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. 2023 May 30;13:8773. doi: 10.1038/s41598-023-35511-y

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© The Author(s) 2023

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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Antibodies produced against two A. algerae protein bands soluble in high concentration of 2-mercaptoethanol specifically labelled the extruded polar tube. (a) SDS-PAGE (10%) of sporal protein extracts obtained first in a buffer containing 100 mM DTT. Then, the insoluble fraction was incubated in a 50% 2-mercaptoethanol (2-ME) solution. Two protein bands running at 75 and 180 kDa (arrows) were selected in the 2-ME extract to produce mouse antibodies and were analysed in mass spectrometry (see Table S2). (b,c) IFA with mouse antisera raised against 180-kDa (b) and 75-kDa (c) protein bands. Both antisera labelled the entire polar tube of germinated A. algerae spores but the signal was less intensive at the end of the tube with the anti-180 kDa antiserum (arrow). Mouse antisera were used at a 1:100 dilution. Secondary antibody was Alexa 488-conjugated goat anti-mouse IgG. Merged pictures were generated with GIMP 2.10.8 software. PT polar tube; S spore; Scale bar: 10 µm.