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Pseudomonas aeruginosa AlgF is a protein-protein interaction mediator required for acetylation of the alginate exopolysaccharide
Open accessPreprint — published as 10.1016/j.jbc.2023.105314 · Paper page
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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Highly accurate protein structure prediction with AlphaFold
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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
- openRxiv
- Published
- 2023-07-25
- Volume
- 299
- Issue
- 11
- Pages
- 105314-105314
- ISSN
- 0021-9258 (ISSN-L)
- 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
- gold
- doi.org
- Licence
- cc-by
- 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) (submittedVersion, cc-by)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, cc-by)
- Funders
- Government of Canada
- Cystic Fibrosis Canada
- Canada Foundation for Innovation
- Hospital for Sick Children
- Canadian Institutes of Health Research (FDN154327, 13337, 154327, 153322_1)
- Natural Sciences and Engineering Research Council of Canada
- Canadian Glycomics Network
- Brookhaven National Laboratory
- 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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