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Updated: Apr 17, 2026
Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Published on: September 14, 2014
Prospects for engineering HIV-specific antibodies for enhanced effector function and half-life
Austin W Boesch1, Galit Alter, Margaret E Ackerman
1aThayer School of Engineering, Dartmouth College, Hanover, New Hampshire bRagon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology, and Harvard University, Cambridge, Massachusetts cDepartment of Microbiology and Immunology, Geisel School of Medicine, Lebanon, New Hampshire, USA.
Antibody Fc receptor engagement is crucial for controlling HIV-1 infection and viremia. Tailoring antibody Fc domains can optimize passive immunotherapy for HIV prevention and eradication.
Area of Science:
- Immunology
- Virology
- Therapeutics
Background:
- Recent animal model data highlights the need to understand how antibodies achieve anti-HIV-1 effects in vivo.
- Passive immunotherapy with antibodies offers promising strategies for HIV treatment and prevention.
Purpose of the Study:
- To review the role of antibody effector functions, particularly Fc receptor (FcR) engagement, in controlling HIV-1 infection.
- To explore how Fc domain modification can optimize antibody-based HIV therapies.
Main Methods:
- Review of evidence from natural infection, vaccination, and animal models.
- Analysis of clinical data from recombinant antibody therapeutics.
- Exploration of engineered antibody variants with differential FcR binding.
Main Results:
- Antibody FcR engagement plays a critical role in reducing HIV-1 infection risk, postinfection viremia, and viral rebound.
- Fc-driven activity is essential for recombinant antibody therapeutics in various disease settings.
- Engineered Fc variants are being studied to understand individual and combined antibody effector functions.
Conclusions:
- Understanding protective antibody activities in vivo is key to developing effective HIV prevention and eradication strategies.
- Tailoring antibody activity through Fc domain modification can optimize therapeutic outcomes for HIV.
