High-throughput, functional screening of the anti-HIV-1 humoral response by an enzymatic nanosensor.
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.
Ferraz
Rosa María
RM
Institut de Biotecnologia i de Biomedicina and Departament de Genètica i de Microbiologia, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain.
Arís
Anna
A
Martínez
Miguel Angel
MA
Villaverde
Antonio
A
D000914:Antibodies, Viral / Q000097:blood* / Q000276:immunology; D001666:Binding Sites, Antibody / Q000276:immunology; D015374:Biosensing Techniques; D000939:Epitopes / Q000276:immunology; D005260:Female; D015700:HIV Envelope Protein gp41 / Q000276:immunology; D015658:HIV Infections / Q000097:blood* / Q000276:immunology; D015497:HIV-1 / Q000276:immunology; D006801:Humans; D007074:Immunoglobulin G / Q000097:blood* / Q000276:immunology; D008297:Male; D036103:Nanotechnology; D013329:Structure-Activity Relationship
D000914:Antibodies, Viral; D000939:Epitopes; D015700:HIV Envelope Protein gp41; D007074:Immunoglobulin G