On January 15, 2018 Biotecnol and University of Naples reported a study on Journal of Immunology, Volume 42 Issue 1: pg 1-10,where it was shown that T-cell recruiting bispecific antibody derivatives (TRBA) offer a more effective alternative to standard antibody therapy (Press release, Biotecnol, JAN 15, 2018, View Source [SID1234570281]). The team evaluated a panel of TRBAs targeting 3 different epitopes on the HER2 receptor either in a bivalent targeting tribody structure or as a monovalent scFv-fusion (BiTE format) for binding, cytotoxicity on Trastuzumab-resistant cell lines, and induction of cardiotoxicity. All three TRBAs did bind with high affinity to the HER2 extracellular domain and a large panel of HER2-positive tumour cells. Tribodies had an increased in vitro cytotoxic potency as compared to BiTEs. It was noted that Tribodies targeting the epitopes on ErbB2 receptor domains I and II bind and activate lysis of mammary and gastric tumour cells more efficiently than a Tribody targeting the Trastuzumab epitope on domain IV. The first 2 are also active on Trastuzumab-resistant cancer cells lacking or masking the epitope recognized by Trastuzumab. None of the Tribodies studied showed significant toxicity on human cardiomyocytes. Altogether these results make these novel anti-HER2 bispecific Tribodies candidates for therapeutic development for treating HER2-positive Trastuzumab-resistant cancer patients.

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