Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.

Lipoic acid (LA) is an essential cofactor of alpha-keto acid dehydrogenase complexes (KADHs) and the glycine cleavage system. In Plasmodium, LA is attached to the KADHs by organelle-specific lipoylation pathways. Biosynthesis of LA exclusively occurs in the apicoplast, comprising octanoyl-[acyl carr...

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Autores principales:	Svenja Günther, Lynsey Wallace, Eva-Maria Patzewitz, Paul J McMillan, Janet Storm, Carsten Wrenger, Ryan Bissett, Terry K Smith, Sylke Müller
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2007
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/252a1ea7e85545459b36b533bd9436f1
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id	oai:doaj.org-article:252a1ea7e85545459b36b533bd9436f1
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spelling	oai:doaj.org-article:252a1ea7e85545459b36b533bd9436f12021-11-25T05:46:48ZApicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.1553-73661553-737410.1371/journal.ppat.0030189https://doaj.org/article/252a1ea7e85545459b36b533bd9436f12007-12-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.0030189https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Lipoic acid (LA) is an essential cofactor of alpha-keto acid dehydrogenase complexes (KADHs) and the glycine cleavage system. In Plasmodium, LA is attached to the KADHs by organelle-specific lipoylation pathways. Biosynthesis of LA exclusively occurs in the apicoplast, comprising octanoyl-[acyl carrier protein]: protein N-octanoyltransferase (LipB) and LA synthase. Salvage of LA is mitochondrial and scavenged LA is ligated to the KADHs by LA protein ligase 1 (LplA1). Both pathways are entirely independent, suggesting that both are likely to be essential for parasite survival. However, disruption of the LipB gene did not negatively affect parasite growth despite a drastic loss of LA (>90%). Surprisingly, the sole, apicoplast-located pyruvate dehydrogenase still showed lipoylation, suggesting that an alternative lipoylation pathway exists in this organelle. We provide evidence that this residual lipoylation is attributable to the dual targeted, functional lipoate protein ligase 2 (LplA2). Localisation studies show that LplA2 is present in both mitochondrion and apicoplast suggesting redundancy between the lipoic acid protein ligases in the erythrocytic stages of P. falciparum.Svenja GüntherLynsey WallaceEva-Maria PatzewitzPaul J McMillanJanet StormCarsten WrengerRyan BissettTerry K SmithSylke MüllerPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 3, Iss 12, p e189 (2007)
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 Svenja Günther Lynsey Wallace Eva-Maria Patzewitz Paul J McMillan Janet Storm Carsten Wrenger Ryan Bissett Terry K Smith Sylke Müller Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.
description	Lipoic acid (LA) is an essential cofactor of alpha-keto acid dehydrogenase complexes (KADHs) and the glycine cleavage system. In Plasmodium, LA is attached to the KADHs by organelle-specific lipoylation pathways. Biosynthesis of LA exclusively occurs in the apicoplast, comprising octanoyl-[acyl carrier protein]: protein N-octanoyltransferase (LipB) and LA synthase. Salvage of LA is mitochondrial and scavenged LA is ligated to the KADHs by LA protein ligase 1 (LplA1). Both pathways are entirely independent, suggesting that both are likely to be essential for parasite survival. However, disruption of the LipB gene did not negatively affect parasite growth despite a drastic loss of LA (>90%). Surprisingly, the sole, apicoplast-located pyruvate dehydrogenase still showed lipoylation, suggesting that an alternative lipoylation pathway exists in this organelle. We provide evidence that this residual lipoylation is attributable to the dual targeted, functional lipoate protein ligase 2 (LplA2). Localisation studies show that LplA2 is present in both mitochondrion and apicoplast suggesting redundancy between the lipoic acid protein ligases in the erythrocytic stages of P. falciparum.
format	article
author	Svenja Günther Lynsey Wallace Eva-Maria Patzewitz Paul J McMillan Janet Storm Carsten Wrenger Ryan Bissett Terry K Smith Sylke Müller
author_facet	Svenja Günther Lynsey Wallace Eva-Maria Patzewitz Paul J McMillan Janet Storm Carsten Wrenger Ryan Bissett Terry K Smith Sylke Müller
author_sort	Svenja Günther
title	Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.
title_short	Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.
title_full	Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.
title_fullStr	Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.
title_full_unstemmed	Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.
title_sort	apicoplast lipoic acid protein ligase b is not essential for plasmodium falciparum.
publisher	Public Library of Science (PLoS)
publishDate	2007
url	https://doaj.org/article/252a1ea7e85545459b36b533bd9436f1
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Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.

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