Legionella and Coxiella effectors: strength in diversity and activity

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Abstract

The intracellular pathogens Legionella pneumophila and Coxiella burnetii use the Dot/Icm type IV secretion system to translocate effectors into host cells. Qiu and Luo explore the biochemical and cell biological functions of these effectors and their roles in our understanding of bacterial virulence.

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Most cited references 89

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The Legionella effector RavZ inhibits host autophagy through irreversible Atg8 deconjugation.

Augustine Choy, Julia Dancourt, Brian Mugo … (2012)

Eukaryotic cells can use the autophagy pathway to defend against microbes that gain access to the cytosol or reside in pathogen-modified vacuoles. It remains unclear if pathogens have evolved specific mechanisms to manipulate autophagy. Here, we found that the intracellular pathogen Legionella pneumophila could interfere with autophagy by using the bacterial effector protein RavZ to directly uncouple Atg8 proteins attached to phosphatidylethanolamine on autophagosome membranes. RavZ hydrolyzed the amide bond between the carboxyl-terminal glycine residue and an adjacent aromatic residue in Atg8 proteins, producing an Atg8 protein that could not be reconjugated by Atg7 and Atg3. Thus, intracellular pathogens can inhibit autophagy by irreversibly inactivating Atg8 proteins during infection.

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Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors.

Xiaoxiao Pan, Anja Lührmann, Ayano Satoh … (2008)

Specialized secretion systems are used by many bacteria to deliver effector proteins into host cells that can either mimic or disrupt the function of eukaryotic factors. We found that the intracellular pathogens Legionella pneumophila and Coxiella burnetii use a type IV secretion system to deliver into eukaryotic cells a large number of different bacterial proteins containing ankyrin repeat homology domains called Anks. The L. pneumophila AnkX protein prevented microtubule-dependent vesicular transport to interfere with fusion of the L. pneumophila-containing vacuole with late endosomes after infection of macrophages, which demonstrates that Ank proteins have effector functions important for bacterial infection of eukaryotic host cells.

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Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites.

Jonathan C Kagan, Craig Roy (2002)

It is unknown how Legionella pneumophila cells escape the degradative lysosomal pathway after phagocytosis by macrophages and replicate in an organelle derived from the endoplasmic reticulum. Here we show that, after internalization, L. pneumophila-containing phagosomes recruit early secretory vesicles. Once L. pneumophila phagosomes have intercepted early secretory vesicles they begin to acquire proteins residing in transitional and rough endoplasmic reticulum. The functions of Sar1 and ADP-ribosylation factor-1 are important for biogenesis of the L. pneumophila replicative organelle. These data indicate that L. pneumophila intercepts vesicular traffic from endoplasmic-reticulum exit sites to create an organelle that permits intracellular replication and prevents destruction by the host cell.

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Author and article information

Journal

Title: Nature Reviews Microbiology

Abbreviated Title: Nat Rev Micro

Publisher: Springer Nature

ISSN (Print): 1740-1526

ISSN (Electronic): 1740-1534

Publication date Created: July 17 2017

Publication date (Print): July 17 2017

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Article

DOI: 10.1038/nrmicro.2017.67

PubMed ID: 28713154

SO-VID: 89a54e0d-dc52-4305-a861-7e6fb4daf4dc

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