Lipoyl-E2-PDH Gets a Second Job
Pyruvate dehydrogenase (PDH) plays a well-known metabolic role inside cells. In this issue of Cell Host & Microbe, Grayczyk et al. (2017) show that the bacterial pathogen Staphylococcus aureus unexpectedly secretes and repurposes the lipoylated E2 subunit of PDH to suppress TLR-mediated activati...
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Veröffentlicht in: | Cell host & microbe 2017-11, Vol.22 (5), p.581-583 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | Pyruvate dehydrogenase (PDH) plays a well-known metabolic role inside cells. In this issue of Cell Host & Microbe, Grayczyk et al. (2017) show that the bacterial pathogen Staphylococcus aureus unexpectedly secretes and repurposes the lipoylated E2 subunit of PDH to suppress TLR-mediated activation of host macrophages by bacterial lipoproteins.
Pyruvate dehydrogenase (PDH) plays a well-known metabolic role inside cells. In this issue of Cell Host & Microbe, Grayczyk et al. (2017) show that the bacterial pathogen Staphylococcus aureus unexpectedly secretes and repurposes the lipoylated E2 subunit of PDH to suppress TLR-mediated activation of host macrophages by bacterial lipoproteins. |
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ISSN: | 1931-3128 1934-6069 |
DOI: | 10.1016/j.chom.2017.10.018 |