The novel E. coli cell division protein, YtfB, plays a role in eukaryotic cell adhesion.

Bottomley, AL; Peterson, E; Iosifidis, G; Yong, AMH; Hartley-Tassell, LE; Ansari, S; McKenzie, C; Burke, C; Duggin, IG; Kline, KA; Harry, EJ

The novel E. coli cell division protein, YtfB, plays a role in eukaryotic cell adhesion.

Bottomley, AL Peterson, E Iosifidis, G Yong, AMH Hartley-Tassell, LE Ansari, S McKenzie, C Burke, C

Duggin, IG Kline, KA Harry, EJ

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Publisher:: Springer Science and Business Media LLC
Publication Type:: Journal Article
Citation:: Scientific reports, 2020, 10, (1), pp. 6745
Issue Date:: 2020-04-21

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Field	Value	Language
dc.contributor.author	Bottomley, AL
dc.contributor.author	Peterson, E
dc.contributor.author	Iosifidis, G
dc.contributor.author	Yong, AMH
dc.contributor.author	Hartley-Tassell, LE
dc.contributor.author	Ansari, S
dc.contributor.author	McKenzie, C
dc.contributor.author	Burke, C https://orcid.org/0000-0002-8917-0019
dc.contributor.author	Duggin, IG
dc.contributor.author	Kline, KA
dc.contributor.author	Harry, EJ
dc.date.accessioned	2020-08-13T05:18:02Z
dc.date.available	2020-04-01
dc.date.available	2020-08-13T05:18:02Z
dc.date.issued	2020-04-21
dc.identifier.citation	Scientific reports, 2020, 10, (1), pp. 6745
dc.identifier.issn	2045-2322
dc.identifier.issn	2045-2322
dc.identifier.uri	http://hdl.handle.net/10453/142092
dc.description.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.
dc.format	Electronic
dc.language	eng
dc.publisher	Springer Science and Business Media LLC
dc.relation.ispartof	Scientific reports
dc.relation.isbasedon	10.1038/s41598-020-63729-7
dc.rights	info:eu-repo/semantics/openAccess
dc.rights	This is a post-peer-review, pre-copyedit version of an article published in Scientific reports. The final authenticated version is available online at: https://dx.doi.org/10.1038/s41598-020-63729-7.	en_US
dc.title	The novel E. coli cell division protein, YtfB, plays a role in eukaryotic cell adhesion.
dc.type	Journal Article
utslib.citation.volume	10
utslib.location.activity	England
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	open_access	*
dc.date.updated	2020-08-13T05:17:51Z
pubs.issue	1
pubs.publication-status	Published
pubs.volume	10
utslib.citation.issue	1

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.

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http://hdl.handle.net/10453/142092