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• W3015659713 abstract "Abstract Background To defend the lungs, mucus adheres to bacterial cells and facilitates their removal by ciliary transport. Our goals were to measure the affinity of mucus for the respiratory pathogen Staphylococcus aureus and identify bacterial genes that regulate this interaction. Methods S. aureus was added to pig tracheas to determine whether it binds mucus or epithelial cells. To quantify its affinity for mucus, we developed a competition assay in microtiter plates. Mucin was added over a dose range as an inhibitor of bacterial attachment. We then examined how transcriptional regulator MgrA and cell wall transpeptidase sortase (SrtA) affect bacterial interaction with mucin. Results In pig tracheas, S. aureus bound mucus strands from submucosal glands more than epithelial cells. In microtiter plate assays, Δ srtA failed to attach even in the absence of mucin. Mucin blocked wild type S. aureus attachment in a dose-dependent manner. Higher concentrations were needed to inhibit binding of Δ mgrA . Co-deletion of ebh and sraP , which encode surface proteins repressed by MgrA, suppressed the Δ mgrA binding phenotype. No differences between Δ mgrA and wild type were observed when methylcellulose or heparin sulfate were substituted for mucin, indicating specificity. Conclusions Mucin decreases attachment of S. aureus to plastic, consistent with its physiologic role in host defense. S. aureus deficient in MgrA has decreased affinity for mucin. Ebh and SraP, which are normally repressed by MgrA, may function as inhibitors of attachment to mucin. These data show that specific bacterial factors may regulate the interaction of S. aureus with mucus." @default.
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• W3015659713 date "2020-04-10" @default.
• W3015659713 modified "2023-10-16" @default.
• W3015659713 title "MgrA regulates interaction of Staphylococcus aureus with mucin" @default.
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• W3015659713 doi "https://doi.org/10.1101/2020.04.09.035261" @default.
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