Universität zu Köln

Zoellner, Robert, Cronenberg, Tom, Kouzel, Nadzeya, Welker, Anton, Koomey, Michael and Maier, Berenike ORCID: 0000-0001-6971-9927 (2019). Type IV Pilin Post-Translational Modifications Modulate Material Properties of Bacterial Colonies. Biophys. J., 116 (5). S. 938 - 948. CAMBRIDGE: CELL PRESS. ISSN 1542-0086

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Abstract

Bacterial type 4 pili (T4P) are extracellular polymers that initiate the formation of microcolonies and biofilms. T4P continuously elongate and retract. These pilus dynamics crucially affect the local order, shape, and fluidity of microcolonies. The major pilin subunit of the T4P bears multiple post-translational modifications. By interfering with different steps of the pilin glycosylation and phosphoform modification pathways, we investigated the effect of pilin post-translational modification on the shape and dynamics of microcolonies formed by Neisseria gonorrhoeae. Deleting the phosphotransferase responsible for phosphoetha-nolamine modification at residue serine 68 inhibits shape relaxations of microcolonies after perturbation and causes bacteria carrying the phosphoform modification to segregate to the surface of mixed colonies. We relate these mesoscopic phenotypes to increased attractive forces generated by T4P between cells. Moreover, by deleting genes responsible for the pilin glycan structure, we show that the number of saccharides attached at residue serine 63 affects the ratio between surface tension and viscosity and cause sorting between bacteria carrying different pilin glycoforms. We conclude that different pilin post-translational modifications moderately affect the attractive forces between bacteria but have severe effects on the material properties of microcolonies.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Zoellner, Robert UNSPECIFIED UNSPECIFIED UNSPECIFIED Cronenberg, Tom UNSPECIFIED UNSPECIFIED UNSPECIFIED Kouzel, Nadzeya UNSPECIFIED UNSPECIFIED UNSPECIFIED Welker, Anton UNSPECIFIED UNSPECIFIED UNSPECIFIED Koomey, Michael UNSPECIFIED UNSPECIFIED UNSPECIFIED Maier, Berenike UNSPECIFIED orcid.org/0000-0001-6971-9927 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-154216
DOI:	10.1016/j.bpj.2019.01.020
Journal or Publication Title:	Biophys. J.
Volume:	116
Number:	5
Page Range:	S. 938 - 948
Date:	2019
Publisher:	CELL PRESS
Place of Publication:	CAMBRIDGE
ISSN:	1542-0086
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Physics > Institut für Biologische Physik
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language O-LINKED GLYCOSYLATION; FUNCTIONAL ANALYSES; NEISSERIA; PROTEIN; RETRACTION; SIMULATION; ADHESION; DEFINE Multiple languages Biophysics Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/15421