Purine nucleoside phosphorylase (PNP) is a key enzyme in the purine salvage pathway. It catalyses the reversible phosphorolysis of purine (2'-deoxy)ribonucleosides to free bases and (2'-deoxy)ribose 1-phosphates. Here, a novel piscine viral PNP gene that was identified from grouper iridovirus (GIV), a causative agent of an epizootic fish disease, is reported. This putative GIV PNP gene encodes a protein of 285 aa with a predicted molecular mass of 30 332 Da and shows high similarity to the human PNP gene. Northern and Western blot analyses of GIV-infected grouper kidney (GK) cells revealed that PNP expression increased in cells with time from 6 h post-infection. Immunocytochemistry localized GIV PNP in the cytoplasm of GIV-infected host cells. PNP-EGFP fusion protein was also observed in the cytoplasm of PNP-EGFP reporter construct-transfected GK and HeLa cells. From HPLC analysis, the recombinant GIV PNP protein was shown to catalyse the reversible phosphorolysis of purine nucleosides and could accept guanosine, inosine and adenosine as substrates. In conclusion, this is the first report of a viral PNP with enzymic activity.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1099/vir.0.80249-0 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Creating a Halotolerant Degrader for Efficient Mineralization of p-Nitrophenol-Substituted Organophosphorus Pesticides in High-Saline Wastewater.
Biotechnol Bioeng
January 2025
Department of Biochemistry and Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
The bioaugmentation performance is severely reduced in the treatment of high-saline pesticide wastewater because the growth and degradation activity of pesticide degraders are significantly inhibited by high salt concentrations. In this study, a heterologous biodegradation pathway comprising the seven genes mpd/pnpABCDEF responsible for the bioconversion of p-nitrophenol (PNP)-substituted organophosphorus pesticides (OPs) into β-oxoadipate and the genes encoding Vitreoscilla hemoglobin (VHb) and green fluorescent protein (GFP) were integrated into the genome of a salt-tolerant chassis Halomonas cupida J9, to generate a genetically engineered halotolerant degrader J9U-MP. RT-PCR assays demonstrated that the nine exogenous genes are successfully transcribed to mRNA in J9U-MP.
View Article and Find Full Text PDFIntegrated bioinformatics analysis and experimental validation of exosome-related gene signature in steroid-induced osteonecrosis of the femoral head.
J Orthop Surg Res
January 2025
Department of Hand-Foot Microsurgery, Shenzhen Nanshan People's Hospital, The 6th Affiliated Hospital of Shenzhen University Health Science Center, Shenzhen, China.
Background: Steroid-induced osteonecrosis of the femoral head (SIONFH) is a universal hip articular disease and is very hard to perceive at an early stage. The understanding of the pathogenesis of SIONFH is still limited, and the identification of efficient diagnostic biomarkers is insufficient. This research aims to recognize and validate the latent exosome-related molecular signature in SIONFH diagnosis by employing bioinformatics to investigate exosome-related mechanisms in SIONFH.
View Article and Find Full Text PDFHematopoietic stem cell transplantation for purine nucleoside phosphorylase deficiency with two novel mutations: a case report and review of literature.
Hematology
December 2025
Department of Hematology & Oncology, Children's Hospital of Soochow University, Suzhou, People's Republic of China.
Purpose: We report the case of a 6-year-old boy who presented with muscular hypertonia, impaired growth, and recurrent infections, who was diagnosed with purine nucleoside phosphorylase (PNP) deficiency with two novel mutations in the gene. He underwent a hematopoietic stem cell transplantation (HSCT) from an unrelated donor, and we observed the clinical outcome.
Methods: We retrospectively analyzed the clinical manifestations and outcomes of this patient who underwent HSCT.
Characterization of a family IV esterase from extremely halophilic archaeon Haloarcula japonica.
Extremophiles
December 2024
School of Life Science and Technology, Institute of Science Tokyo, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan.
Article Synopsis
- The novel esterase gene lipP1, found in the extremely halophilic archaeon Haloarcula japonica, encodes the enzyme HjEstP1, classified as a family IV esterase with specific conserved motifs.
- HjEstP1 was expressed in its original strain, purified, and characterized, revealing optimal activity at a pH of 6.0 and temperatures above 60 °C.
- The enzyme demonstrated increased activity with higher NaCl concentrations, peaking at over 4.5 M, and preferentially hydrolyzed pNP and glycerol esters with short-chain fatty acids, marking it as the first esterase identified from an extremely halophilic archaeon through homologous expression.
[Molecular mechanism of high-altitude hypoxia-induced lipid metabolism disorder in mouse spleen tissue].
Nan Fang Yi Ke Da Xue Xue Bao
October 2024
College of Medicine of Qinghai University, Xining 810016, China.
Objective: To investigate the molecular mechanism of lipid metabolism disorder in mouse spleen tissues due to high-altitude hypoxia.
Methods: Ten C57BL/6 male mice were randomly divided into normoxia group (maintained at an altitude of 400 m) and high-altitude hypoxia group (maintained at 4200 m) for 30 days (=5). Lipidomics and metabolomics analyses of the spleen tissue of the mice were conducted using liquid chromatography-mass spectrometry (LC-MS) to identify the differential metabolites, which were further analyzed by KEGG enrichment and pathway analyses, and the differential genes were screened through transcriptome sequencing.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!