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Notes

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• 2.2C: The results confirm that Nef and Vpu protect HIV-1-infected cells from ADCC, but also show that not all classes of antibody can mediate ADCC. Anti-cluster-A antibodies are able to mediate potent ADCC responses, whereas anti-coreceptor binding site antibodies are not. Position 69 in gp120 is important for antibody-mediated cellular toxicity by anti-cluster-A antibodies. The angle of approach of a given class of antibodies could impact its capacity to mediate ADCC. Mabs A32, N12-i3, 2.2c, N26-i1, and N5-i5, were used as ADCC-positive anti-cluster A Abs. Ding2015 (ADCC)
• 22C: LANL database note: This monoclonal antibody is a CHAVI reagent (http://chavi.org/); Species: human; Category: A32 and A32-like; Contact person: James Robinson
• 2.2c: The discordance between ADCC (Ab-dependent cellular cytotoxicity) responses and antibody-binding responses at A32-like binding sites was explained by comparing the crystal structures of 2 Abs with overlapping epitopes, N5-i5 and 2.2c. Differences were found in precise angle of epitope targeting (orientation) and mode of antibody attachment (formation of multivalent gp120-antibody complexes) in ADCC responses, the latter having greater effect. N5-i5 has a 75-fold better ADCC potency than Ab 2.2c. Acharya2014 (ADCC, binding affinity, structure)
• 2.2C: 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. 2.2C was used as an anti-gp120 constant region Ab to study effects of Ab specificity and affinity on ADCC against HIV-1 infected targets. Smalls-Mantey2012 (ADCC, assay or method development)
• 2.2C: Resurfaced stabilized core 3 (RSC3) protein was designed to preserve the antigenic structure of the gp120 CD4bs neutralizing surface but eliminate other antigenic regions of HIV-1. RSC3 did not show binding to 2.2C. Wu2010 (binding affinity)

References

Showing 4 of 4 references.

Acharya2014 Priyamvada Acharya, William D. Tolbert, Neelakshi Gohain, Xueji Wu, Lei Yu, Tongyun Liu, Wensheng Huang, Chih-chin Huang, Young Do Kwon, Robert K. Louder, Timothy S. Luongo, Jason S. McLellan, Marie Pancera, Yongping Yang, Baoshan Zhang, Robin Flinko, James S. Foulke, Jr., Mohammad M. Sajadi, Roberta Kamin-Lewis, James E. Robinson, Loïc Martin, Peter D. Kwong, Yongjun Guan, Anthony L. DeVico, George K. Lewis, and Marzena Pazgier. Structural Definition of an Antibody-Dependent Cellular Cytotoxicity Response Implicated in Reduced Risk for HIV-1 Infection. J. Virol., 88(21):12895-12906, Nov 2014. PubMed ID: 25165110. Show all entries for this paper.

Ding2015 Shilei Ding, Maxime Veillette, Mathieu Coutu, Jérémie Prévost, Louise Scharf, Pamela J. Bjorkman, Guido Ferrari, James E. Robinson, Christina Stürzel, Beatrice H. Hahn, Daniel Sauter, Frank Kirchhoff, George K. Lewis, Marzena Pazgier, and Andrés Finzi. A Highly Conserved Residue of the HIV-1 gp120 Inner Domain Is Important for Antibody-Dependent Cellular Cytotoxicity Responses Mediated by Anti-cluster A Antibodies. J. Virol., 90(4):2127-2134, Feb 2016. PubMed ID: 26637462. 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.

Wu2010 Xueling Wu, Zhi-Yong Yang, Yuxing Li, Carl-Magnus Hogerkorp, William R. Schief, Michael S. Seaman, Tongqing Zhou, Stephen D. Schmidt, Lan Wu, Ling Xu, Nancy S. Longo, Krisha McKee, Sijy O'Dell, Mark K. Louder, Diane L. Wycuff, Yu Feng, Martha Nason, Nicole Doria-Rose, Mark Connors, Peter D. Kwong, Mario Roederer, Richard T. Wyatt, Gary J. Nabel, and John R. Mascola. Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1. Science, 329(5993):856-861, 13 Aug 2010. PubMed ID: 20616233. Show all entries for this paper.