Diversification of a Salmonella Virulence Protein Function by Ubiquitin-Dependent Differential Localization

Patel, Jayesh; Hueffer, Karsten; Lam, TuKiet T.; Galán, Jorge E.

doi:10.1016/j.cell.2009.01.056

Cited by 139 publications

(201 citation statements)

References 43 publications

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“…Although PI phosphatases have been reported from other bacterial pathogens, such as the PI-4-phosphatases IpgD from Shigella flexneri (14), SigD/SopB from S. typhimurium (16,17), no such enzymes have been reported from Legionella species. Our discovery of a PI phosphatase in L. pneumophila not only establishes an archetypal family of PI phosphatase, but also opens a new avenue toward the understanding of the roles of PI signaling and metabolism in L. pneumophila infection.…”

Section: Discussionmentioning

confidence: 99%

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Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase

Hsu

Zhu

Brennan

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

104

112

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Legionella pneumophila is an opportunistic intracellular pathogen that causes sporadic and epidemic cases of Legionnaires' disease. Emerging data suggest that Legionella infection involves the subversion of host phosphoinositide (PI) metabolism. However, how this bacterium actively manipulates PI lipids to benefit its infection is still an enigma. Here, we report that the L. pneumophila virulence factor SidF is a phosphatidylinositol polyphosphate 3-phosphatase that specifically hydrolyzes the D3 phosphate of PI(3,4)P 2 and PI(3,4,5)P 3 . This activity is necessary for anchoring of PI(4)Pbinding effectors to bacterial phagosomes. Crystal structures of SidF and its complex with its substrate PI(3,4)P 2 reveal striking conformational rearrangement of residues at the catalytic site to form a cationic pocket that specifically accommodates the D4 phosphate group of the substrate. Thus, our findings unveil a unique Legionella PI phosphatase essential for the establishment of lipid identity of bacterial phagosomes.phosphoinositide signaling | phagocytosis | membrane trafficking | type IV secretion system | virulence factor

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Section: Discussionmentioning

confidence: 99%

“…Salmonella typhimurium, which is responsible for most food-borne gastroenteritis (15), delivers the PI phosphatase SigD/SopB into the host. By hydrolyzing PI(3,4,5)P 3 , SopB contributes to the localized membrane ruffling that leads to bacterial internalization in nonphagocytic cells (16,17).…”

mentioning

confidence: 99%

Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase

Hsu

Zhu

Brennan

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

104

112

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“…At a later time point SopB gets ubiquitinated, which initiates its localization to Salmonella-containing vacuoles, where it establishes a replicative niche for the bacteria. 24 The cytotoxic Pseudomonas aeruginosa protein ExoS localizes to membranes in host cells via a leucine-rich domain at the N-terminus of the protein. Deletion of this domain disrupts the intracellular localization of ExoS and its ability to ADP-ribosylate Ras GTPases and its RhoGAP activity.…”

Section: Interaction Of Bacterial Factors With Cellular Compartments mentioning

confidence: 99%

Purpose of recently detected inhibitory domain of theHelicobacter pyloriprotein CagA

Steininger

Pelz²,

Vogelmann³

2011

Gut Microbes

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H elicobacter pylori infection is the most common bacterial infection worldwide and is strongly associated with gastric oncogenesis. Recently, we discovered that the H. pylori protein CagA, a risk factor for carcinogenesis, consists of two distinct membranetargeting domains. The C-terminal membrane-binding domain induces host cell responses associated with a high oncogenic potential. The N-terminal membrane-targeting domain, however, localizes to a different membrane substructure at the site of newly formed cellcell contacts thereby diminishing the effects of C-terminal signaling motifs on host cell physiology. This inhibitory function may allow H. pylori to establish a colonization niche in the host by maintaining the host epithelial architecture and thus decreasing the oncogenic potential as a side effect. From a bacterial standpoint, however, its main purpose maybe is to translocate the CagA protein via the type IV secretion apparatus into host epithelial cells.

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“…In plants, most of the localization studies of T3Es have been performed in Agrobacterium tumefaciens-mediated transient expression systems using constitutive promoters (Block and Alfano, 2011;Macho, 2016). However, several biochemical studies revealed bacterial effectors undergo posttranslocational modification for proper targeting in the host cells (Boucrot et al, 2003;Reinicke et al, 2005;Patel et al, 2009;Fernández-Álvarez et al, 2012). Therefore, Agrobacterium-mediated expressions may not reflect dynamic localization of respective effectors originally secreted by T3SS.…”

Section: Introductionmentioning

confidence: 99%

Spatiotemporal Monitoring of Pseudomonas syringae Effectors via Type III Secretion Using Split Fluorescent Protein Fragments

et al. 2017

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Pathogenic gram-negative bacteria cause serious diseases in animals and plants. These bacterial pathogens use the type III secretion system (T3SS) to deliver effector proteins into host cells; these effectors then localize to different subcellular compartments to attenuate immune responses by altering biological processes of the host cells. The fluorescent protein (FP)-based approach to monitor effectors secreted from bacteria into the host cells is not possible because the folded FP prevents effector delivery through the T3SS. Therefore, we optimized an improved variant of self-assembling split super-folder green fluorescent protein (sfGFP OPT ) system to investigate the spatiotemporal dynamics of effectors delivered through bacterial T3SS into plant cells. In this system, effectors are fused to 11th b-strand of super-folder GFP (sfGFP11), and when delivered into plant cells expressing sfGFP1-10 b-strand (sfGFP1-10 OPT ), the two proteins reconstitute GFP fluorescence. We generated a number of Arabidopsis thaliana transgenic lines expressing sfGFP1-10 OPT targeted to various subcellular compartments to facilitate localization of sfGFP11-tagged effectors delivered from bacteria. We demonstrate the efficacy of this system using Pseudomonas syringae effectors AvrB and AvrRps4 in Nicotiana benthamiana and transgenic Arabidopsis plants. The versatile split sfGFP OPT system described here will facilitate a better understanding of bacterial invasion strategies used to evade plant immune responses.

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Diversification of a Salmonella Virulence Protein Function by Ubiquitin-Dependent Differential Localization

Cited by 139 publications

References 43 publications

Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase

Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase

Purpose of recently detected inhibitory domain of theHelicobacter pyloriprotein CagA

Spatiotemporal Monitoring of Pseudomonas syringae Effectors via Type III Secretion Using Split Fluorescent Protein Fragments

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