2026-10-12T00:42:55Z https://api.figshare.com/v2/oai

oai:figshare.com:article/33803652 2026-09-15T15:41:02Z category_4 category_8 category_19 category_21 category_24 category_873 category_46 category_64 category_128 category_132 category_134 portal_63 item_type_3 month_year_09_2026

Antibody Affinity Maturation by Yeast Mating against a Diverse Antigen Library Enhances Antibody Resistance to Viral Mutations Ryan Hard (9211631) Young Su Ko (24943449) Jonathan Parkinson (7220564) Wei Wang (17594) Biochemistry Microbiology Pharmacology Biotechnology Evolutionary Biology Chemical Sciences not elsewhere classified Immunology Cancer Hematology Infectious Diseases Virology largest interaction screen single antigen yet future antigen variants 102 tested rbds antibody affinity maturation starting antigen variants unseen antibody pair improved affinity test case sars cov resistance mutations library screening large panel binding domain binding capacity Antibodies suffer from resistance mutations in their targets, which diminishes their efficacy. Most antibody library screens use a single antigen yet should ideally use many antigens to ensure that the hits have broad-binding capacity. As a test case, we used the receptor-binding domain (RBD) of SARS COV-2 and CR3022 as the starting antigen/antibody pair. We screened a CR3022 library against a large panel of RBDs (94) and isolated a hit (C8) that has improved affinity for 95/102 tested RBDs. C8 has improved affinity to variants unseen in the library screening, indicating that C8 is more resistant to future antigen variants. This study, to our knowledge, represents the largest interaction screen (10⁷) performed to date using synthetic agglutination in yeast. 2026-09-15T00:00:00Z Dataset Dataset 10.1021/acsptsci.6c00213.s002 https://figshare.com/articles/dataset/Antibody_Affinity_Maturation_by_Yeast_Mating_against_a_Diverse_Antigen_Library_Enhances_Antibody_Resistance_to_Viral_Mutations/33803652 CC BY-NC 4.0