A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies
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DOI：
10.1002/pmic.201500091
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发表时间：
2015-11-01
期刊：
影响因子：
3.4
通讯作者：
Schmidt, Frank
中科院分区：
文献类型：
--
作者：
Depke, Maren;Michalik, Stephan;Schmidt, Frank
金黄色葡萄球菌是一种机会性的人类病原体，可导致危及生命的疾病。对细菌的蛋白质组分析可以为其病理生理学和代谢适应的重要方面提供新的见解，从而有助于识别干预的目标。然而，这种蛋白质组研究的价值随着其综合性的增加而增加。我们提出了一种MS驱动的，全蛋白质组的金黄色葡萄球菌HG001菌株的特征。结合144个高精度蛋白质组数据，我们从2088个不同的金黄色葡萄球菌HG001蛋白中鉴定出19 109个多肽，占预测ORF的72%。进一步从等电点、肉汁和可检测性分数等方面对多肽进行了表征，以了解8.7%的低多肽覆盖率(在220 245个理论多肽中有19 109个)。在高度复杂的宿主-病原体相互作用实验中，高质量的以多肽为中心的光谱被组织到一个全面的多肽片段文库(SpectraST)中，用于鉴定金黄色葡萄球菌类型的多肽，与吉祥物搜索相比，这显著提高了鉴定的金黄色葡萄球菌蛋白的数量。这项工作现在可以通过全面的蛋白质组分析来阐明金黄色葡萄球菌特异性宿主-病原体相互作用研究中的关键病理生理学问题。这里开发的金黄色葡萄球菌特有的光谱资源也是SRM或独立于数据采集MS方法的重要谱库。所有MS数据都已存放在ProteomeXchange中，标识符为PXD000702(http://proteomecentral.proteomexchange.org/dataset/PXD000702).
Staphylococcus aureus is an opportunistic human pathogen, which can cause life-threatening disease. Proteome analyses of the bacterium can provide new insights into its pathophysiology and important facets of metabolic adaptation and, thus, aid the recognition of targets for intervention. However, the value of such proteome studies increases with their comprehensiveness. We present an MS-driven, proteome-wide characterization of the strain S. aureus HG001. Combining 144 high precision proteomic data sets, we identified 19 109 peptides from 2088 distinct S. aureus HG001 proteins, which account for 72% of the predicted ORFs. Peptides were further characterized concerning pI, GRAVY, and detectability scores in order to understand the low peptide coverage of 8.7% (19 109 out of 220 245 theoretical peptides). The high quality peptide-centric spectra have been organized into a comprehensive peptide fragmentation library (SpectraST) and used for identification of S. aureus-typic peptides in highly complex host-pathogen interaction experiments, which significantly improved the number of identified S. aureus proteins compared to a MASCOT search. This effort now allows the elucidation of crucial pathophysiological questions in S. aureus-specific host-pathogen interaction studies through comprehensive proteome analysis. The S. aureus-specific spectra resource developed here also represents an important spectral repository for SRM or for data-independent acquisition MS approaches. All MS data have been deposited in the ProteomeXchange with identifier PXD000702 (http://proteomecentral.proteomexchange.org/dataset/PXD000702).