{"entity": "publication", "iuid": "26af6db331c94816a7e2f5292e77637a", "timestamp": "2026-08-20T20:42:30.426Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/26af6db331c94816a7e2f5292e77637a.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/26af6db331c94816a7e2f5292e77637a"}}, "title": "An anti-CEA affibody showing high-definition staining in human pancreatic cancer tissue sections and selective tumor targeting in vivo.", "authors": [{"family": "Nilvebrant", "given": "Johan", "initials": "J"}, {"family": "Moro", "given": "Carlos Fern\u00e1ndez", "initials": "CF"}, {"family": "Papalanis", "given": "Eleftherios", "initials": "E"}, {"family": "Novin", "given": "Masih Ostad", "initials": "MO"}, {"family": "Ding", "given": "Haozhong", "initials": "H"}, {"family": "Li", "given": "Ruonan", "initials": "R"}, {"family": "Oroujeni", "given": "Maryam", "initials": "M"}, {"family": "Selvam", "given": "Arun", "initials": "A"}, {"family": "Boz\u00f3ky", "given": "B\u00e9la", "initials": "B"}, {"family": "Gr\u00e4slund", "given": "Torbj\u00f6rn", "initials": "T"}, {"family": "Szekerczes", "given": "Timea", "initials": "T"}, {"family": "Sandalova", "given": "Tatiana", "initials": "T"}, {"family": "Salter", "given": "Hugh", "initials": "H"}, {"family": "Achour", "given": "Adnane", "initials": "A"}, {"family": "Tolmachev", "given": "Vladimir", "initials": "V"}, {"family": "Bj\u00f6rnstedt", "given": "Mikael", "initials": "M"}, {"family": "Nygren", "given": "Per-\u00c5ke", "initials": "P\u00c5"}], "type": "journal article", "published": "2025-11-00", "journal": {"title": "Transl Oncol", "issn": "1936-5233", "volume": "61", "pages": "102512", "issn-l": null}, "abstract": "We report development and characterization of small non-immunoglobulin affibody affinity proteins directed to the highly glycosylated human carcinoembryonic antigen-related adhesion molecule 5 (CEACAM5, CEA), and their use in immunohistochemical (IHC) analyses of human pancreatic cancer samples and for in vivo tumor imaging. A total of nineteen unique anti-CEA affibodies were identified from large phage display libraries constructed using combinatorial protein engineering of a small 58 amino acid three-helix bundle protein domain. Molecular modeling suggested that all enriched clones share a binding surface with several clustered tryptophan residues interacting with a hydrophobic patch in the N1 domain of CEA centered around a phenylalanine residue. One variant, designated as C9, exhibited the highest affinity in biosensor analyses and was reformatted into a 15 kDa homodimer expressed in Escherichia coli. The biotinylated form, C9-C9-Bio, was evaluated for its IHC performance on matched frozen and formalin-fixed, paraffin-embedded (FFPE) sections of human pancreatic cancer samples (n = 7). Compared to clinical-grade monoclonal antibodies II-7 and CEA31, as well as a polyclonal reagent, C9-C9-Bio demonstrated highly sensitive CEA detection with minimal background staining. Statistical analyses including intraclass correlation and Bland-Altman assessments revealed excellent agreement between C9-C9-Bio and the two monoclonal antibodies in FFPE tissue samples. Further, a 99mTc[Tc]-labeled C9-C9 construct showed CEA-dependent binding to human cancer cell lines in vitro, and selectively bound to CEA-expressing BxPC3 xenografts in mice when investigated as a tracer for in vivo imaging, allowing for a visualization of tumors after four hours. In summary, these findings highlight the potential use of the easily produced CEA-binding C9 affibody for various clinical applications, including IHC and medical imaging, and as a targeting moiety for directing various therapeutic modalities to CEA-expressing tumors.", "doi": "10.1016/j.tranon.2025.102512", "pmid": "40882560", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC12410180"}, {"db": "pii", "key": "S1936-5233(25)00243-8"}], "notes": [], "created": "2026-08-20T08:06:08.293Z", "modified": "2026-08-20T08:06:08.310Z"}