ArticlePloS one2021
Staphylococcus aureus Lipase 3 (SAL3) is a surface-associated lipase that hydrolyzes short chain fatty acids.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Cultivation and molecular profiling reveal ammonia-oxidizing archaea as skin commensals.The ISME journal · 2026Article
- Gram-positive pathogens, inflammation, and the host lipid environment.Current opinion in microbiology · 2025Review
- Potential Therapeutic Targets for Combination Antibody Therapy AgainstAntibiotics (Basel, Switzerland) · 2024Review
- Untargeted and temporal analysis of retinal lipidome in bacterial endophthalmitis.Prostaglandins & other lipid mediators · 2024Review
- Article
- Bacterial contact induces polar plug disintegration to mediate whipworm egg hatching.PLoS pathogens · 2023Article
- The Small Protein ScrA Influences Staphylococcus aureus Virulence-Related Processes via the SaeRS System.Microbiology spectrum · 2023Article
- The Phospholipase A1 Activity of Glycerol Ester Hydrolase (Geh) Is Responsible for Extracellular 2-12(mSphere · 2023Article
- Bacterial contact induces polar plug disintegration to mediate whipworm egg hatching.bioRxiv : the preprint server for biology · 2023Article
- Chemical Proteomics Reveals Antibiotic Targets of Oxadiazolones in MRSA.Journal of the American Chemical Society · 2023Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial lipases play important roles during infection. The Staphylococcus aureus genome contains several genes that encode well-characterized lipases and several genes predicted to encode lipases or esterases for which the function has not yet been established. In this study, we sought to define the function of an uncharacterized S. aureus protein, and we propose the annotation S. aureus lipase 3 (SAL3) (SAUSA300_0641). We confirmed that SAL3 is a lipase and that it is surface associated and secreted through an unknown mechanism. We determined that SAL3 specifically hydrolyzes short chain (4-carbon and fewer) fatty acids and specifically binds negatively charged lipids including phosphatidic acid, phosphatidylinositol phosphate, and phosphatidylglycerol, which is the most abundant lipid in the staphylococcal cell membrane. Mutating the catalytic triad S66-A, D167-A, S168-A, and H301-A in the recombinant protein abolished lipase activity without altering binding to host lipid substrates. Taken together we report the discovery of a novel lipase from S. aureus specific to short chain fatty acids with yet to be determined roles in host pathogen interactions.
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