<scp>d</scp>
            -
            <i>myo</i>
            -Inositol 1,4,5,6-tetrakisphosphate produced in human intestinal epithelial cells in response to
            <i>Salmonella</i>
            invasion inhibits phosphoinositide 3-kinase signaling pathways

Eckmann, Lars; Rudolf, Marco T.; Ptasznik, Andrzej; Schultz, Carsten; Jiang, Tao; Wolfson, Nora; Tsien, Roger Y.; Fierer, Joshua; Shears, Stephen B.; Kagnoff, Martin F.; Traynor‐Kaplan, Alexis

doi:10.1073/pnas.94.26.14456

Cited by 96 publications

(97 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Our previous studies have shown that SopB is an inositol phosphate phosphatase (14), and the recombinant protein assayed in vitro hydrolyzes a wide range of inositol phosphates and phospholipids (not including InsP 6 ). However, when a virulent strain of S. dublin is added to HeLa cells, it appears that Ins-1,3,4,5,6-P 5 is the major, if not only, phosphatase substrate with cellular levels of Ins-1,4,5,6-P 4 rising 14-fold in 30 min (14,15). Thus, other bacterial proteins besides SopB may be affecting intracellular inositol metabolites.…”

Section: Resultsmentioning

confidence: 99%

“…In contrast, when S. dublin was added to HeLa cells there was a rapid (1 h) increase in the levels of inositol 1,4,5,6-tetrakisphosphate (Ins-1,4,5,6-P 4 ) without significant changes in other inositol phosphates or phospholipids (14,15). This finding was significant because Ins-1,4,5,6-P 4 has been shown to antagonize the phosphatidylinositol 3,4,5-trisphosphate-mediated closing of cellular chloride channels (15). Thus, we speculated that SopB may enhance chloride and water secretion, thereby inducing diarrhea during infection.…”

mentioning

confidence: 98%

“…When SopB was expressed in E. coli and assayed in vitro, it hydrolyzed a variety of inositol phosphates and phospholipids, although it did not hydrolyze InsP 6 in vitro (14). In contrast, when S. dublin was added to HeLa cells there was a rapid (1 h) increase in the levels of inositol 1,4,5,6-tetrakisphosphate (Ins-1,4,5,6-P 4 ) without significant changes in other inositol phosphates or phospholipids (14,15). This finding was significant because Ins-1,4,5,6-P 4 has been shown to antagonize the phosphatidylinositol 3,4,5-trisphosphate-mediated closing of cellular chloride channels (15).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export

Feng¹

2001

Proceedings of the National Academy of Sciences

View full text Add to dashboard Cite

SopB is an inositol phosphate phosphatase that is a virulence factor in Salmonella species. We have overexpressed SopB cDNA in a tetracycline-dependent system in human embryonic 293 cells, and used this model system to directly analyze the role of SopB in altering inositol metabolite levels in vivo. Addition of tetracycline to these cells resulted in the rapid induction of SopB expression, which was coincident with perturbations in the cellular levels of multiple soluble inositol phosphates. All of the changes induced by SopB expression were reversed within 24 h on removal of tetracycline from media. Specifically, cellular inositol 1,3,4,5,6-pentakisphosphate (InsP 5) and inositol hexakisphosphate (InsP6) levels were depleted within 4 to 6 h after inducing SopB expression. A transient rise in cellular inositol 1,4,5,6-tetrakisphosphate was also observed and was accompanied by increased chloride channel activity. This indicates that SopB alone is sufficient for changes in chloride channel function in cells infected with Salmonella organisms. Depletion of inositol phosphates, including InsP 5 and InsP6 metabolites, was coincident with the accumulation of polyadenylated RNA in the nucleus. This suggested that a defect in nuclear export had occurred. Moreover, the penetrance of the export defect required localization of SopB to the nucleus. These results provide evidence that inositol phosphate productions may be required for efficient mRNA export in mammalian cells.

