{"entity": "publication", "iuid": "7386f457e7374f8aa65207511569e960", "timestamp": "2026-08-20T20:40:34.411Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/7386f457e7374f8aa65207511569e960.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/7386f457e7374f8aa65207511569e960"}}, "title": "Affibody-based hBCMA x CD16 dual engagers for NK cell-mediated killing of multiple myeloma cells.", "authors": [{"family": "Giang", "given": "Kim Anh", "initials": "KA"}, {"family": "Boxaspen", "given": "Thorstein", "initials": "T"}, {"family": "Diao", "given": "Yumei", "initials": "Y"}, {"family": "Nilvebrant", "given": "Johan", "initials": "J"}, {"family": "Kosugi-Kanaya", "given": "Mizuha", "initials": "M"}, {"family": "Kanaya", "given": "Minoru", "initials": "M"}, {"family": "Krokeide", "given": "Silje Zandstra", "initials": "SZ"}, {"family": "Lehmann", "given": "Fredrik", "initials": "F"}, {"family": "Svensson Gelius", "given": "Stefan", "initials": "S"}, {"family": "Malmberg", "given": "Karl-Johan", "initials": "KJ"}, {"family": "Nygren", "given": "Per-\u00c5ke", "initials": "P\u00c5"}], "type": "journal article", "published": "2023-11-25", "journal": {"title": "N Biotechnol", "issn": "1876-4347", "volume": "77", "pages": "139-148", "issn-l": "1871-6784"}, "abstract": "We describe the development and characterization of the (to date) smallest Natural Killer (NK) cell re-directing human B Cell Maturation Antigen (hBCMA) x CD16 dual engagers for potential treatment of multiple myeloma, based on combinations of small 58 amino acid, non-immunoglobulin, affibody affinity proteins. Affibody molecules to human CD16a were selected from a combinatorial library by phage display resulting in the identification of three unique binders with affinities (KD) for CD16a in the range of 100 nM-3 \u00b5M. The affibody exhibiting the highest affinity demonstrated insensitivity towards the CD16a allotype (158F/V) and did not interfere with IgG (Fc) binding to CD16a. For the construction of hBCMA x CD16 dual engagers, different CD16a binding arms, including bi-paratopic affibody combinations, were genetically fused to a high-affinity hBCMA-specific affibody. Such 15-23 kDa dual engager constructs showed simultaneous hBCMA and CD16a binding ability and could efficiently activate resting primary NK cells and trigger specific lysis of a panel of hBCMA-positive multiple myeloma cell lines. Hence, we report a novel class of uniquely small NK cell engagers with specific binding properties and potent functional profiles.", "doi": "10.1016/j.nbt.2023.09.002", "pmid": "37673373", "labels": [], "xrefs": [{"db": "pii", "key": "S1871-6784(23)00045-6"}], "notes": [], "created": "2026-08-20T08:01:55.357Z", "modified": "2026-08-20T08:01:55.371Z"}