Synthetic integrin antibodies discovered by yeast display reveal αV subunit pairing preferences with β subunits.

ABSTRACT: Eight of the 24 integrin heterodimers bind to the tripeptide Arg-Gly-Asp (RGD) motif in their extracellular ligands, and play essential roles in cell adhesion, migration, and homeostasis. Despite similarity in recognizing the RGD motif and some redundancy, these integrins can selectively recognize RGD-containing ligands including fibronectin, vitronectin, fibrinogen, nephronectin and the prodomain of the transforming growth factors to fulfill specific functions in cellular processes. Subtype-specific antibodies against RGD-binding integrins are desirable for investigating their specific functions. In this study, we discovered 11 antibodies that exhibit high specificity and affinity towards integrins αVβ3, αVβ5, αVβ6, αVβ8, and α5β1 from a synthetic yeast-displayed Fab library. Of these, 6

SUBMITTER: Hao Y 

PROVIDER: S-EPMC10849667 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature