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• 2G6: 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)
• 2G6: Binds to JRFL oligomer with an affinity comparable to IgG1b12, but does not neutralize the virus, so binding of oligomer is not always predictive of neutralization -- conclusions of this paper contrast with Parren1998 -- authors propose a model where 205-46-9 and 2G6 may inhibit CD4 binding, but cause a conformational shift which enhances CCR5 binding and thus counteracts the neutralizing effect Fouts1998. Fouts1998,Parren1998 (antibody binding site, variant cross-reactivity)

References

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Fouts1998 T. R. Fouts, A. Trkola, M. S. Fung, and J. P. Moore. Interactions of Polyclonal and Monoclonal Anti-Glycoprotein 120 Antibodies with Oligomeric Glycoprotein 120-Glycoprotein 41 Complexes of a Primary HIV Type 1 Isolate: Relationship to Neutralization. AIDS Res. Hum. Retroviruses, 14:591-597, 1998. Ab reactivity to oligomeric forms of gp120 were compared to neutralization of the macrophage tropic primary virus JRFL, and did not always correlate. This builds upon studies which have shown that oligomer binding while required for neutralization, is not always sufficient. MAb 205-46-9 and 2G6 bind oligomer with high affinity, comparable to IgG1b12, but unlike IgG1b12, cannot neutralize JRFL. Furthermore, neutralizing and non-neutralizing sera from HIV-1 infected people are similar in their reactivities to oligomeric JRFL Envelope. PubMed ID: 9591713. 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.

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.