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 98%

mentioning

confidence: 99%

See 1 more Smart Citation

Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export

Feng¹

2001

Proceedings of the National Academy of Sciences

View full text Add to dashboard Cite

show abstract

“…The yeast homolog of IMPK -the kinase Arg82 -has been shown to be involved in transcriptional regulation suggesting a functional role of Ins(1,3,4,5,6)P 4 in regulation of gene expression. Furthermore, Ins(1,3,4,5,6)P 4 is elevated during Salmonella enterica infection [65]. In 2012, Watson et al [66] published the crystal structure of histone deacetylase 3 (HDAC3) in complex with the transcriptional co-repressor silencing mediator of retinoid and thyroid hormone receptors (SMRT).…”

Section: Inositol Tetraphosphatementioning

confidence: 99%

Stabilization of protein–protein interactions by small molecules

Giordanetto¹,

Schäfer

Ottmann

2014

Drug Discovery Today

View full text Add to dashboard Cite

“…In fact, in addition to being preferred sites of infection in the natural hosts by the respective Salmonella host-restricted serotypes [215,216] (S. Uzzau and colleagues, unpublished results), they all represent primary lymphoid organs for the B-cell repertoire of that particular animal species. It is tempting to speculate, therefore, that a convergence exists between the evolution of S. enterica subspecies I strains able to colonize internal organs of warm blood animals, and the acquisition by these hosts of primary lymphoid tissues for B-cell maturation that are more sophisticated than those of the S. bongori and S. enterica subspecies II, IIIa, IIIb, IV, VI, and VII natural hosts, i.e.…”

Section: Extraintestinal Infection : Interaction With the Reticulo-enmentioning

confidence: 99%

Host adapted serotypes of Salmonella enterica

et al. 2000

View full text Add to dashboard Cite

Salmonella constitutes a genus of zoonotic bacteria of worldwide economic and health importance. The current view of salmonella taxonomy assigns the members of this genus to two species: S. enterica and S. bongori. S. enterica itself is divided into six subspecies, enterica, salamae, arizonae, diarizonae, indica, and houtenae, also known as subspecies I, II, IIIa, IIIb, IV, and VI, respectively [1]. Members of Salmonella enterica subspecies enterica are mainly associated with warm-blooded vertebrates and are usually transmitted by ingestion of food or water contaminated by infected faeces. The pathogenicity of most of the distinct serotypes remains undefined, and even within the most common serotypes, many questions remain to be answered regarding the interactions between the organism and the infected host.Salmonellosis manifests itself in three major forms: enteritis, septicaemia, and abortion, each of which may be present singly or in combination, depending on both the serotype and the host involved. Although currently over 2300 serovars of Salmonella are recognized, only about 50 serotypes are isolated in any significant numbers as human or animal pathogens [2, 3] and they all belong to subspecies enterica. Of these, most cause acute gastroenteritis characterized by a short incubation period and a severe systemic disease in man or animals, characterized by septicaemia, fever and/or abortion, and such serotypes are often associated with one or few host species [4–6].It is the intention of this review to present a summary of current knowledge of these host-adapted serotypes of S. enterica. The taxonomic relationships between the serotypes will be discussed together with a comparison of the pathology and pathogenesis of the disease that they cause in their natural host(s). Since much of our knowledge on salmonellosis is based on the results of work on Typhimurium, this serotype will often be used as the baseline in discussion. It is hoped that an appreciation of the differences that exist in the way these serotypes interact with the host will lead to a greater understanding of the complex host–parasite relationship that characterizes salmonella infections.

show abstract

d - myo -Inositol 1,4,5,6-tetrakisphosphate produced in human intestinal epithelial cells in response to Salmonella invasion inhibits phosphoinositide 3-kinase signaling pathways

Abstract: ABSTRACT

Cited by 96 publications

References 30 publications

Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export

Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export

Stabilization of protein–protein interactions by small molecules

Host adapted serotypes of Salmonella enterica

Contact Info

Product

Resources

About