Ryan Hard, Young Su Ko, Jonathan Parkinson, Wei Wang
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引用次数: 0
Abstract
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.
期刊介绍：
ACS Pharmacology & Translational Science publishes high quality, innovative, and impactful research across the broad spectrum of biological sciences, covering basic and molecular sciences through to translational preclinical studies. Clinical studies that address novel mechanisms of action, and methodological papers that provide innovation, and advance translation, will also be considered. We give priority to studies that fully integrate basic pharmacological and/or biochemical findings into physiological processes that have translational potential in a broad range of biomedical disciplines. Therefore, studies that employ a complementary blend of in vitro and in vivo systems are of particular interest to the journal. Nonetheless, all innovative and impactful research that has an articulated translational relevance will be considered.
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