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OmniAb Announces Publication of Scientific Paper on Heavy Chain-Only Single-Domain Antibody Chicken Platform in the Journal of Immunology
2024년 06월 05일 (수) 11:53:36 이인화 기자 chrisdon@naver.com
라인 밴드 트위터 페이스북 네이버 구글 msn

 EMERYVILLE, CALIF.--OmniAb, Inc. (NASDAQ: OABI) today announced the publication of a peer-reviewed paper titled “Chickens with a Truncated Light Chain Transgene Express Single-Domain H Chain-Only Antibodies” in the Journal of Immunology demonstrating that chickens can be genetically engineered to produce functional heavy chain-only single-domain antibodies.

sdAbs are produced naturally by camelids and have gained popularity as small, robust and highly modular building blocks for antibody discovery. While most other vertebrates use the standard heterodimeric IgG structure due to the pairing of heavy and light chains and do not produce sdAb format immunoglobulins, OmniAb’s scientific team led this study to investigate if chickens can support an immune repertoire based upon a heavy chain-only scaffold.

“Our team’s published data provided the foundational work supporting the feasibility of the Company’s next-generation transgenic chicken OmnidAb that produces fully human stabilized sdAbs. Unique physical properties of sdAbs can be leveraged for evolving fields of antibody discovery, including alternate routes of administration, diagnostic applications and therapeutic approaches that are being explored by many of our partners,” said Matt Foehr, Chief Executive Officer of OmniAb. “We currently have 80 partners leveraging OmniAb’s various platform technologies and accessing OmniAb antibodies, spanning major geographies and ranging from multinational big pharmas to venture-backed startups and leading academics.”

“Our truncated light chain chickens are designed to produce heavy (H) chain-only antibodies by deleting the light (L) chain variable region and maintaining only the constant region to serve as a chaperone for antibody secretion from the cell. We confirmed in this published study that the H chain variable region functions autonomously as a single domain without further engineering, producing sdAbs with favorable biophysical properties and antigen recognition profiles,” said Philip Leighton, Ph.D., Fellow of Molecular Biology of OmniAb. “Truncated L chain design successfully supported sdAb development and expression in chickens, and we are delighted that this work enabled the successful launch of OmnidAb.”

This article is available in the Scientific Publications section of OmniAb’s website.

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