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Sequestration of host metabolism by an intracellular pathogen.

Gehre L, Gorgette O, Perrinet S, Prevost MC, Ducatez M, Giebel AM, Nelson DE, Ball SG, Subtil A - Elife (2016)

Bottom Line: We provide evidence that bacterial glycogen metabolism enzymes are secreted into the vacuole lumen through type 3 secretion.Our data bring strong support to the following scenario: bacteria co-opt the host transporter SLC35D2 to import UDP-glucose into the vacuole, where it serves as substrate for de novo glycogen synthesis, through a remarkable adaptation of the bacterial glycogen synthase.Based on these findings we propose that parasitophorous vacuoles not only offer protection but also provide a microorganism-controlled metabolically active compartment essential for redirecting host resources to the pathogens.

View Article: PubMed Central - PubMed

Affiliation: Unité de Biologie cellulaire de l'infection microbienne, Institut Pasteur, Paris, France.

ABSTRACT
For intracellular pathogens, residence in a vacuole provides a shelter against cytosolic host defense to the cost of limited access to nutrients. The human pathogen Chlamydia trachomatis grows in a glycogen-rich vacuole. How this large polymer accumulates there is unknown. We reveal that host glycogen stores shift to the vacuole through two pathways: bulk uptake from the cytoplasmic pool, and de novo synthesis. We provide evidence that bacterial glycogen metabolism enzymes are secreted into the vacuole lumen through type 3 secretion. Our data bring strong support to the following scenario: bacteria co-opt the host transporter SLC35D2 to import UDP-glucose into the vacuole, where it serves as substrate for de novo glycogen synthesis, through a remarkable adaptation of the bacterial glycogen synthase. Based on these findings we propose that parasitophorous vacuoles not only offer protection but also provide a microorganism-controlled metabolically active compartment essential for redirecting host resources to the pathogens.

No MeSH data available.


Related in: MedlinePlus

GlgX accumulates at the inclusion membrane.HeLa cells were infected for 24 hr with LGV, fixed with 3% PFA and stained with the anti-GlgX antibody (green), an antibody against the inclusion protein CT813 (red) and Hoechst (blue). Insets to the right show enlargements of the boxed areas. Scale bar: 10 µm.DOI:http://dx.doi.org/10.7554/eLife.12552.013
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fig3s3: GlgX accumulates at the inclusion membrane.HeLa cells were infected for 24 hr with LGV, fixed with 3% PFA and stained with the anti-GlgX antibody (green), an antibody against the inclusion protein CT813 (red) and Hoechst (blue). Insets to the right show enlargements of the boxed areas. Scale bar: 10 µm.DOI:http://dx.doi.org/10.7554/eLife.12552.013


Sequestration of host metabolism by an intracellular pathogen.

Gehre L, Gorgette O, Perrinet S, Prevost MC, Ducatez M, Giebel AM, Nelson DE, Ball SG, Subtil A - Elife (2016)

GlgX accumulates at the inclusion membrane.HeLa cells were infected for 24 hr with LGV, fixed with 3% PFA and stained with the anti-GlgX antibody (green), an antibody against the inclusion protein CT813 (red) and Hoechst (blue). Insets to the right show enlargements of the boxed areas. Scale bar: 10 µm.DOI:http://dx.doi.org/10.7554/eLife.12552.013
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4829429&req=5

fig3s3: GlgX accumulates at the inclusion membrane.HeLa cells were infected for 24 hr with LGV, fixed with 3% PFA and stained with the anti-GlgX antibody (green), an antibody against the inclusion protein CT813 (red) and Hoechst (blue). Insets to the right show enlargements of the boxed areas. Scale bar: 10 µm.DOI:http://dx.doi.org/10.7554/eLife.12552.013
Bottom Line: We provide evidence that bacterial glycogen metabolism enzymes are secreted into the vacuole lumen through type 3 secretion.Our data bring strong support to the following scenario: bacteria co-opt the host transporter SLC35D2 to import UDP-glucose into the vacuole, where it serves as substrate for de novo glycogen synthesis, through a remarkable adaptation of the bacterial glycogen synthase.Based on these findings we propose that parasitophorous vacuoles not only offer protection but also provide a microorganism-controlled metabolically active compartment essential for redirecting host resources to the pathogens.

View Article: PubMed Central - PubMed

Affiliation: Unité de Biologie cellulaire de l'infection microbienne, Institut Pasteur, Paris, France.

ABSTRACT
For intracellular pathogens, residence in a vacuole provides a shelter against cytosolic host defense to the cost of limited access to nutrients. The human pathogen Chlamydia trachomatis grows in a glycogen-rich vacuole. How this large polymer accumulates there is unknown. We reveal that host glycogen stores shift to the vacuole through two pathways: bulk uptake from the cytoplasmic pool, and de novo synthesis. We provide evidence that bacterial glycogen metabolism enzymes are secreted into the vacuole lumen through type 3 secretion. Our data bring strong support to the following scenario: bacteria co-opt the host transporter SLC35D2 to import UDP-glucose into the vacuole, where it serves as substrate for de novo glycogen synthesis, through a remarkable adaptation of the bacterial glycogen synthase. Based on these findings we propose that parasitophorous vacuoles not only offer protection but also provide a microorganism-controlled metabolically active compartment essential for redirecting host resources to the pathogens.

No MeSH data available.


Related in: MedlinePlus