Substrate-mediated regulation of the arginine transporter of Toxoplasma gondii.

Intracellular parasites, such as the apicomplexan Toxoplasma gondii, are adept at scavenging nutrients from their host. However, there is little understanding of how parasites sense and respond to the changing nutrient environments they encounter during an infection. TgApiAT1, a member of the apicom...

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Autores principales:	Esther Rajendran, Morgan Clark, Cibelly Goulart, Birte Steinhöfel, Erick T Tjhin, Simon Gross, Nicholas C Smith, Kiaran Kirk, Giel G van Dooren
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/e6aa59b199ac4fd4be72d45596137ba1
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spelling	oai:doaj.org-article:e6aa59b199ac4fd4be72d45596137ba12021-12-02T20:00:25ZSubstrate-mediated regulation of the arginine transporter of Toxoplasma gondii.1553-73661553-737410.1371/journal.ppat.1009816https://doaj.org/article/e6aa59b199ac4fd4be72d45596137ba12021-08-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.1009816https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Intracellular parasites, such as the apicomplexan Toxoplasma gondii, are adept at scavenging nutrients from their host. However, there is little understanding of how parasites sense and respond to the changing nutrient environments they encounter during an infection. TgApiAT1, a member of the apicomplexan ApiAT family of amino acid transporters, is the major uptake route for the essential amino acid L-arginine (Arg) in T. gondii. Here, we show that the abundance of TgApiAT1, and hence the rate of uptake of Arg, is regulated by the availability of Arg in the parasite's external environment, increasing in response to decreased [Arg]. Using a luciferase-based 'biosensor' strain of T. gondii, we demonstrate that the expression of TgApiAT1 varies between different organs within the host, indicating that parasites are able to modulate TgApiAT1-dependent uptake of Arg as they encounter different nutrient environments in vivo. Finally, we show that Arg-dependent regulation of TgApiAT1 expression is post-transcriptional, mediated by an upstream open reading frame (uORF) in the TgApiAT1 transcript, and we provide evidence that the peptide encoded by this uORF is critical for mediating regulation. Together, our data reveal the mechanism by which an apicomplexan parasite responds to changes in the availability of a key nutrient.Esther RajendranMorgan ClarkCibelly GoulartBirte SteinhöfelErick T TjhinSimon GrossNicholas C SmithKiaran KirkGiel G van DoorenPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 17, Iss 8, p e1009816 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Esther Rajendran Morgan Clark Cibelly Goulart Birte Steinhöfel Erick T Tjhin Simon Gross Nicholas C Smith Kiaran Kirk Giel G van Dooren Substrate-mediated regulation of the arginine transporter of Toxoplasma gondii.
description	Intracellular parasites, such as the apicomplexan Toxoplasma gondii, are adept at scavenging nutrients from their host. However, there is little understanding of how parasites sense and respond to the changing nutrient environments they encounter during an infection. TgApiAT1, a member of the apicomplexan ApiAT family of amino acid transporters, is the major uptake route for the essential amino acid L-arginine (Arg) in T. gondii. Here, we show that the abundance of TgApiAT1, and hence the rate of uptake of Arg, is regulated by the availability of Arg in the parasite's external environment, increasing in response to decreased [Arg]. Using a luciferase-based 'biosensor' strain of T. gondii, we demonstrate that the expression of TgApiAT1 varies between different organs within the host, indicating that parasites are able to modulate TgApiAT1-dependent uptake of Arg as they encounter different nutrient environments in vivo. Finally, we show that Arg-dependent regulation of TgApiAT1 expression is post-transcriptional, mediated by an upstream open reading frame (uORF) in the TgApiAT1 transcript, and we provide evidence that the peptide encoded by this uORF is critical for mediating regulation. Together, our data reveal the mechanism by which an apicomplexan parasite responds to changes in the availability of a key nutrient.
format	article
author	Esther Rajendran Morgan Clark Cibelly Goulart Birte Steinhöfel Erick T Tjhin Simon Gross Nicholas C Smith Kiaran Kirk Giel G van Dooren
author_facet	Esther Rajendran Morgan Clark Cibelly Goulart Birte Steinhöfel Erick T Tjhin Simon Gross Nicholas C Smith Kiaran Kirk Giel G van Dooren
author_sort	Esther Rajendran
title	Substrate-mediated regulation of the arginine transporter of Toxoplasma gondii.
title_short	Substrate-mediated regulation of the arginine transporter of Toxoplasma gondii.
title_full	Substrate-mediated regulation of the arginine transporter of Toxoplasma gondii.
title_fullStr	Substrate-mediated regulation of the arginine transporter of Toxoplasma gondii.
title_full_unstemmed	Substrate-mediated regulation of the arginine transporter of Toxoplasma gondii.
title_sort	substrate-mediated regulation of the arginine transporter of toxoplasma gondii.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/e6aa59b199ac4fd4be72d45596137ba1
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_version_	1718375754363830272

Substrate-mediated regulation of the arginine transporter of Toxoplasma gondii.

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