Pseudomonas aeruginosa AlgF is a protein-protein interaction mediator required for acetylation of the alginate exopolysaccharide.

Autor:	Low KE; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada., Gheorghita AA; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada., Tammam SD; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada., Whitfield GB; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada., Li YE; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada., Riley LM; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada., Weadge JT; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada., Caldwell SJ; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada., Chong PA; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada., Walvoort MTC; Leiden Institute of Chemistry, Leiden University, Leiden, The Netherlands., Kitova EN; Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada., Klassen JS; Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada., Codée JDC; Leiden Institute of Chemistry, Leiden University, Leiden, The Netherlands., Howell PL; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada. Electronic address: howell@sickkids.ca.
Jazyk:	angličtina
Zdroj:	The Journal of biological chemistry [J Biol Chem] 2023 Nov; Vol. 299 (11), pp. 105314. Date of Electronic Publication: 2023 Oct 04.
DOI:	10.1016/j.jbc.2023.105314
Abstrakt:	Enzymatic modifications of bacterial exopolysaccharides enhance immune evasion and persistence during infection. In the Gram-negative opportunistic pathogen Pseudomonas aeruginosa, acetylation of alginate reduces opsonic killing by phagocytes and improves reactive oxygen species scavenging. Although it is well known that alginate acetylation in P. aeruginosa requires AlgI, AlgJ, AlgF, and AlgX, how these proteins coordinate polymer modification at a molecular level remains unclear. Here, we describe the structural characterization of AlgF and its protein interaction network. We characterize direct interactions between AlgF and both AlgJ and AlgX in vitro and demonstrate an association between AlgF and AlgX, as well as AlgJ and AlgI, in P. aeruginosa. We determine that AlgF does not exhibit acetylesterase activity and is unable to bind to polymannuronate in vitro. Therefore, we propose that AlgF functions to mediate protein-protein interactions between alginate acetylation enzymes, forming the periplasmic AlgJFXK (AlgJ-AlgF-AlgX-AlgK) acetylation and export complex required for robust biofilm formation. Competing Interests: Conflict of interest P. L. H. is the recipient of a Tier I Canada Research Chair. The other authors declare that they have no conflicts of interest with the contents of this article. (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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