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. 2020 Nov 10;10:19483. doi: 10.1038/s41598-020-76557-6

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© The Author(s) 2020

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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α3 integrin levels in A549 cells after incubation with P. brasiliensis yeasts or PAM₃CSK₄. A549 cells were incubated or not (C) with P. brasiliensis yeasts (Pb) (MOI = 2.5) (a–c) or with 5 μg/mL of the TLR2-specific ligand PAM₃CSK₄ (PAM) (d,e)_. After 5 h or 24 h, epithelial cells were lysed and aliquots were submitted to SDS–PAGE. α3 integrin levels (α3 int) were analysed by Western blot. (c) α3 integrin levels from (b) in a higher exposure time in the UVITEC imaging system. Arrow corresponds to a band with lower molecular weight than α3 integrin (150 kDa). β-actin was used as loading protein control. Relative α3 integrin levels were determined by densitometric analysis. Values represent the ratio of the intensity of α3 integrin band divided by the corresponding intensity of β-actin band. Similar results were obtained from three independent experiments. Dashed lines in (a,e) represent cropped images. Uncropped images are presented in Supplementary Fig. S4.