Autor: |
Lo SY; Department of Laboratory Medicine and Biotechnology, Tzu Chi University, Hualien 970, Taiwan.; Department of Laboratory Medicine, Buddhist Tzu Chi General Hospital, Hualien 970, Taiwan., Lai MJ; Department of Laboratory Medicine and Biotechnology, Tzu Chi University, Hualien 970, Taiwan., Yang CH; Department of Laboratory Medicine and Biotechnology, Tzu Chi University, Hualien 970, Taiwan.; Department of Microbiology and Immunology, School of Medicine, Tzu Chi University, Hualien 970, Taiwan., Li HC; Department of Biochemistry, School of Medicine, Tzu Chi University, Hualien 970, Taiwan. |
Abstrakt: |
Deoxynucleoside triphosphates (dNTPs) are crucial for the replication and maintenance of genomic information within cells. The balance of the dNTP pool involves several cellular enzymes, including dihydrofolate reductase (DHFR), ribonucleotide reductase (RNR), and SAM and HD domain-containing protein 1 (SAMHD1), among others. DHFR is vital for the de novo synthesis of purines and deoxythymidine monophosphate, which are necessary for DNA synthesis. SAMHD1, a ubiquitously expressed deoxynucleotide triphosphohydrolase, converts dNTPs into deoxynucleosides and inorganic triphosphates. This process counteracts the de novo dNTP synthesis primarily carried out by RNR and cellular deoxynucleoside kinases, which are most active during the S phase of the cell cycle. The intracellular levels of dNTPs can influence various viral infections. This review provides a concise summary of the interactions between different viruses and the genes involved in dNTP metabolism. |