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Notes

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• b14: The original Fab fragment was derived from a combinatorial phage library from bone marrow of an HIV-1 positive individual who had been asymptomatic for six years. It was subsequently sequenced by Barbas1993. Barbas1993,Burton1991 (antibody generation)
• b14: This review summarizes MAbs directed to HIV-1 Env. There are 51 CD4BS MAbs and Fabs in the database; most, like this Fab, neutralize TCLA strains only. Gorny2003 (review)
• b14: The rank order of Fab binding affinity to monomeric gp120 (Loop 2 > 3B3 > b12 = DO8i > b11 > b3 > b14 > b13 > DO142-10 > DA48 > L17) was markedly different than Fab binding affinity to the mature oligomeric form (3B3 > b12 > DO142-10 > Loop 2 > b11 > L17 > b6 > DO8i > b14 > DA48 > b3 > b13) and binding to oligomeric form and neutralization were correlated for both Fabs and MAbs -- authors suggest that neutralization is determined by the fraction of Ab sites occupied on a virion irrespective of the epitope. Parren1998 (binding affinity)

References

Showing 4 of 4 references.

Isolation Paper
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.