Lipoyl-E2-PDH Gets a Second Job

Seth W Dickey; Michael Otto

doi:10.1016/j.chom.2017.10.018

Lipoyl-E2-PDH Gets a Second Job

Cell Host Microbe. 2017 Nov 8;22(5):581-583. doi: 10.1016/j.chom.2017.10.018.

Authors

Seth W Dickey¹, Michael Otto²

Affiliations

¹ Pathogen Molecular Genetics Section, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, U.S. National Institutes of Health, Bethesda, MD, USA.
² Pathogen Molecular Genetics Section, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, U.S. National Institutes of Health, Bethesda, MD, USA. Electronic address: motto@niaid.nih.gov.

PMID: 29120739
DOI: 10.1016/j.chom.2017.10.018

Abstract

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.

Published by Elsevier Inc.

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MeSH terms

Acetyltransferases
Dihydrolipoamide Dehydrogenase*
Pyruvate Dehydrogenase Complex*
Staphylococcus aureus

Substances

Pyruvate Dehydrogenase Complex
Dihydrolipoamide Dehydrogenase
Acetyltransferases