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Twist Bioscience Publishes Data on VHH Single Domain Antibody Discovery Using New Methodology on Optofluidic Platform
Demonstrates Ability to Generate Humanized PSMA-Specific VHH Single Domain Antibodies via Single B Cell Screening on the Beacon Platform SOUTH SAN FRANCISCO,

About this update from Twist Bioscience Corporation
[{"type":"text","content":"\nDemonstrates Ability to Generate Humanized PSMA-Specific VHH Single Domain Antibodies via Single B Cell Screening on the Beacon Platform\n\n SOUTH SAN FRANCISCO, Calif.--(BUSINESS WIRE)--\nTwist Bioscience Corporation (NASDAQ: TWST), a company enabling customers to succeed through its offering of high-quality synthetic DNA using its silicon platform, today published on the successful discovery of alpaca-derived VHH antibodies using a disruptive, function-forward in vivo discovery workflow developed by Abveris, also known as Twist Boston, on the Beacon optofluidic platform. The paper, titled “Alpaca Single B Cell Interrogation and Heavy-Chain-Only Antibody Discovery on an Optofluidic Platform,” was published in BioRxiv.\n\n“In vivo discovery approaches for VHH antibodies have been limited by the lack of methodologies available for camelid B cell interrogation to discover heavy-chain-only antibodies. Twist Boston developed highly sophisticated assay formats for use on the Beacon optofluidic platform, which can enable the enrichment and screening of alpaca B cells in a way that provides in-depth functional data from each cell,” said Emily M. Leproust, Ph.D., CEO and co-founder of Twist Bioscience. “We are able to offer customers in vivo and library based VHH antibody discovery and optimization approaches, providing them with integrated solutions to identify VHH and other antibodies with improved characteristics, such as higher binding affinity and functional activity for difficult targets.”\n\nA VHH single domain antibody is the antigen binding domain from unique heavy-chain-only antibodies generated in camelids such as llamas and alpacas. Most antibodies contain two variable domains, the heavy and the light chains; however, camelids make antibodies containing just a heavy chain, from which the VHH single domain is derived. The small size of the VHH single domain antibodies allow them to access targets that traditional antibodies cannot, with tight binding affinities and high specificity. In addition, the lack of a paired light chain in VHH single domain antibodies simplifies downstream engineering, accelerating development timelines.\n\nIn this proof-of-concept study, custom enrichment, culture, detection, and sequencing methods were used to screen single B cells directly from immunized alpacas for target specificity and heavy-c...