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Updated: Jul 11, 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

Neutralizing antibodies decrease the envelope fluidity of HIV-1.

Shinji Harada¹, Kazuaki Monde, Yuetsu Tanaka

¹Department of Medical Virology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto 860-8556, Japan. biodef@gpo.kumamoto-u.ac.jp

|September 29, 2007

Summary

Increasing temperature enhances human immunodeficiency virus type 1 (HIV-1) infectivity by promoting viral envelope fluidity. This enhanced infectivity can be neutralized by specific antibodies that suppress viral envelope fluidity.

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Area of Science:

Virology
Immunology
Biophysics

Background:

Human immunodeficiency virus type 1 (HIV-1) entry requires fusion pore formation, facilitated by plasma membrane and viral envelope fluidization.
Viral fusion involves interactions between viral envelope glycoproteins, such as gp41 and gp120, and host cell receptors like CXCR4.

Purpose of the Study:

To investigate the role of viral envelope fluidity in HIV-1 infectivity and neutralization.
To determine if temperature affects HIV-1 infectivity through modulation of membrane fluidity.

Main Methods:

Viral adsorption at 25°C followed by incubation at 40°C to assess temperature-dependent infectivity.
Neutralization assays using various antibodies (anti-CXCR4, anti-V3, anti-HLA-II, anti-HTLV-I gp46) and non-neutralizing antibodies.
Measurement of viral envelope fluidity using biophysical techniques.

Main Results:

A 1.4-fold increase in HIV-1 infectivity was observed when temperature was raised from 25°C to 40°C after viral adsorption.
Enhanced infectivity was inhibited by post-attachment neutralizing antibodies (T140, anti-V3 antibodies), but not by non-neutralizing antibodies.
Anti-V3 and anti-HLA-II antibodies suppressed viral envelope fluidity, correlating with their neutralizing activity.
Non-neutralizing antibodies did not affect viral envelope fluidity.

Conclusions:

Viral envelope fluidity is a critical factor in HIV-1 infectivity and represents a key target for neutralization.
Antibody-mediated suppression of viral envelope fluidity is a significant mechanism of HIV-1 neutralization, complementing the inhibition of viral attachment.