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. 2022 Jul 18;12:12268. doi: 10.1038/s41598-022-16411-z

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Recognition of phage-displayed domains of HER-1 and HER-2 by monoclonal antibodies in ELISA. Purified phages were incubated on polyvinyl chloride microtiter plates coated with monoclonal antibodies. Bound phages were detected with anti-M13 antibody conjugated to horseradish peroxidase. Humanized T1 antibody (hT1) was used as unrelated coating antibody to assess specificity. Coating 9E10 mAb recognizing all c-myc tagged proteins was used as positive control. Phages displaying c-myc only were also evaluated. Recognition of phage-displayed HER-1 domain III by nimotuzumab, cetuximab and panitumumab (a). Recognition of HER-1 domain IV by D1 (scFv)₂-Fc molecule (b). Recognition of HER-2 domain IV by trastuzumab (c). Lack of recognition of HER-2 domain II by pertuzumab (d).