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Displaying record number 2728
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10-188:This study identified a B cell lineage of bNAbs in an HIV-1 elite post-treatment controller (ePTC; donor: PTC-005002). Circulating viruses in PTC escaped bNAb pressure but remained sensitive to autologous neutralization by other Ab populations. Anti-V3 crown antibody 10-188 was included as a positive control for SOSIP binding in ELISA.
Molinos-Albert2023
(binding affinity)
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10-188: IgA and IgG bNAbs of 3 distinct B cell lineages were characterized in a viremic controller (pt7). Two lineages comprised only IgG+ or IgA+ blood memory B cells; the third combined both IgG and IgA clonal variants. BNAb 7-269 in the IgA-only lineage displayed the highest neutralizing capacity despite limited somatic mutation. Immunotherapy with 7-269 in humanized mice delayed viral rebound. AD8-infected cell killing by primary human natural killer (NK) cells via ADCC was observed with all pt7 bNAbs binding strongly to target cells and expressed as IgGs, except for 7-155. BNAbs in all three lineages targeted the N332 glycan supersite. Epitope mapping showed that all pt7 IgA and IgG bNAbs target the high-mannose patch centered on the N332 glycan without interacting with the V3 loop base, which contrasts with numerous bNAbs targeting the N332 supersite. The cryo-EM structure of 7-269 in complex with BG505 SOSIP revealed an epitope mainly composed of sugar residues comprising the N332 and N295 glycans; onto which 7-269 positions itself in a structurally similar way to 2G12. Binding and cryo-EM structural analyses showed that antibodies from the two other lineages interact mostly with glycans N332 and N386. Hence, multiple B cell lineages of IgG and IgA bNAbs focused on a unique HIV-1 site of vulnerability can codevelop in HIV-1 viremic controllers. Other antibodies used as controls included 10-188, 3BNC117, PGT121, PGT135, 10-1074, BG8, BG18, and SF12.
Lorin2022
(antibody binding site, binding affinity, structure)
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10-188: Somatic hypermutations are preferably found in CDR loops, which alter the Ab combining sites, but not the overall structure of the variable domain. FWR of CDR are usually resistant to and less tolerant of mutations. This study reports that most bnAbs require somatic mutations in the FWRs which provide flexibility, increasing Ab breadth and potency. To determine the consequence of FWR mutations the framework residues were reverted to the Ab's germline counterpart (FWR-GL) and binding and neutralizing properties were then evaluated. 10-188 had limited neutralizing activity recognizing the V3 loop and carrieding fewer somatic mutations than bnAbs. 10-188 FWR-GL showed decreased binding.
Klein2013
(neutralization, structure, antibody lineage)
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10-188: Several antibodies including 10-1074 were isolated from B-cell clone encoding PGT121, from a clade A-infected African donor using YU-2 gp140 trimers as bait. These antibodies were segregated into PGT121-like (PGT121-123 and 9 members) and 10-1074-like (20 members) groups distinguished by sequence, binding affinity, carbohydrate recognition, neutralizing activity, the V3 loop binding and the role of glycans in epitope formation. The epitopes for both groups contain a potential N-linked glycosylation site (PNGS) at Asn332gp120 and the base of the V3 loop of the gp120 subunit of the HIV spike. However, the 10-1074–like Abs required an intact PNGS at Asn332gp120 for their neutralizing activity, whereas PGT121-like antibodies were able to neutralize some viral strains lacking the Asn332gp120 PNGS. 10-188 was used as a control in virus neutralization assay. Detail information on the binding and neutralization assays are described in the figures S2-S11.
Mouquet2012a
(antibody generation, glycosylation, neutralization, binding affinity)
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10-188: A bispecific Ab (BiAb) that can bind bivalently by virtue of one scFv arm recognizing gp120 and a second arm recognizing gp41, has been engineered to show increased neutralizing potency. 10-188 antibody was used to produce homodimeric scFvs (scFv2-Fc). Purified 10-188 scFv2-Fc recognized artificial YU-2gp140 trimers and YU-2 gp120 with the same binding profile as 10-188 IgG. BiAb 10-188/5-25 and corresponding negative control 10-188/mGO53 were designed with non HIV antibody mG053. Repertoire and reactivity of the antibodies are described in Table S1.
Mouquet2012
(neutralization, binding affinity, broad neutralizer)
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10-188: YU2 gp140 bait was used to characterize 189 new MAbs representing 51 independent IgG memory B cell clones from 3 clade A or B HIV infected patients exhibiting broad neutralizing activity. None of the individual antibodies exhibited bNAb properties, suggesting a potential lack of efficiency of the single-cell capture method used in this paper. 10-188 antibody, however, neutralized 100% of Tier-1 HIV viruses and 19% of Tier-2 HIV viruses tested. This MAb, along with clonally related 10-380, ranked in the top 5% of neutralizers in the paper. VH-CDR3(aa): YGDIYWAPPEDHDYYGMDV VHmut:36; VL-l CDR3:AAWDDSLNGPV; Vk/l mut:28. Heavy and light chain genes are listed in Table S2. Ab sequence and epitope mapping is shown in Figure 6.
Mouquet2011
(antibody generation, neutralization, antibody sequence)
References
Showing 6 of
6 references.
