The ACBP gene family in Rhodnius prolixus : Expression, characterization and function of RpACBP-1

Majerowicz, David; Hannibal-Bach, Hans Kristian; Castro, Rodolfo S C; Bozaquel-Morais, Bruno L.; Auger, Michèle; Grillo, Luciano Aparecido Meireles; Masuda, Cláudio A.; Færgeman, Nils J.; Knudsen, Jens; Gondim, Kátia C.

doi:10.1016/j.ibmb.2016.03.002

Cited by 26 publications

(31 citation statements)

References 51 publications

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“…Overexpression of ACBP6 in Arabidopsis results in a decrease in PC, an increase in phosphatidic acid (Liao, Chen, & Chye, ). ACBP1 knockdown in Rhodnius prolixus leads to reduction in TAG (Majerowicz et al, ), whereas our research showed that TgACBP1 and TgSCP2 double disruption blocked production of glyceride, such as TAG, DAG, and MAG containing various acyl chains. We also observed an overall decrease in the abundance of various CDP‐DAG.…”

Section: Discussioncontrasting

confidence: 55%

Synergistic roles of acyl-CoA binding protein (ACBP1) and sterol carrier protein 2 (SCP2) inToxoplasmalipid metabolism

Cui²,

Liu

et al. 2018

Cellular Microbiology

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Toxoplasma gondii relies on apicoplast‐localised FASII pathway and endoplasmic reticulum‐associated fatty acid elongation pathway for the synthesis of fatty acids, which flow through lipid metabolism mainly in the form of long‐chain acyl‐CoA (LCACoAs) esters. Functions of Toxoplasma acyl‐CoA transporters in lipid metabolism remain unclear. Here, we investigated the roles of acyl‐CoA‐binding protein (TgACBP1) and a sterol carrier protein‐2 (TgSCP2) as cytosolic acyl‐CoA transporters in lipid metabolism. The fluormetric binding assay and yeast complementation confirmed the acyl‐CoA binding activities of TgACBP1 and TgSCP2, respectively. Disruption of either TgACBP1 or TgSCP2 caused no obviously phenotypic changes, whereas double disruption resulted in defects in intracellular growth and virulence to mice. Gas chromatography coupled with mass spectrometry (GC–MS) results showed that TgACBP1 or TgSCP2 disruption alone led to decreased abundance of C18:1, whereas double disruption resulted in reduced abundance of C18:1, C22:1, and C24:1. 13C labelling assay combined with GC–MS showed that double disruption of TgACBP1 and TgSCP2 led to reduced synthesis rates of C18:0, C22:1, and C24:1. Furthermore, high performance liquid chromatography coupled with high resolution mass spectrometry (HPLC‐HRMS) was used for lipidomic analysis of parasites and indicated that loss of TgACBP1 and TgSCP2 caused serious defects in production of glycerides and phospholipids. Collectively, TgACBP1 and TgSCP2 play synergistic roles in lipid metabolism in T. gondii.

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Section: Discussioncontrasting

confidence: 55%

Synergistic roles of acyl-CoA binding protein (ACBP1) and sterol carrier protein 2 (SCP2) inToxoplasmalipid metabolism

Cui²,

Liu

et al. 2018

Cellular Microbiology

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“…Arabidopsis thaliana mutants lacking ACBPs showed altered lipid composition, thereby increasing stress susceptibility (Chye et al ., ; Chen et al ., ; Xiao et al ., ; Du et al ., ,b; Xue et al ., ), retarding pollen development (Hsiao et al ., ), reducing seed weight (Hsiao et al ., 2014a), and causing embryonic lethality (Chen et al ., ). ACBP mutations also adversely affected embryogenesis in mammals (Zhou et al ., ; Landrock et al ., ), worms (Elle et al ., ), and insects (Majerowicz et al ., ).…”

Section: Introductionmentioning

confidence: 97%

The overexpression of rice ACYL‐CoA‐BINDING PROTEIN2 increases grain size and bran oil content in transgenic rice

