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 in vitro, progressive degradation of native virus into 80S empty capsids occurred upon incubation at 37 °C in a buffer of low ionic strength containing 20 mm-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-mm-Tris-HCl pH 7.5 containing 2 mm-CaCl2. Although the poliovirus receptor is able to induce conformational alterations of the capsid, low ion concentration could contribute to virus uncoating as well.
CordsC. E.,
JamesC. G.,
McLarenL. C.1975; Alteration of capsid proteins of coxsackievirus A 13 by low ionic concentrations. Journal of Virology 15:244–252
CrowellR. L.,
LandauB. J.1983; Receptors in the initiation of picornavirus infections. In Comprehensive Virology vol 18 pp 1–42 Edited by
Fraenkel-ConratH.,
WagnerR. R.
New York: Plenum Press;
De SenaJ.,
MandelB.1976; Studies on the in vitro uncoating of poliovirus. I. Characterization of the modifying factor and the modifying reaction. Virology 70:470–483
FricksC. E.,
HogleJ. M.1990; Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP 1 is responsible for liposome binding. Journal of Virology 64:1934–1945
GuttmanN.,
BaltimoreD.1977; A plasma membrane component able to bind and alter virions of poliovirus type 1: studies on cell-free alteration using a simplified assay. Virology 82:25–36
KaplanG.,
FreistadtM. S.,
RacanielloV. R.1990; Neutralization of poliovirus by cell receptors expressed in insect cells. Journal of Virology 64:4697–4702
KrausslichH.-G.,
HölscherC.,
ReuerQ.,
HarberJ.,
WimmerE.1990; Myristoylation of the poliovirus polyprotein is required for proteolytic processing of the capsid and for viral infectivity. Journal of Virology 64:2433–2436
KrüseJ.,
TimminsP. A.,
WitzJ.1982; A neutron scattering study on the structure of compact and swollen forms of southern bean mosaic virus. Virology 119:42–50
Lonberg-HolmK.,
GosserL. B.,
ShimshickE. J.1976; Interaction of liposomes with subviral particles of poliovirus type 2 and rhinovirus type 2. Journal of Virology 19:746–749
MadshusI. H.,
OlsnesS.,
SandvigK.1984; Mechanism of entry into the cytosol of poliovirus type 1: requirement for low pH. Journal of Cell Biology 98:1194–1200
MarcD.,
MassonG.,
GirardM.,
Van der WerfS.1990; Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of non-infectious virus particles. Journal of Virology 64:4099–4107
RombautB.,
VrijsenR.,
BrioenP.,
BoeyéA.1982; A pH-dependent antigenic conversion of empty capsids of poliovirus studied with the aid of monoclonal antibodies to N and H antigen. Virology 122:215–218
WetzK.,
ZeichhardtH.,
WillingmannP.,
HabermehlK.-O.1983; Dense particles and slow sedimenting particles produced by ultraviolet irradiation of poliovirus. Journal of General Virology 64:1263–1275