Toward an effective AIDS vaccine development

Sakai, Keiko; Takiguchi, Masafumi

doi:10.1002/eji.201370125

Cited by 1 publication

(1 citation statement)

References 18 publications

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“…The infected cell machinery is also responsible for heavily glycosylating Env, comprising about 50% of its total mass 11,12 . The resulting complex structure allows Env to be conformationally flexible 13,14 , while providing a metastability that is thought to allow Env to adapt and hide certain highly immunogenic epitopes that would otherwise be exposed [15][16][17][18][19] , highlighting the importance to better understand the different conformations sampled by the native Env trimer.…”

Section: Introductionmentioning

confidence: 99%

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

Veillette

Coutu

Richard

et al. 2014

JoVE

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HIV-1 envelope glycoproteins (Env) mediate viral entry into target cells and are essential to the infectious cycle. Understanding how those glycoproteins are able to fuel the fusion process through their conformational changes could lead to the design of better, more effective immunogens for vaccine strategies. Here we describe a cell-based ELISA assay that allows studying the recognition of trimeric HIV-1 Env by monoclonal antibodies. Following expression of HIV-1 trimeric Env at the surface of transfected cells, conformation specific anti-Env antibodies are incubated with the cells. A horseradish peroxidase-conjugated secondary antibody and a simple chemiluminescence reaction are then used to detect bound antibodies. This system is highly flexible and can detect Env conformational changes induced by soluble CD4 or cellular proteins. It requires minimal amount of material and no highly-specialized equipment or know-how. Thus, this technique can be established for medium to high throughput screening of antigens and antibodies, such as newly-isolated antibodies. Video LinkThe video component of this article can be found at

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