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Related Experiment Video

Updated: Mar 6, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

Published on: September 14, 2014

HIV-1 Consensus Envelope-Induced Broadly Binding Antibodies.

R Ryan Meyerhoff^1,2, Richard M Scearce¹, Damon F Ogburn¹

¹1 Duke Human Vaccine Institute, Duke University School of Medicine , Durham, North Carolina.

AIDS Research and Human Retroviruses

|March 19, 2017

Summary

Monoclonal antibodies targeting HIV-1 envelopes (Envs) were characterized. Specific antibodies bind conserved epitopes on gp120, with potential for HIV-1 diagnostics and therapeutics.

Keywords:

ADCC HIV antibody-mediated immunity monoclonal vaccine design

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Area of Science:

Immunology and Virology
Structural Biology of Viral Proteins

Background:

Antibodies cross-reactive with multiple Human Immunodeficiency Virus type 1 (HIV-1) envelopes (Envs) are valuable tools for Env protein characterization and purification.
Previous work identified ten murine monoclonal antibodies (mAbs) from CON-6 immunization exhibiting broad Env cross-reactivity.

Purpose of the Study:

To delineate the specific epitopes on HIV-1 Env proteins recognized by the previously identified cross-reactive monoclonal antibodies.
To assess the potential utility of these antibodies in diagnostic and therapeutic applications, including targeting infected cells.

Main Methods:

Epitope mapping of seven murine monoclonal antibodies to linear regions within the gp120 subunit of HIV-1 Env.
ELISA and SDS-PAGE/Western blot analyses to determine the binding reactivity of antibodies against various HIV-1 Envs.
Functional assays including assessment of reactivity with HIV-1-infected CD4+ T cells and antibody-dependent cellular cytotoxicity (ADCC).

Main Results:

Seven mAbs mapped to linear epitopes in gp120, with five binding the N-terminus and two the C-terminus.
Antibody 13D7 targets the gp120 N-terminus (aa 30-42), reacts with HIV-1-infected cells, and mediates ADCC.
Antibodies 13D7, 3B3, and 16H3 demonstrated 100% reactivity with tested HIV-1 Envs, indicating broad epitope coverage.

Conclusions:

The defined epitopes of these monoclonal antibodies provide valuable reagents for characterizing recombinant HIV-1 Envs.
The epitope targeted by 13D7 is present on the surface of HIV-1-infected CD4+ T cells, suggesting diagnostic or therapeutic potential.
Glycan-dependent binding was observed for antibody 18F11 at the gp120 C-terminus.