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. 2023 Jul 11;14(1):2228657. doi: 10.1080/21505594.2023.2228657

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© 2023 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The terms on which this article has been published allow the posting of the Accepted Manuscript in a repository by the author(s) or with their consent.

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Figure 6. — Sau-41 interacts directly with RNAIII. (a) the base pairing region of Sau-41 and RNAIII was predicted with IntaRNA software. (b) Complex formations between RNAIII and Sau-41 were analysed by EMSA. Labeled Sau-41 mixed with increasing concentrations of RNAIII and RNAIII-mutant (5, 10, 25 nM and 50 nM; RNAIII-mutant: wild-type RNAIII with H1-H2 region deleted). Blank: Biotin-labelled Sau-41 without RNAIII/RNAIII-mutant addition. (c) Illustration of the speculated biological function of Sau-41. Sau-41 modulates S. aureus haemolytic activity by binding with RNAIII. (d) Competition between Sau-41 and hla^UTR binding with RNAIII was analysed by EMSA. Biotin-labelled hla^UTR interacted with RNAIII, and increasing concentrations of Sau-41 (10, 25, 50 and 125 nM) were added to interrupt the interaction. Ctrl: hla^UTR RNA (6 nM) interacting with RNAIII (6 nM) without the addition of Sau-41.