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Echovirus 9 strain barty non-structural protein 2C has NTPase activity.
M Klein1, H J Eggers, B Nelsen-Salz
1Institut für Virologie der Universität zu Köln, Fürst-Pückler-Str. 56, 50935, Cologne, Germany.
Virus Research
|December 3, 1999
Summary
Picornavirus replication involves non-structural protein 2C, which binds nucleotides. Echovirus 9
Area of Science:
- Virology
- Molecular Biology
- Protein Biochemistry
Background:
- Non-structural protein 2C is crucial for picornavirus replication.
- Protein 2C contains a consensus nucleotide-binding sequence (NTB).
Purpose of the Study:
- To investigate the nucleotide-binding and hydrolysis activity of echovirus 9 protein 2C.
- To determine the role of protein 2C in picornavirus replication.
Main Methods:
- Expressed P2 genes in Escherichia coli as glutathione S-transferase (GST) fusion proteins.
- Purified GST-2B, GST-2C, and GST-2BC fusion proteins.
- Assayed ATPase and GTPase activities of purified proteins in vitro.
Main Results:
- GST-2C and GST-2BC fusion proteins exhibited both ATPase and GTPase activity.
- GST-2B fusion protein did not show significant NTPase activity.
- These findings indicate that protein 2C possesses nucleotide-binding and hydrolysis capabilities.
Conclusions:
- Echovirus 9 protein 2C has intrinsic NTPase activity.
- The nucleotide-binding and hydrolysis site is located within protein 2C.
- Protein 2C is essential for picornavirus replication through its NTPase function.