and the Fabs generally bound gp120 with high affinity. The methods used to obtain this panel could be used to obtain antibodies to test passive immunization as a therapy for AIDS. PubMed ID: 1719545. Show all entries for this paper.
Gorny2003 Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162. Show all entries for this paper.
Parren1998 P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629. Show all entries for this paper.
Barbas1993 C. F. Barbas III, T. A. Collet, P. Roben, J. Binley, W. Amberg, D. Hoekstra, D. Cabana, T. M. Jones, R. A. Williamson, G. R. Pilkington, N. L. Haigwood, A. C. Satterthwait, I. Sanz, and D. R. Burton. Molecular profile of an antibody response to HIV-1 as probed by combinatorial libraries. J. Mol. Biol., 230:812-823, 1993. PubMed ID: 8478936. Show all entries for this paper.