Host proteasomal degradation generates amino acids essential for intracellular bacterial growth

Christopher T.D. Price, Tasneem Al-Quadan, Marina Santic, Ilan Rosenshine, Yousef Abu Kwaik*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

160 Scopus citations

Abstract

Legionella pneumophila proliferates in environmental amoeba and human cells within the Legionella-containing vacuole (LCV). The exported AnkB F-box effector of L. pneumophila is anchored into the LCV membrane by host-mediated farnesylation. Here, we report that host proteasomal degradation of Lys 48-linked polyubiquitinated proteins, assembled on the LCV by AnkB, generates amino acids required for intracellular bacterial proliferation. The severe defect of the ankB null mutant in proliferation within amoeba and human cells is rescued by supplementation of a mixture of amino acids or cysteine, serine, pyruvate, or citrate, similar to rescue by genetic complementation. Defect of the ankB mutant in intrapulmonary proliferation in mice is rescued upon injection of a mixture of amino acids or cysteine. Therefore, Legionella promotes eukaryotic proteasomal degradation to generate amino acids needed as carbon and energy sources for bacterial proliferation within evolutionarily distant hosts.

Original languageAmerican English
Pages (from-to)1553-1557
Number of pages5
JournalScience
Volume334
Issue number6062
DOIs
StatePublished - 16 Dec 2011

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