Isolation Paper
Mouquet2011
Hugo Mouquet, Florian Klein, Johannes F. Scheid, Malte Warncke, John Pietzsch, Thiago Y. K. Oliveira, Klara Velinzon, Michael S. Seaman, and Michel C. Nussenzweig. Memory B Cell Antibodies to HIV-1 gp140 Cloned from Individuals Infected with Clade A and B Viruses. PLoS One, 6(9):e24078, 2011. PubMed ID: 21931643.
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Klein2013
Florian Klein, Ron Diskin, Johannes F. Scheid, Christian Gaebler, Hugo Mouquet, Ivelin S. Georgiev, Marie Pancera, Tongqing Zhou, Reha-Baris Incesu, Brooks Zhongzheng Fu, Priyanthi N. P. Gnanapragasam, Thiago Y. Oliveira, Michael S. Seaman, Peter D. Kwong, Pamela J. Bjorkman, and Michel C. Nussenzweig. Somatic Mutations of the Immunoglobulin Framework Are Generally Required for Broad and Potent HIV-1 Neutralization. Cell, 153(1):126-138, 28 Mar 2013. PubMed ID: 23540694.
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Lorin2022
Valérie Lorin, Ignacio Fernández, Guillemette Masse-Ranson, Mélanie Bouvin-Pley, Luis M. Molinos-Albert, Cyril Planchais, Thierry Hieu, Gérard Péhau-Arnaudet, Dominik Hrebik, Giulia Girelli-Zubani, Oriane Fiquet, Florence Guivel-Benhassine, Rogier W. Sanders, Bruce D. Walker, Olivier Schwartz, Johannes F. Scheid, Jordan D. Dimitrov, Pavel Plevka, Martine Braibant, Michael S. Seaman, François Bontems, James P. Di Santo, Félix A. Rey, and Hugo Mouquet. Epitope Convergence of Broadly HIV-1 Neutralizing IgA and IgG Antibody Lineages in a Viremic Controller. J. Exp. Med., 219(3), 7 Mar 2022. PubMed ID: 35230385.
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Mouquet2012
Hugo Mouquet, Malte Warncke, Johannes F. Scheid, Michael S. Seaman, and Michel C. Nussenzweig. Enhanced HIV-1 Neutralization by Antibody Heteroligation. Proc. Natl. Acad. Sci. U.S.A., 109(3):875-880, 17 Jan 2012. PubMed ID: 22219363.
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Mouquet2012a
Hugo Mouquet, Louise Scharf, Zelda Euler, Yan Liu, Caroline Eden, Johannes F. Scheid, Ariel Halper-Stromberg, Priyanthi N. P. Gnanapragasam, Daniel I. R. Spencer, Michael S. Seaman, Hanneke Schuitemaker, Ten Feizi, Michel C. Nussenzweig, and Pamela J. Bjorkman. Complex-Type N-Glycan Recognition by Potent Broadly Neutralizing HIV Antibodies. Proc. Natl. Acad. Sci. U.S.A, 109(47):E3268-E3277, 20 Nov 2012. PubMed ID: 23115339.
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Molinos-Albert2023
Luis M. Molinos-Albert, Eduard Baquero, Melanie Bouvin-Pley, Valerie Lorin, Caroline Charre, Cyril Planchais, Jordan D. Dimitrov, Valerie Monceaux, Matthijn Vos, Laurent Hocqueloux, Jean-Luc Berger, Michael S. Seaman, Martine Braibant, Veronique Avettand-Fenoel, Asier Saez-Cirion, and Hugo Mouquet. Anti-V1/V3-glycan broadly HIV-1 neutralizing antibodies in a post-treatment controller. Cell Host Microbe, 31(8):1275-1287e8 doi, Aug 2023. PubMed ID: 37433296
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Displaying record number 2772
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Notes
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1 note.
-
10-380: YU2 gp140 bait was used to characterize 189 new MAbs representing 51 independent IgG memory B cell clones from 3 clade A or B HIV infected patients exhibiting broad neutralizing activity. None of the individual antibodies exhibited bNAb properties, suggesting a potential lack of efficiency of the single-cell capture method used in this paper. 10-380 antibody neutralized 83% of Tier-1 HIV viruses and 15% of Tier-2 HIV viruses tested. This MAb, along with clonally related 10-188, ranked in the top 5% of neutralizers in the paper. VH-CDR3(aa):YGDIYWSPPPPEEYDYVGVDV VHmut:36; VL-l CDR3:ATWDASLNRPT Vk/l mut:30. Heavy and light chain genes are listed in Table S2. Ab sequence and epitope mapping is shown in Figure 6.
Mouquet2011
(antibody generation, neutralization, antibody sequence)
References
Showing 1 of
1 reference.
Isolation Paper
Mouquet2011
Hugo Mouquet, Florian Klein, Johannes F. Scheid, Malte Warncke, John Pietzsch, Thiago Y. K. Oliveira, Klara Velinzon, Michael S. Seaman, and Michel C. Nussenzweig. Memory B Cell Antibodies to HIV-1 gp140 Cloned from Individuals Infected with Clade A and B Viruses. PLoS One, 6(9):e24078, 2011. PubMed ID: 21931643.
Show all entries for this paper.
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