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Cited by 11Bacterial biofilms and quorum sensingPolysaccharides Composition and ApplicationsBacterial Genetics and Biotechnology

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

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Low, Kristin E., Gheorghita, Andreea A., Tammam, Stephanie D., Whitfield, Gregory B., Li, Yancheng E., Riley, Laura M., Weadge, Joel T., Caldwell, Shane J., Chong, P. Andrew, Walvoort, Marthe T.C., Kitova, Elena N., Klassen, John S., Codée, Jeroen D.C., Howell, P. Lynne·2023·Journal of Biological Chemistry
DOI 10.1016/j.jbc.2023.105314PMC PMC10641220

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Abstract

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.

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Metadata

Authors
Low, K. E., Gheorghita, A. A., Tammam, S. D., Whitfield, G. B., Li, Y. E., Riley, L. M., Weadge, J. T., Caldwell, S. J., Chong, P. A., Walvoort, M. T. C., Kitova, E. N., Klassen, J. S., Codée, J. D. C., & Howell, P. L.
Affiliations
  • Hospital for Sick Children (CA)
  • University of Toronto (CA)
  • Leiden University (NL)
  • University of Alberta (CA)
Corresponding author
Howell, P. Lynne
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2023-11
Volume
299
Issue
11
Pages
105314
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/j.jbc.2023.105314
PMC
PMC10641220
OpenAlex
W4387341449
Cited by
11
References
1
Citations by year
2026: 3 · 2025: 4 · 2024: 3 · 2023: 1
FWCI
0.98
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Leiden Repository (Leiden University) (publishedVersion, cc-by)
  • Leiden Repository (Leiden University) (submittedVersion, cc-by)
  • University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, cc-by)
Funders
  • Canada Foundation for Innovation
  • The Hospital for Sick Children
  • GlycoNet
  • Government of Canada
  • Canadian Institutes of Health Research (FDN-154327, PJT-153322)
  • Cystic Fibrosis Canada
  • Natural Sciences and Engineering Research Council of Canada
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
Pseudomonas aeruginosa, protein-protein interaction, biofilm formation, immune evasion, reactive oxygen species scavenging
MeSH terms
Acetylation, Alginates, Bacterial Proteins, Protein Processing, Post-Translational, Pseudomonas aeruginosa, Biofilms, Periplasm

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