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Homo sapiens

ABSTRACT: mRNA sequencing of Borna disease virus-infected cells

PROVIDER: PRJDB7385 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	DRR157556_1.fastq.gz	Fastqsanger.gz
	DRR157556_2.fastq.gz	Fastqsanger.gz
	DRR157557_1.fastq.gz	Fastqsanger.gz
	DRR157557_2.fastq.gz	Fastqsanger.gz

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Borna disease virus

Project description:Borna disease virus

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BoDV-1 infection during neuronal differentiation

Project description:Borna disease virus (BoDV-1) is a highly neurotropic RNA virus, which causes neurobehavioral disturbances such as abnormal social activities and memory impairment. In this study, we investigated the effects of BoDV-1 infection on neuronal differentiation and transcriptome of differentiated neuronal cells using persistently BoDV-1-infected SH-SY5Y (SB) cells. Differentiated neuronal cells exhibited transcriptomic changes of genes related to neurite outgrowth and antiviral immune system.

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Crystal structure of Homo sapiens kynureninase.

Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.

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Homo sapiens whole blood.

Project description:RNA extracted at 240min. Samples are rRNA depleted. Expression measurement of Homo sapiens genes.

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2018-12-26 | GSE114175 | GEO

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