Zymeworks Showcases Preclinical Assets, Including New Therapeutic Platform, ProTECT, and Zanidatamab Mechanisms of Action at AACR Annual Meeting

Zymeworks Inc. (NYSE: ZYME), a clinical-stage biopharmaceutical company developing multifunctional biotherapeutics, today announced five presentations at the American Association for Cancer Research (AACR) Annual Meeting. The presentations highlight preclinical data that reveal new insights into the unique mechanisms of action of lead clinical candidate, zanidatamab, introduce Zymeworks’ fourth therapeutic platform, ProTECT, and describe two new preclinical assets focused on the cytokine, IL-12, and the immune-oncology target, 4-1BB.

This press release features multimedia. View the full release here: https://www.businesswire.com/news/home/20210410005031/en/

(Photo: Business Wire)

Presentations are now available to registrants of the AACR Annual Meeting and will also be archived on the Zymeworks website.

Zanidatamab Presentations

Super-resolution imaging studies of zanidatamab: providing insights into its bispecific mode of action

Abstract: 1032
Session Category: Experimental and Molecular Therapeutics
Session Title: Cellular Responses to Anticancer Drugs

The bispecific antibody zanidatamab’s (ZW25’s) unique mechanisms of action and durable anti-tumor activity in HER2-expressing cancers

Abstract: 1005
Session Category: Experimental and Molecular Therapeutics
Session Title: Cellular Responses to Anticancer Drugs

Zanidatamab, Zymeworks’ lead clinical candidate, is currently enrolling in a pivotal trial for refractory HER2-amplified biliary tract cancer (HERIZON-BTC-01) as well as several Phase 2 trials for HER2-expressing gastroesophageal and breast cancers. Zanidatamab is a bispecific antibody that simultaneously binds two distinct sites on HER2 resulting in multiple mechanisms of action. Research presented today at AACR continues to demonstrate that zanidatamab induces the formation of HER2 receptor clusters and receptor internalization resulting in their downregulation, inhibits growth factor-dependent and -independent tumor cell proliferation, and potently activates the immune system via antibody-dependent cellular cytotoxicity (ADCC) and antibody-dependent cellular phagocytosis (ADCP). New findings from this research have revealed that zanidatamab can form complexes with HER2 with distinct higher order geometry on the cell surface. The potential for zanidatamab-induced HER2 localization may promote C1q engagement and is consistent with the additional finding that zanidatamab has the unique ability to promote complement dependent cytotoxicity (CDC). This was not observed with either of the HER2-targeted monospecific antibodies, trastuzumab and pertuzumab, or their combination and may contribute to zanidatamab’s promising clinical activity.