The twin-arginine translocation system is vital for cell adhesion and uptake of iron in the cystic fibrosis pathogen Achromobacter xylosoxidans
(2023) In Virulence- Abstract
- Background
Achromobacter xylosoxidans is an emerging pathogen that causes airway infections in patients with cystic fibrosis. Knowledge of virulence factors and protein secretion systems in this bacterium is limited. Twin arginine translocation (Tat) is a protein secretion system that transports folded proteins across the inner cell membranes of gram-negative bacteria. Tat has been shown to be important for virulence and cellular processes in many different bacterial species. This study aimed to investigate the role of Tat in iron metabolism and host cell adhesion in A. xylosoxidans.
Methods
Putative Tat substrates in A. xylosoxidans were identified using the TatFind, TatP, and PRED-Tat prediction tools. An isogenic tatC... (More) - Background
Achromobacter xylosoxidans is an emerging pathogen that causes airway infections in patients with cystic fibrosis. Knowledge of virulence factors and protein secretion systems in this bacterium is limited. Twin arginine translocation (Tat) is a protein secretion system that transports folded proteins across the inner cell membranes of gram-negative bacteria. Tat has been shown to be important for virulence and cellular processes in many different bacterial species. This study aimed to investigate the role of Tat in iron metabolism and host cell adhesion in A. xylosoxidans.
Methods
Putative Tat substrates in A. xylosoxidans were identified using the TatFind, TatP, and PRED-Tat prediction tools. An isogenic tatC deletion mutant (ΔtatC) was generated and phenotypically characterized. The wild-type and ΔtatC A. xylosoxidans were fractionated into cytosolic, membrane, and periplasmic fractions, and the expressed proteome of the different fractions was analyzed using liquid chromatography-mass spectrometry (LC-MS/MS).
Results
A total of 128 putative Tat substrates were identified in the A. xylosoxidans proteome. The ΔtatC mutant showed attenuated host cell adhesion, growth rate, and iron acquisition. Twenty predicted Tat substrates were identified as expressed proteins in the periplasmic compartment, nine of which were associated with the wild type.
Conclusion
The data indicate that Tat secretion is important for iron acquisition and host cell adhesion in A. xylosoxidans. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1c59d4f9-5921-49cc-a044-91c4f14f7844
- author
- Khademi, S. M. Hossein LU ; Sahl, Cecilia LU ; Happonen, Lotta LU ; Forsberg, Åke and Påhlman, Lisa LU
- organization
- publishing date
- 2023-11-16
- type
- Contribution to journal
- publication status
- epub
- subject
- in
- Virulence
- publisher
- Landes Bioscience
- external identifiers
-
- pmid:37974335
- ISSN
- 2150-5594
- DOI
- 10.1080/21505594.2023.2284513
- language
- English
- LU publication?
- yes
- id
- 1c59d4f9-5921-49cc-a044-91c4f14f7844
- date added to LUP
- 2023-11-17 10:54:02
- date last changed
- 2024-02-17 03:00:51
@article{1c59d4f9-5921-49cc-a044-91c4f14f7844, abstract = {{Background<br/>Achromobacter xylosoxidans is an emerging pathogen that causes airway infections in patients with cystic fibrosis. Knowledge of virulence factors and protein secretion systems in this bacterium is limited. Twin arginine translocation (Tat) is a protein secretion system that transports folded proteins across the inner cell membranes of gram-negative bacteria. Tat has been shown to be important for virulence and cellular processes in many different bacterial species. This study aimed to investigate the role of Tat in iron metabolism and host cell adhesion in A. xylosoxidans.<br/>Methods<br/>Putative Tat substrates in A. xylosoxidans were identified using the TatFind, TatP, and PRED-Tat prediction tools. An isogenic tatC deletion mutant (ΔtatC) was generated and phenotypically characterized. The wild-type and ΔtatC A. xylosoxidans were fractionated into cytosolic, membrane, and periplasmic fractions, and the expressed proteome of the different fractions was analyzed using liquid chromatography-mass spectrometry (LC-MS/MS).<br/>Results<br/>A total of 128 putative Tat substrates were identified in the A. xylosoxidans proteome. The ΔtatC mutant showed attenuated host cell adhesion, growth rate, and iron acquisition. Twenty predicted Tat substrates were identified as expressed proteins in the periplasmic compartment, nine of which were associated with the wild type.<br/>Conclusion<br/>The data indicate that Tat secretion is important for iron acquisition and host cell adhesion in A. xylosoxidans.}}, author = {{Khademi, S. M. Hossein and Sahl, Cecilia and Happonen, Lotta and Forsberg, Åke and Påhlman, Lisa}}, issn = {{2150-5594}}, language = {{eng}}, month = {{11}}, publisher = {{Landes Bioscience}}, series = {{Virulence}}, title = {{The twin-arginine translocation system is vital for cell adhesion and uptake of iron in the cystic fibrosis pathogen Achromobacter xylosoxidans}}, url = {{http://dx.doi.org/10.1080/21505594.2023.2284513}}, doi = {{10.1080/21505594.2023.2284513}}, year = {{2023}}, }