Biochemical characterization of Periplaneta fuliginosa densovirus non-structural protein NS1

Biochemical and Biophysical Research Communications
Bo YangYuanyang Hu

Abstract

The non-structural (NS) proteins of parvoviruses are involved in essential steps of the viral life cycle. Various biochemical functions, such as ATP binding, ATPase, site-specific DNA binding and nicking, and helicase activities, have been assigned to the protein NS1. Compared with the non-structural proteins of the vertebrate parvoviruses, the NS proteins of the Densovirinae have not been well characterized. Here, we describe the biochemical properties of NS1 of Periplaneta fuliginosa densovirus (PfDNV). We have expressed and purified NS1 using a baculovirus system and analyzed its enzymatic activity. The purified recombinant NS1 protein possesses ATPase- and ATP- or dATP-dependent helicase activity requiring either Mg(2+) or Mn(2+) as a cofactor. The ATPase activity of NS1 can be efficiently stimulated by single-stranded DNA. The ATPase coupled helicase activity was detected on blunt-ended double-stranded oligonucleotide substrate. Using South-Western and Dot-spot assays, we identified a DNA fragment that is recognized specifically by the recombinant NS1 protein. The fragment consists of (CAC)(4) and is located on the hairpin region of the terminal palindrome. The domain for DNA binding was defined to the amino-terminal regio...Continue Reading

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Citations

Sep 9, 2011·Journal of Virology·Tatiana V KapelinskayaDmitry V Mukha
Sep 3, 2010·The American Journal of Tropical Medicine and Hygiene·Jin-Bao GuXiao-Guang Chen
Apr 29, 2008·Journal of Genetics and Genomics = Yi Chuan Xue Bao·Huijuan YinKeping Chen
May 23, 2007·Biochemical and Biophysical Research Communications·Liu HuYuanyang Hu
Nov 5, 2016·Biochemistry·Jonathan L SanchezNancy C Horton
Nov 28, 2019·Parasites & Vectors·Michaela Herz, Klaus Brehm

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