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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 mutated variants of phage-displayed domain III of HER-1 and domain IV of HER-2 by monoclonal antibodies. Purified phages displaying either wild-type (wt) or mutated HER domains were incubated on polyvinyl chloride microtiter plates coated with monoclonal antibodies. Bound phages were detected with an anti-M13 antibody conjugated to horseradish peroxidase. Relative reactivity (%) of each variant against a given antibody was calculated taking recognition of the wt non-mutated domain by the same antibody as the reference value (100%). Recognition of mutated variants of HER-1 domain III (a). Recognition of mutated variants of HER-2 domain IV (b).