Structure of the AlgKX modification and secretion complex required for alginate production and biofilm attachment in Pseudomonas aeruginosa

Andreea A. Gheorghita, Yancheng E. Li, Elena N. Kitova, Duong T. Bui, Roland Pfoh, Kristin E. Low, Gregory B. Whitfield, Marthe T. C. Walvoort, Qingju Zhang, Jeroen D. C. Codée, John S. Klassen and P. Lynne Howell ()
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Andreea A. Gheorghita: The Hospital for Sick Children
Yancheng E. Li: The Hospital for Sick Children
Elena N. Kitova: University of Alberta
Duong T. Bui: University of Alberta
Roland Pfoh: The Hospital for Sick Children
Kristin E. Low: The Hospital for Sick Children
Gregory B. Whitfield: The Hospital for Sick Children
Marthe T. C. Walvoort: Leiden University
Qingju Zhang: Leiden University
Jeroen D. C. Codée: Leiden University
John S. Klassen: University of Alberta
P. Lynne Howell: The Hospital for Sick Children

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract Synthase-dependent secretion systems are a conserved mechanism for producing exopolysaccharides in Gram-negative bacteria. Although widely studied, it is not well understood how these systems are organized to coordinate polymer biosynthesis, modification, and export across both membranes and the peptidoglycan. To investigate how synthase-dependent secretion systems produce polymer at a molecular level, we determined the crystal structure of the AlgK-AlgX (AlgKX) complex involved in Pseudomonas aeruginosa alginate exopolysaccharide acetylation and export. We demonstrate that AlgKX directly binds alginate oligosaccharides and that formation of the complex is vital for polymer production and biofilm attachment. Finally, we propose a structural model for the AlgEKX outer membrane modification and secretion complex. Together, our study provides insight into how alginate biosynthesis proteins coordinate production of a key exopolysaccharide involved in establishing persistent Pseudomonas lung infections.

Date: 2022
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DOI: 10.1038/s41467-022-35131-6

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