et al. 2019

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As Oryza sativa (rice) seeds represent food for over three billion people worldwide, the identification of genes that enhance grain size and composition is much desired. Past reports have indicated that Arabidopsis thaliana acyl-CoA-binding proteins (ACBPs) are important in seed development but did not affect seed size. Herein, rice OsACBP2 was demonstrated not only to play a role in seed development and germination, but also to influence grain size. OsACBP2 mRNA accumulated in embryos and endosperm of germinating seeds in qRT-PCR analysis, while b-glucuronidase (GUS) assays on OsACBP2pro::GUS rice transformants showed GUS expression in embryos, as well as the scutellum and aleurone layer of germinating seeds. Deletion analysis of the OsACBP2 5'-flanking region revealed five copies of the seed cis-element, Skn-I-like motif (À1486/À1482, À956/À952, À939/À935, À826/À822, and À766/À762), and the removal of any adversely affected expression in seeds, thereby providing a molecular basis for OsACBP2 expression in seeds. When OsACBP2 function was investigated using osacbp2 mutants and transgenic rice overexpressing OsACBP2 (OsACBP2-OE), osacbp2 was retarded in germination, while OsACBP2-OEs performed better than the wild-type and vector-transformed controls, in germination, seedling growth, grain size and grain weight. Transmission electron microscopy of OsACBP2-OE mature seeds revealed an accumulation of oil bodies in the scutellum cells, while confocal laser scanning microscopy indicated oil accumulation in OsACBP2-OE aleurone tissues. Correspondingly, OsACBP2-OE seeds showed gain in triacylglycerols and long-chain fatty acids over the vector-transformed control. As dietary rice bran contains beneficial bioactive components, OsACBP2 appears to be a promising candidate for enriching seed nutritional value.

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“…Our biochemical data indicate that rNcACBP is capable of binding to palmitoyl-CoA (25 μM) with the highest binding affinity (K D = 11.65 nM) in vitro. In addition, the abnormal phenotype of slow growth and an increased number of multilobed vacuoles in ΔScACBP mutant yeast [15] can be rescued by NcACBP, similar to the effect of RpACBP-1 [48], demonstrating that NcACBP possibly plays a similar role to that of ScACBP as a homologous protein.…”

Section: Discussionmentioning

confidence: 72%

Functional characterization of acyl-CoA binding protein in Neospora caninum

Zhou

Zhang

et al. 2020

Parasites Vectors

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Background: Lipid metabolism is pivotal for the growth of apicomplexan parasites. Lipid synthesis requires bulk carbon skeleton acyl-CoAs, the transport of which depends on the acyl-CoA binding protein (ACBP). In Neospora caninum, the causative agent of neosporosis, the FASII pathway is required for growth and pathogenicity. However, little is known about the fatty acid transport mechanism in N. caninum. Methods:We have identified a cytosolic acyl-CoA binding protein, with highly conserved amino acid residues and a typical acyl-CoA binding domain in N. caninum. The recombinant NcACBP protein was expressed to verify the binding activities of NcACBP in vitro, and the heterologous expression of NcACBP in Δacbp yeast in vivo. Lipid extraction from ΔNcACBP or the wild-type of N. caninum was analyzed by GC-MS or TLC. Furthermore, transcriptome analysis was performed to compare the gene expression in different strains.Results: The NcACBP recombinant protein was able to specifically bind acyl-CoA esters in vitro. A yeast complementation assay showed that heterologous expression of NcACBP rescued the phenotypic defects in Δacbp yeast, indicating of the binding activity of NcACBP in vivo. The disruption of NcACBP did not perturb the parasite's growth but enhanced its pathogenicity in mice. The lipidomic analysis showed that disruption of NcACBP caused no obvious changes in the overall abundance and turnover of fatty acids while knockout resulted in the accumulation of triacylglycerol. Transcriptional analysis of ACBP-deficient parasites revealed differentially expressed genes involved in a wide range of biological processes such as lipid metabolism, posttranslational modification, and membrane biogenesis. Conclusions:Our study demonstrated that genetic ablation of NcACBP did not impair the survival and growth phenotype of N. caninum but enhanced its pathogenicity in mice. This deletion did not affect the overall fatty acid composition but modified the abundance of TAG. The loss of NcACBP resulted in global changes in the expression of multiple genes. This study provides a foundation for elucidating the molecular mechanism of lipid metabolism in N. caninum.

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The ACBP gene family in Rhodnius prolixus : Expression, characterization and function of RpACBP-1

Cited by 26 publications

References 51 publications

Synergistic roles of acyl-CoA binding protein (ACBP1) and sterol carrier protein 2 (SCP2) inToxoplasmalipid metabolism

Synergistic roles of acyl-CoA binding protein (ACBP1) and sterol carrier protein 2 (SCP2) inToxoplasmalipid metabolism

The overexpression of rice ACYL‐CoA‐BINDING PROTEIN2 increases grain size and bran oil content in transgenic rice

Functional characterization of acyl-CoA binding protein in Neospora caninum

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