Staphylococcus aureus Lipase 3 (SAL3) is a surface-associated lipase that hydrolyzes short chain fatty acids.
Staphylococcus aureus Lipase 3 (SAL3) is a surface-associated lipase that hydrolyzes short chain fatty acids.
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DOI：
10.1371/journal.pone.0258106
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发表时间：
2021
期刊：
影响因子：
3.7
通讯作者：
Jefferson KK
中科院分区：
文献类型：
--
作者：
Kumar NG;Contaifer D Jr;Wijesinghe DS;Jefferson KK
细菌脂肪酶在感染过程中起重要作用。金黄色葡萄球菌基因组包含编码充分表征的脂肪酶的几个基因和预测编码功能尚未确定的脂肪酶或酯酶的几个基因。在这项研究中，我们试图定义一个未表征的S的功能。aureus蛋白，我们提出了注释S.金黄色葡萄球菌脂肪酶3（SAL 3）（SAUSA300_0641）。我们证实了SAL 3是一种脂肪酶，它是表面相关的，并通过一种未知的机制分泌。我们确定，SAL 3特异性水解短链（4-碳和更少）脂肪酸，并特异性结合带负电荷的脂质，包括磷脂酸，磷脂酰肌醇磷酸和磷脂酰甘油，这是葡萄球菌细胞膜中最丰富的脂质。突变重组蛋白中的催化三联体S66-A、D167-A、S168-A和H301-A消除了脂肪酶活性，而不改变与宿主脂质底物的结合。总之，我们报告的发现，一种新的脂肪酶从S。金黄色葡萄球菌对短链脂肪酸具有特异性，在宿主病原体相互作用中的作用尚未确定。
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.