Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/146112
Title: The novel E. coli cell division protein, YtfB, plays a role in eukaryotic cell adhesion
Authors: Bottomley, Amy L.
Peterson, Elizabeth
Iosifidis, Gregory
Yong, Adeline Mei Hui
Hartley-Tassell, Lauren E.
Ansari, Shirin
McKenzie, Chris
Burke, Catherine
Duggin, Iain G.
Kline, Kimberly A.
Harry, Elizabeth J.
Keywords: Science::Biological sciences
Issue Date: 2020
Source: Bottomley, A. L., Peterson, E., Iosifidis, G., Yong, A. M. H., Hartley-Tassell, L. E., Ansari, S., . . . Harry, E. J. (2020). The novel E. coli cell division protein, YtfB, plays a role in eukaryotic cell adhesion. Scientific Reports, 10(1), 6745-. doi:10.1038/s41598-020-63729-7
Journal: Scientific Reports 
Abstract: Characterisation of protein function based solely on homology searches may overlook functions under specific environmental conditions, or the possibility of a protein having multiple roles. In this study we investigated the role of YtfB, a protein originally identified in a genome-wide screen to cause inhibition of cell division, and has demonstrated to localise to the Escherichia coli division site with some degree of glycan specificity. Interestingly, YtfB also shows homology to the virulence factor OapA from Haemophilus influenzae, which is important for adherence to epithelial cells, indicating the potential of additional function(s) for YtfB. Here we show that E. coli YtfB binds to N’acetylglucosamine and mannobiose glycans with high affinity. The loss of ytfB results in a reduction in the ability of the uropathogenic E. coli strain UTI89 to adhere to human kidney cells, but not to bladder cells, suggesting a specific role in the initial adherence stage of ascending urinary tract infections. Taken together, our results suggest a role for YtfB in adhesion to specific eukaryotic cells, which may be additional, or complementary, to its role in cell division. This study highlights the importance of understanding the possible multiple functions of proteins based on homology, which may be specific to different environmental conditions.
URI: https://hdl.handle.net/10356/146112
ISSN: 2045-2322
DOI: 10.1038/s41598-020-63729-7
Rights: © 2020 The Author(s). 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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