The impact of antibodies on the target's epitope conformation is a major determinant of HIV-1 neutralization and a potential contributor to disease progression. We explore here a conformation-sensitive enzymatic nanosensor for the high-throughput functional screening of human anti-HIV-1 antibodies in sera. When displaying a model epitope from a gp41 immunodominant region (Env residues from 579 to 613), the sensing signal quantitatively distinguishes between adaptive and non-adaptive antibody binding. By using this tool, we have identified IgG4 as the immunoglobulin subpopulation most efficient in the structural modification of the target epitope. © 2006 Elsevier Ltd. All rights reserved.
- Adaptive binding
- Allosteric biosensor
- Viral infection
Ferraz, R. M., Arís, A., Martínez, M. A., & Villaverde, A. (2006). High-throughput, functional screening of the anti-HIV-1 humoral response by an enzymatic nanosensor. Molecular Immunology, 43(13), 2119-2123. https://doi.org/10.1016/j.molimm.2005.12.012