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. 2022 Jan 21;53:5. doi: 10.1186/s13567-022-01023-2

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© The Author(s) 2022

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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PhoE-specific antibody responses in mice detected by Western blotting and iELISA. A Recognition of PhoE by mouse sera in a Western blot. Lane M: Pre-Stained Protein maker, lane 1 is the sample of purified PhoE protein; line 2 is the negative control of E. coli lysate containing the empty pET28a vector. For Western blot analysis, the primary antibody was the mouse serum isolated from the mice immunized with PhoE, the secondary antibody was an HRP-conjugated goat anti-mouse IgG. B Serum was tested for the presence of IgG antibodies by iELISA using PhoE as coating antigen. The absorbance of the developed HRP reaction was measured at 450 nm. Bars represent arithmetic means ± SD of antibody titers. **p < 0.01.