Proteomic Analysis of <i>Staphylococcus aureus</i> Treated with ShangKeHuangShui

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  • Liu Lichu
    Institute of Orthopedics and Traumatology, Foshan Hospital of Traditional Chinese Medicine
  • Zhao Na
    Institute of Orthopedics and Traumatology, Foshan Hospital of Traditional Chinese Medicine
  • Yang Kuangyang
    Institute of Orthopedics and Traumatology, Foshan Hospital of Traditional Chinese Medicine
  • Liao Honghong
    Institute of Orthopedics and Traumatology, Foshan Hospital of Traditional Chinese Medicine
  • Liu Xiaofang
    Institute of Orthopedics and Traumatology, Foshan Hospital of Traditional Chinese Medicine
  • Wu Ying
    Laboratory Medicine Center, Foshan Hospital of Traditional Chinese Medicine
  • Wang Yan
    Center for Translational Medicine Research and Development, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences
  • Peng Xiao
    Institute of Orthopedics and Traumatology, Foshan Hospital of Traditional Chinese Medicine
  • Wu Yuanyan
    Institute of Orthopedics and Traumatology, Foshan Hospital of Traditional Chinese Medicine

Abstract

<p>Staphylococcus aureus (SAU) stands as the prevailing pathogen in post-traumatic infections, with the emergence of antibiotic resistance presenting formidable treatment hurdles. The pressing need is to explore novel antibiotics to address this challenge. ShangKeHuangShui (SKHS), a patented traditional Chinese herbal formula, has gained widespread use in averting post-traumatic infections, but its biological effects remain incomplete understanding. This study’s primary objective was to delve into the antibacterial properties, potential antibacterial compounds within SKHS, and their associated molecular targets. In vitro SKHS antibacterial assays demonstrated that the minimum inhibitory concentration (MIC) was 8.625 mg/mL and the minimum bactericide concentration (MBC) was 17.25 mg/mL. Proteomic analysis based on tandem mass tag (TMT) showed significant changes in the expression level of 246 proteins in SKHS treated group compared to control group, with 79 proteins upregulated and 167 proteins downregulated (>1.5-fold, p < 0.05). Subsequently, thirteen target proteins related to various biological processes and multiple metabolic pathways were selected to conduct parallel reaction monitoring (PRM) and molecular docking screen. In protein tyrosine phosphatase PtpA (ptpA) docking screening, phellodendrine and obacunone can bind to ptpA with the binding energy of − 8.4 and − 8.3 kcal/mol, respectively. This suggests their potential impact on antibacterial activity by modulating the two-component system of SAU. The discovery lays a groundwork for future research endeavors for exploring new antibacterial candidates and elucidating specific active chemical components within SKHS that match target proteins. Further investigations are imperative to unveil the biological effects of these monomers and their potential synergistic actions.</p>

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