Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding
Abstract
The HIV-1 envelope glycoprotein (Env) undergoes conformational transitions consequent to CD4 binding and coreceptor engagement during viral entry. The physical steps in this process are becoming defined, but less is known about their significance as targets of antibodies potentially protective against HIV-1 infection. Here we probe the functional significance of transitional epitope exposure by characterizing 41 human mAbs specific for epitopes exposed on trimeric Env after CD4 engagement. These mAbs recognize three epitope clusters: cluster A, the gp120 face occluded by gp41 in trimeric Env; cluster B, a region proximal to the coreceptor-binding site (CoRBS) and involving the V1/V2 domain; and cluster C, the coreceptor-binding site. The mAbs were evaluated functionally by antibody-dependent, cell-mediated cytotoxicity (ADCC) and for neutralization of Tiers 1 and 2 pseudoviruses. All three clusters included mAbs mediating ADCC. However, there was a strong potency bias for cluster A, which harbors at least three potent ADCC epitopes whose cognate mAbs have electropositive paratopes. Cluster A epitopes are functional ADCC targets during viral entry in an assay format using virion-sensitized target cells. In contrast, only cluster C contained epitopes that were recognized by neutralizing mAbs. There was significant diversity in breadth and potency that correlated with epitope finemore »
- Authors:
-
- Univ. of Maryland School of Medicine, Baltimore, MD (United States)
- Tulane Univ., New Orleans, LA (United States)
- Harvard Medical School, Boston, MA (United States)
- Profectus Biosciences, Inc., Baltimore, MD (United States)
- Publication Date:
- Research Org.:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1136677
- Report Number(s):
- SLAC-REPRINT-2014-212
Journal ID: ISSN 0027-8424
- Grant/Contract Number:
- AC02-76SF00515
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Proceedings of the National Academy of Sciences of the United States of America
- Additional Journal Information:
- Journal Volume: 110; Journal Issue: 1; Journal ID: ISSN 0027-8424
- Publisher:
- National Academy of Sciences, Washington, DC (United States)
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Guan, Yongjun, Pazgier, Marzena, Sajadi, Mohammad M., Kamin-Lewis, Roberta, Al-Darmarki, Salma, Flinko, Robin, Lovo, Elena, Wu, Xueji, Robinson, James E., Seaman, Michael S., Fouts, Timothy R., Gallo, Robert C., DeVico, Anthony L., and Lewis, George K. Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding. United States: N. p., 2012.
Web. doi:10.1073/pnas.1217609110.
Guan, Yongjun, Pazgier, Marzena, Sajadi, Mohammad M., Kamin-Lewis, Roberta, Al-Darmarki, Salma, Flinko, Robin, Lovo, Elena, Wu, Xueji, Robinson, James E., Seaman, Michael S., Fouts, Timothy R., Gallo, Robert C., DeVico, Anthony L., & Lewis, George K. Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding. United States. https://doi.org/10.1073/pnas.1217609110
Guan, Yongjun, Pazgier, Marzena, Sajadi, Mohammad M., Kamin-Lewis, Roberta, Al-Darmarki, Salma, Flinko, Robin, Lovo, Elena, Wu, Xueji, Robinson, James E., Seaman, Michael S., Fouts, Timothy R., Gallo, Robert C., DeVico, Anthony L., and Lewis, George K. Thu .
"Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding". United States. https://doi.org/10.1073/pnas.1217609110. https://www.osti.gov/servlets/purl/1136677.
@article{osti_1136677,
title = {Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding},
author = {Guan, Yongjun and Pazgier, Marzena and Sajadi, Mohammad M. and Kamin-Lewis, Roberta and Al-Darmarki, Salma and Flinko, Robin and Lovo, Elena and Wu, Xueji and Robinson, James E. and Seaman, Michael S. and Fouts, Timothy R. and Gallo, Robert C. and DeVico, Anthony L. and Lewis, George K.},
abstractNote = {The HIV-1 envelope glycoprotein (Env) undergoes conformational transitions consequent to CD4 binding and coreceptor engagement during viral entry. The physical steps in this process are becoming defined, but less is known about their significance as targets of antibodies potentially protective against HIV-1 infection. Here we probe the functional significance of transitional epitope exposure by characterizing 41 human mAbs specific for epitopes exposed on trimeric Env after CD4 engagement. These mAbs recognize three epitope clusters: cluster A, the gp120 face occluded by gp41 in trimeric Env; cluster B, a region proximal to the coreceptor-binding site (CoRBS) and involving the V1/V2 domain; and cluster C, the coreceptor-binding site. The mAbs were evaluated functionally by antibody-dependent, cell-mediated cytotoxicity (ADCC) and for neutralization of Tiers 1 and 2 pseudoviruses. All three clusters included mAbs mediating ADCC. However, there was a strong potency bias for cluster A, which harbors at least three potent ADCC epitopes whose cognate mAbs have electropositive paratopes. Cluster A epitopes are functional ADCC targets during viral entry in an assay format using virion-sensitized target cells. In contrast, only cluster C contained epitopes that were recognized by neutralizing mAbs. There was significant diversity in breadth and potency that correlated with epitope fine specificity. In contrast, ADCC potency had no relationship with neutralization potency or breadth for any epitope cluster. In conclusion, Fc-mediated effector function and neutralization coselect with specificity in anti-Env antibody responses, but the nature of selection is distinct for these two antiviral activities.},
doi = {10.1073/pnas.1217609110},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 1,
volume = 110,
place = {United States},
year = {Thu Dec 13 00:00:00 EST 2012},
month = {Thu Dec 13 00:00:00 EST 2012}
}
Web of Science
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Dual-Affinity Re-Targeting proteins direct T cell–mediated cytolysis of latently HIV-infected cells
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Quantifying Anti-HIV Envelope-Specific Antibodies in Plasma from HIV Infected Individuals
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Adaption of human antibody λ and κ light chain architectures to CDR repertoires
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Incomplete Downregulation of CD4 Expression Affects HIV-1 Env Conformation and Antibody-Dependent Cellular Cytotoxicity Responses
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Uninfected Bystander Cells Impact the Measurement of HIV-Specific Antibody-Dependent Cellular Cytotoxicity Responses
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Stabilizing Exposure of Conserved Epitopes by Structure Guided Insertion of Disulfide Bond in HIV-1 Envelope Glycoprotein
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Preparation and Evaluation of the Fully Humanized Monoclonal Antibody GD-mAb Against Respiratory Syncytial Virus
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The Early Antibody-Dependent Cell-Mediated Cytotoxicity Response Is Associated With Lower Viral Set Point in Individuals With Primary HIV Infection
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Concurrent Exposure of Neutralizing and Non-neutralizing Epitopes on a Single HIV-1 Envelope Structure
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A Sample-Sparing Multiplexed ADCP Assay
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Antibody-Dependent Cellular Cytotoxicity (ADCC)-Mediating Antibodies Constrain Neutralizing Antibody Escape Pathway
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Structural Basis for Epitopes in the gp120 Cluster A Region that Invokes Potent Effector Cell Activity
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Quantifying Anti-HIV Envelope-Specific Antibodies in Plasma from HIV Infected Individuals
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Conformational Masking and Receptor-Dependent Unmasking of Highly Conserved Env Epitopes Recognized by Non-Neutralizing Antibodies That Mediate Potent ADCC against HIV-1
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