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Host ubiquitin protein tags lipid to fight bacteria

Host cells battle invading bacteria using a degradation process facilitated by the protein ubiquitin. The discovery of the host enzyme responsible and its bacterial target reveals that this process defies convention.
  1. Brenda A. Schulman

    1. Brenda A. Schulman is in the Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.

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  2. J. Wade Harper

    1. J. Wade Harper is in the Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.

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Intracellular bacteria such as Salmonella are a major threat to human health. These disease-causing microorganisms enter human cells cloaked in a host-derived membrane, which forms a structure termed a vacuole. To proliferate, Salmonella then need to access the cytoplasm, a feat that they typically manage through vacuole rupture. Writing in Nature, Otten et al.1 reveal the host’s front-line mode of attack against invading Salmonella — a previously unknown mechanism and machinery that marks Salmonella with the host protein ubiquitin. This tagging sets in motion events that lead to the degradation of the microbial invader.

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Nature 594, 28-29 (2021)

doi: https://doi.org/10.1038/d41586-021-01267-6

Updates & Corrections

  • Correction 21 May 2021: One of the authors (B.A.S.) has added further information to their statement on competing financial interests.

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Competing Interests

The authors are founding scientific advisory board members of Interline Therapeutics. J.W.H. is a founder and member of the scientific advisory board of Caraway Therapeutics. B.A.S. is also on the scientific advisory board of BioTheryX and is a co-inventor of intellectual property related to DCN1 small-molecule inhibitors, licensed to Cinsano.

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