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单羧酸转运蛋白参与类质体中的代谢，与寄生虫的存活有关。

The monocarboxylate transporters are involved in the metabolism within the apicoplast and are linked to parasite survival.

机构信息

National Key Laboratory of Veterinary Public Health Safety, and College of Veterinary Medicine, China Agricultural University, Beijing, China.

National Animal Protozoa Laboratory and School of Veterinary Medicine, China Agricultural University, Beijing, China.

出版信息

Elife. 2024 Mar 19;12:RP88866. doi: 10.7554/eLife.88866.

DOI:10.7554/eLife.88866
PMID:38502570
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10950331/
Abstract

The apicoplast is a four-membrane plastid found in the apicomplexans, which harbors biosynthesis and organelle housekeeping activities in the matrix. However, the mechanism driving the flux of metabolites, in and out, remains unknown. Here, we used TurboID and genome engineering to identify apicoplast transporters in . Among the many novel transporters, we show that one pair of apicomplexan monocarboxylate transporters (AMTs) appears to have evolved from a putative host cell that engulfed a red alga. Protein depletion showed that AMT1 and AMT2 are critical for parasite growth. Metabolite analyses supported the notion that AMT1 and AMT2 are associated with biosynthesis of isoprenoids and fatty acids. However, stronger phenotypic defects were observed for AMT2, including in the inability to establish parasite virulence in mice. This study clarifies, significantly, the mystery of apicoplast transporter composition and reveals the importance of the pair of AMTs in maintaining the apicoplast activity in apicomplexans.

摘要

类质体是一种在顶复门生物中发现的四膜质质体，它在基质中承载生物合成和细胞器维护活动。然而，驱动代谢物进出的机制仍然未知。在这里，我们使用 TurboID 和基因组工程来鉴定. 中的类质体转运蛋白。在许多新的转运蛋白中，我们表明一对顶复门单羧酸转运蛋白（AMT）似乎是从吞噬了红藻的宿主细胞进化而来的。蛋白耗竭表明 AMT1 和 AMT2 对寄生虫的生长至关重要。代谢物分析支持了 AMT1 和 AMT2 与类异戊二烯和脂肪酸生物合成相关的观点。然而，对 AMT2 观察到更强的表型缺陷，包括在无法在小鼠中建立寄生虫毒力。这项研究显著阐明了类质体转运蛋白组成的奥秘，并揭示了这对 AMT 在维持顶复门生物类质体活性方面的重要性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/c9fe186959d9/elife-88866-fig6-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/766314bfb400/elife-88866-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/502bd01be99f/elife-88866-fig1-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/86c20576706f/elife-88866-fig1-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/a45989267e24/elife-88866-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/ee73c13fec06/elife-88866-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/cded1692a0e6/elife-88866-fig3-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/8df4976daf1d/elife-88866-fig3-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/cee17fdfe7be/elife-88866-fig3-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/19021a75518e/elife-88866-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/7d017e5372b3/elife-88866-fig4-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/4273550f537d/elife-88866-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/a62dd59ae9c2/elife-88866-fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/c9fe186959d9/elife-88866-fig6-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/766314bfb400/elife-88866-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/502bd01be99f/elife-88866-fig1-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/86c20576706f/elife-88866-fig1-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/a45989267e24/elife-88866-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/ee73c13fec06/elife-88866-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/cded1692a0e6/elife-88866-fig3-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/8df4976daf1d/elife-88866-fig3-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/cee17fdfe7be/elife-88866-fig3-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/19021a75518e/elife-88866-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/7d017e5372b3/elife-88866-fig4-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/4273550f537d/elife-88866-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/a62dd59ae9c2/elife-88866-fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93d9/10950331/c9fe186959d9/elife-88866-fig6-figsupp1.jpg

相似文献

[1]
The monocarboxylate transporters are involved in the metabolism within the apicoplast and are linked to parasite survival.

Elife. 2024-3-19

[2]
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[3]
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[8]
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[9]
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[10]
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引用本文的文献

[1]
A Major Facilitator Superfamily Transporter Is Critical for the Metabolism and Biogenesis of the Apicoplast.

Pathogens. 2025-8-1

[2]
Cross-lineage 5-methylcytosine methylome profiling reveals methylated divergence among Toxoplasma gondii tachyzoites of the three major clonal lineages.

Infect Dis Poverty. 2025-8-19

[3]
A P5-ATPase, TgFLP12, diverging from plant chloroplast lipid transporters mediates apicoplast fatty export in Toxoplasma.

Nat Commun. 2025-7-1

[4]
The Major Facilitator Superfamily Transporter HAP12 Is Critical in Survival and Virulence.

Int J Mol Sci. 2025-4-21

[5]
Dissecting apicoplast functions through continuous cultivation of Toxoplasma gondii devoid of the organelle.

Nat Commun. 2025-3-1

[6]
Functional dissection of prenyltransferases reveals roles in endocytosis and secretory vacuolar sorting in type 2-ME49 strain of .

Virulence. 2024-12

本文引用的文献

[1]
VEuPathDB: the eukaryotic pathogen, vector and host bioinformatics resource center in 2023.

Nucleic Acids Res. 2024-1-5

[2]
Functional screening reveals prenylated proteins required for endocytic trafficking and rhoptry protein sorting.

mBio. 2023-8-31

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Stable endocytic structures navigate the complex pellicle of apicomplexan parasites.

Nat Commun. 2023-4-15

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The Toxoplasma micropore mediates endocytosis for selective nutrient salvage from host cell compartments.

Nat Commun. 2023-2-22

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Two apicoplast dwelling glycolytic enzymes provide key substrates for metabolic pathways in the apicoplast and are critical for Toxoplasma growth.

PLoS Pathog. 2022-11

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The Heptaprenyl Diphosphate Synthase (Coq1) Is the Target of a Lipophilic Bisphosphonate That Protects Mice against Toxoplasma gondii Infection.

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The Extracellular Milieu of 's Lytic Cycle Drives Lab Adaptation, Primarily by Transcriptional Reprogramming.

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