Functional conservation of the effector protein translocators PopB/YopB and PopD/YopD of <i>Pseudomonas aeruginosa</i> and <i>Yersinia pseudotuberculosis</i>

Frithz‐Lindsten, Elisabet; Holmström, Anna; Jacobsson, Lars; Soltani, Mehnam; Olsson, Jan; Rosqvist, Roland; Försberg, Åke

doi:10.1046/j.1365-2958.1998.00994.x

Cited by 94 publications

(91 citation statements)

References 45 publications

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“…No doubt these features contribute to the ability of the pcrGVHpopBD translocation operon of P. aeruginosa to restore Yop-effector translocation into cells infected with corresponding deletion mutants of Yersinia (Bröms et al, 2003a;Frithz-Lindsten et al, 1998). In this study, we were keen to address the molecular mechanisms of this common virulence strategy using a functional comparison approach.…”

Section: Discussionmentioning

confidence: 99%

“…The fact that PopD could not cooperate with Yersinia components to complement a Yersinia DyopD null mutant is an exciting observation, especially considering that coproduction with P. aeruginosa components encoded within the pcrGVHpopBD operon was sufficient for complementation (Bröms et al, 2003a;Frithz-Lindsten et al, 1998). This was not due to variable PopD secretion, since relative levels were comparable in each experimental set-up.…”

Section: Discussionmentioning

confidence: 99%

“…With this in mind, we wondered whether an earlier study showing efficient complementation of DyopB and DyopD mutants of Yersinia by the translocon operon of P. aeruginosa could be misleading (Frithz-Lindsten et al, 1998). Therefore, to directly test the functional conservation of PopB and YopB, we generated a near full-length DyopB null mutant allele in which only the first 12 and last two codons of YopB remained (pMF463) (Bröms et al, 2003a) in wild-type Yersinia creating YPIII/pIB615 (see Fig.…”

Section: Popb Of P Aeruginosa and Yopb Of Y Pseudotuberculosis Are mentioning

confidence: 99%

“…However, while PcrV alone can functionally complement a Yersinia DlcrV null mutant for regulation (Bröms et al, 2003a;Pettersson et al, 1999), efficient effector translocation clearly requires co-production of additional P. aeruginosa translocon components (Bröms et al, 2003a). In light of this finding, the fact that PopB and PopD could complement reciprocal defects in YopB and YopD of Yersinia when the entire P. aeruginosa translocase operon was used in the complementation study (Frithz-Lindsten et al, 1998) could be misleading. Efforts to complement using individual genes were hitherto not performed.…”

Section: Introductionmentioning

confidence: 99%

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Dissection of homologous translocon operons reveals a distinct role for YopD in type III secretion by Yersinia pseudotuberculosis

