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• 4-133: The sera of 20 HIV-1 patients were screened for ADCC in a novel assay measuring granzyme B (GrB) and T cell elimination and reported that complex sera mediated greater levels of ADCC than anti-HIV mAbs. The data suggested that total amount of IgG bound is an important determinant of robust ADCC which improves the vaccine potency. 4-133 was cloned from serum exhibiting ADCC and used as an anti gp120 binding Ab to study effects of Ab specificity and affinity on ADCC against HIV-1 infected targets. Smalls-Mantey2012 (ADCC, assay or method development)
• 4-133: 134 unique anti-gp140 and 52 control non-gp140 reactive antibodies were studied for polyreactivity and its effect on binding affinity and neutralization. 75% of antibodies were polyreactive. 4-133 is sensitive to neutralization and binds to ssDNA, dsDNA, LPS (lipopolysaccharide), insulin, ANA (antinuclear antibody) and CL (cardiolipin). Both Somatically Mutated and Reverted 4-133 are polyreactive and bind with gp140, dsDNA, ssDNA, Insulin and LPS (lipopolysaccharide) but only Somatically Mutated 4-133 binds to Hep2 and is sensitive to neutralization. Somatically Mutated 4-133 neutralizes clade A, clade C and clade B (SF162.LS, BaL.26 and 6535.3) viruses whereas Reverted 2-470 does not neutralize any virus. Mouquet2010 (neutralization, binding affinity, antibody polyreactivity)
• 4-133: Substitutions in the CD4bs (E370A and/or D368A) or in close proximity to the CD4bs (N276A, R480A and Y384A) reduced binding of b12 but had no effect on binding activity of 4-133, indicating that binding characteristics of the anti-CD4bs Ab and anti-core Abs are distinct. Three mutations, D747A, M475A and R476A, had no effect on b12 binding but two (D474A and R476A) reduced binding of anti-core 4-133 MAb. These three residues were shown to be required for optimal viral infectivity. These results indicate that anti-core Abs recognize a conformational epitope including the α5 helix at the outer-domain-inner-domain junction of gp120. The epitope was highly conserved across different HIV-1 isolates. Pietzsch2010a (antibody binding site, optimal epitope, variant cross-reactivity, binding affinity)
• 4-133: This Ab was cloned from HIV envelope-binding memory B cells from a patient with broadly neutralizing Abs in serum, and was reactive to gp120 core, recognizing epitope in the vicinity of the CD4bs and the CD4i site. 4-133 was shown to have high affinity for gp140 and it competed with CD4bs and CD4i Abs for binding to gp140. 4-133 neutralized 4/5 Tier 1 and 1/5 Tier 2 viruses, but did not show broad serum-neutralizing activity. In total, 433 Abs were isolated from 6 patients, with neutralizing activity directed against several epitopes on gp120. Tier-2 neutralization was observed only with mixtures of MAbs, but only at high concentrations. Scheid2009 (antibody generation, neutralization, kinetics, binding affinity, antibody sequence)

References

Showing 4 of 4 references.

Isolation Paper
Scheid2009 Johannes F. Scheid, Hugo Mouquet, Niklas Feldhahn, Michael S. Seaman, Klara Velinzon, John Pietzsch, Rene G. Ott, Robert M. Anthony, Henry Zebroski, Arlene Hurley, Adhuna Phogat, Bimal Chakrabarti, Yuxing Li, Mark Connors, Florencia Pereyra, Bruce D. Walker, Hedda Wardemann, David Ho, Richard T. Wyatt, John R. Mascola, Jeffrey V. Ravetch, and Michel C. Nussenzweig. Broad Diversity of Neutralizing Antibodies Isolated from Memory B Cells in HIV-Infected Individuals. Nature, 458(7238):636-640, 2 Apr 2009. PubMed ID: 19287373. Show all entries for this paper.

Mouquet2010 Hugo Mouquet, Johannes F. Scheid, Markus J. Zoller, Michelle Krogsgaard, Rene G. Ott, Shetha Shukair, Maxim N. Artyomov, John Pietzsch, Mark Connors, Florencia Pereyra, Bruce D. Walker, David D. Ho, Patrick C. Wilson, Michael S. Seaman, Herman N. Eisen, Arup K. Chakraborty, Thomas J. Hope, Jeffrey V. Ravetch, Hedda Wardemann, and Michel C. Nussenzweig. Polyreactivity Increases the Apparent Affinity of Anti-HIV Antibodies by Heteroligation. Nature, 467(7315):591-595, 30 Sep 2010. PubMed ID: 20882016. Show all entries for this paper.

Pietzsch2010a John Pietzsch, Johannes F. Scheid, Hugo Mouquet, Florian Klein, Michael S. Seaman, Mila Jankovic, Davide Corti, Antonio Lanzavecchia, and Michel C. Nussenzweig. Human Anti-HIV-Neutralizing Antibodies Frequently Target a Conserved Epitope Essential for Viral Fitness. J. Exp. Med., 207(9):1995-2002, 30 Aug 2010. PubMed ID: 20679402. Show all entries for this paper.

Smalls-Mantey2012 Adjoa Smalls-Mantey, Nicole Doria-Rose, Rachel Klein, Andy Patamawenu, Stephen A. Migueles, Sung-Youl Ko, Claire W. Hallahan, Hing Wong, Bai Liu, Lijing You, Johannes Scheid, John C. Kappes, Christina Ochsenbauer, Gary J. Nabel, John R. Mascola, and Mark Connors. Antibody-Dependent Cellular Cytotoxicity against Primary HIV-Infected CD4+ T Cells Is Directly Associated with the Magnitude of Surface IgG Binding. J. Virol., 86(16):8672-8680, Aug 2012. PubMed ID: 22674985. Show all entries for this paper.