1887

Abstract

Poliovirus eclipse products were totally precipitated from infected HeLa cells after different times of infection by using TCA, suggesting that cellular enzymic digestion of parental proteins was not involved in virus uncoating. In an investigation of poliovirus thermal stability , progressive degradation of native virus into 80S empty capsids occurred upon incubation at 37 °C in a buffer of low ionic strength containing 20 m-Tris-HCl pH 7.5, whereas in Eagle's medium or in the presence of L cells degradation was very slow. Degradation was faster at alkaline than at acid pH. Furthermore, liberation of the viral RNA was prevented and 135S particles were produced upon treatment of virus at 37 °C in 20-m-Tris-HCl pH 7.5 containing 2 m-CaCl. Although the poliovirus receptor is able to induce conformational alterations of the capsid, low ion concentration could contribute to virus uncoating as well.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-72-10-2541
1991-10-01
2019-08-19
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-72-10-2541
Loading

Most Cited This Month

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error