et al. 2003

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The homologous pcrGVHpopBD and lcrGVHyopBD translocase operons of Pseudomonas aeruginosa and pathogenic Yersinia spp., respectively, are responsible for the translocation of anti-host effectors into the cytosol of infected eukaryotic cells. In Yersinia, this operon is also required for yop-regulatory control. To probe for key molecular interactions during the infection process, the functional interchangeability of popB/yopB and popD/yopD was investigated. Secretion of PopB produced in trans in a DyopB null mutant of Yersinia was only observed when co-produced with its native chaperone PcrH, but this was sufficient to complement the yopB translocation defect. The Yersinia DyopD null mutant synthesized and secreted PopD even in the absence of native PcrH, yet this did not restore YopD-dependent yop-regulatory control or effector translocation. Thus, this suggests that key residues in YopD, which are not conserved in PopD, are essential for functional Yersinia type III secretion. INTRODUCTIONAll pathogenic Yersinia spp. encode a wide assortment of virulence determinants to establish a host infection (Revell & Miller, 2001). Significantly, a common plasmid-borne type III secretion system (TTSS) is essential for the fitness of Yersinia inside the host . This specialized virulence strategy links protein secretion across the bacterial envelope with translocation of anti-host virulence effectors through the plasma membrane of target eukaryotic cells. Effector proteins localized inside the target cell disable crucial signal transduction pathways, rendering the cell incapable of mounting an effective immune defence (Bliska, 2000; Fällman et al., 2002).The bacterial envelope component of the TTSSs of many plant-and animal-interacting bacteria resembles the flagella basal body, while a hollow needle-like protrusion extends from the bacterial surface through which effectors are believed to traverse (Blocker et al., 1999;Hoiczyk & Blobel, 2001;Jin & He, 2001;Kubori et al., 1998; Sekiya et al., 2001;Tamano et al., 2000). Furthermore, translocation into target cells by Yersinia requires the structural proteins LcrV, YopB and YopD. These proteins interact (Neyt & Cornelis, 1999b;Sarker et al., 1998) to presumably form a complex that facilitates pore formation in target cell membranes to allow entry of effector proteins into target cells (Bröms et al., 2003a; Holmström et al., 2001;Neyt & Cornelis, 1999a;Tardy et al., 1999). At odds with this dogma is a report suggesting that the needle component YscF is the sole requirement for effector translocation (Hoiczyk & Blobel, 2001). Clearly, the molecular mechanisms of this process are still unresolved. Interestingly, both LcrV and YopD also contribute to the control of type III substrate synthesis and secretion. Yop synthesis in LcrV-defective strains is significantly down-regulated (Bergman et al., 1991;Price et al., 1991;Skrzypek & Straley, 1995). On the other hand, Yersinia defective for YopD constitutively produce Yop proteins and LcrV (Francis & Wolf-Watz, 1998;Williams & Strale...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Popb Of P Aeruginosa and Yopb Of Y Pseudotuberculosis Are mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Dissection of homologous translocon operons reveals a distinct role for YopD in type III secretion by Yersinia pseudotuberculosis

et al. 2003

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“…YopH localizes to the focal adhesion complexes and is essential for anti-phagocytosis and virulence (25). YopE localizes to cytoplasmic granules and the perinuclear region (26,27). However, how type III toxins traffic in intoxicated cells has not been established.…”

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confidence: 99%

Intracellular Localization of Type III-delivered Pseudomonas ExoS with Endosome Vesicles

Zhang

Deng

Barbieri

2007

Journal of Biological Chemistry

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ExoS (453 amino acids) is a bi-functional type III cytotoxin produced by Pseudomonas aeruginosa. Residues 96 -219 include the Rho GTPase-activating protein (RhoGAP) domain, and residues 234 -453 include the 14-3-3-dependent ADPribosyltransferase domain. Earlier studies also identified an N-terminal domain (termed the membrane localization domain) that comprises residues 51-77 and includes a novel leucine-rich motif that targets ExoS to the perinuclear region of cultured cells. There is limited information on how ExoS or other type III cytotoxins enter and target intracellular host proteins. Type III-delivered ExoS localized to both plasma membrane and perinuclear region, whereas ExoS(⌬MLD) was localized to the cytosol. Plasma membrane localization of ExoS was transient and had a half-life of ϳ20 min. Type III-delivered ExoS co-immunoprecipitated 14-3-3 proteins and Rab9, Rab6, and Rab5. Immunofluorescence experiments showed that ExoS colocalized with Rab9, Rab6, and Rab5. Fluorescent energy transfer was detected between ExoS and 14-3-3 proteins but not between ExoS and Rabs proteins. Together, these results indicate that type III-delivered ExoS localizes on the host endosomes and utilizes multiple pathways to traffic from the plasma membrane to the perinuclear region of intoxicated host cells.

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Type IV pili are not specifically required for contact dependent translocation of exoenzymes by Pseudomonas aeruginosa

Sundin

Wolfgang

Lory

et al. 2002

Microbial Pathogenesis

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Functional conservation of the effector protein translocators PopB/YopB and PopD/YopD of Pseudomonas aeruginosa and Yersinia pseudotuberculosis

Cited by 94 publications

References 45 publications

Dissection of homologous translocon operons reveals a distinct role for YopD in type III secretion by Yersinia pseudotuberculosis

Dissection of homologous translocon operons reveals a distinct role for YopD in type III secretion by Yersinia pseudotuberculosis

Intracellular Localization of Type III-delivered Pseudomonas ExoS with Endosome Vesicles

Type IV pili are not specifically required for contact dependent translocation of exoenzymes by Pseudomonas aeruginosa

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