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Published, Version of Record (VoR)Open Access via Drexel Libraries Read and Publish Program 2025CC BY V4.0, Open
Journal article
Vibrio cholerae can Recycle Fatty Acids Via an Acyl-Acyl Carrier Protein Synthetase
Current microbiology, v 82(8), 352
30 Jun 2025
PMID: 40586929
Featured in Collection : Research Supported by Drexel Libraries' OA Programs
Abstract
Fatty acids are crucial building blocks for membranes, co-factors, and secondary metabolites, and they are produced by the fatty acid synthase (FAS). Several antibiotics target the bacterial FAS but some bacteria can circumvent FAS inhibition by import and utilization of exogenous fatty acids. The acyl-acyl carrier protein synthetase (AasS) facilitates the direct utilization of fatty acids without the need for breakdown through β-oxidation. Using a combination of unnatural fatty acid supplementation and mass spectrometry we identify here an AasS of Vibrio cholerae. In vitro characterization shows that the enzyme can load diverse fatty acids on the FAS acyl carrier protein as well as on coenzyme A. We show that three different FAS-targeted antibiotics can arrest growth of wild type V. cholerae and that fatty acid supplementation can rescue this inhibition. In an AasS deletion strain, supplementation with cerulenin and fatty acids allows for growth showcasing the redundancy of environmental fatty acid utilization in V. cholerae.
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Details
- Title
- Vibrio cholerae can Recycle Fatty Acids Via an Acyl-Acyl Carrier Protein Synthetase
- Creators
- Amanda J. Platt - Drexel UniversityAmy T Ma - Drexel University, Microbiology and ImmunologyJoris Beld (Corresponding Author) - Drexel University, Microbiology and Immunology
- Publication Details
- Current microbiology, v 82(8), 352
- Publisher
- Springer Nature
- Number of pages
- 11
- Grant note
- Center for Advanced Microbial Processing (CAMP)Institute for Molecular Medicine & Infectious Disease (IMMID)Pennsylvania Commonwealth (CURE grant)
This research was supported by the Center for Advanced Microbial Processing (CAMP), the Institute for Molecular Medicine & Infectious Disease (IMMID), and the Pennsylvania Commonwealth (CURE grant).
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:001520172300004
- Scopus ID
- 2-s2.0-105009549739
- Other Identifier
- 991022058833904721
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- Web of Science research areas
- Microbiology