Studies on the in vitro uncoating of poliovirus

Sena, John De; Mandel, Benjamin

doi:10.1016/0042-6822(76)90288-9

Cited by 66 publications

(8 citation statements)

References 25 publications

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“…7, and it is evident that there were no differences between control and inactivated viruses. In these experiments, the early modified and further modified articles described by DeSena and Torian (8) were observed in gradient profiles of cells infected with control or chlorine dioxide-inactivated virus.…”

Section: Resultsmentioning

confidence: 99%

“…Direction of sedimentation is indicated by the horizontal arrows. dioxide has been reported to remain undissociated in aqueous solutions at pH values from 4.0 to 8.4 (2). In an alkaline solution it disproportionates to chlorite (C102-) and chlorate (Cd03-) via the following reaction: 2C102 + 20H-= H20 + C102-+ C103- (8). Since the end product formed as a result of the oxidation of organic matter by undissociated chlorine dioxide is the C102ion (9, 16), it is possible that C103is the most active species in inactivation of poliovirus at alkaline pH levels.…”

Section: Discussionmentioning

confidence: 99%

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Mechanisms of inactivation of poliovirus by chlorine dioxide and iodine

Alvarez¹,

O’Brien²

1982

Appl Environ Microbiol

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Chlorine dioxide and iodine inactivated poliovirus more efficiently at pH 10.0 than at pH 6.0. Sedimentation analyses of viruses inactivated by chlorine dioxide and iodine at pH 10.0 showed that viral RNA separated from the capsids, resulting in the conversion of virions from 156S structures to 80S particles. The RNAs released from both chlorine dioxide-and iodine-inactivated viruses cosedimented with intact 35S viral RNA. Both chlorine dioxide and iodine reacted with the capsid proteins of poliovirus and changed the pI from pH 7.0 to pH 5.8. However, the mechanisms of inactivation of poliovirus by chlorine dioxide and iodine were found to differ. Iodine inactivated viruses by impairing their ability to adsorb to HeLa cells, whereas chlorine dioxide-inactivated viruses were able to adsorb, penetrate, and initiate uncoating normally. Sedimentation analysis of extracts of HeLa cells infected with chlorine dioxide-inactivated viruses showed a reduced incorporation of [14C]uridine into new viral RNA. We concluded, then, that chlorine dioxide inactivated poliovirus by reacting with the viral RNA and impairing the ability of the viral genome to act as a template for RNA synthesis.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Mechanisms of inactivation of poliovirus by chlorine dioxide and iodine

Alvarez¹,

O’Brien²

1982

Appl Environ Microbiol

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“…Receptor binding can also result in conformational transitions of viral capsids. In vitro, poliovirus forms 135 and 80S particles upon incubation with extracts of susceptible cells or soluble forms of the poliovirus receptor at a neutral pH above 30°C (6,20,27,50). This again is in contradiction to in vivo data showing that intact poliovirus can be recovered from cells even 4 h after infection (7,33,69).…”

mentioning

confidence: 81%

Uncoating of human rhinovirus serotype 2 from late endosomes

Prchla

Kuechler

Blaas

et al. 1994

J Virol

143

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The internalization pathway and mechanism of uncoating of human rhinovirus serotype 2 (HRV2), a minor-group human rhinovirus, were investigated. Kinetic analysis revealed a late endosomal compartment as the site of capsid modification from D to C antigenicity. The conformational change as well as the infection was prevented by the specific V-ATPase inhibitor bafilomycin Al. A requirement for ATP was also demonstrated with purified endosomes in vitro. Capsid modifications occurred at a pH of 5.5 regardless of whether the virus was entrapped in isolated endosomes or free in solution. These findings suggest that the receptor is not directly involved

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“…In polioviruses, the N-HRVs have pseudo T Å 3 icosahedral symmetry. The terminus of VP1 is externalized and is available for prodiameter of the virus is about 300 Å and the molecular teolytic cleavage (DeSana and Mandell, 1977). After the weight of the virus is approximately 8.5 1 10 6 Da, includ-''A'' particles have released their RNA, they form empty ing RNA.…”

Section: Introductionmentioning

confidence: 99%

Cations in Human Rhinoviruses

et al. 1997

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All known crystal structures of rhinoviruses have some uninterpreted electron density on their fivefold axes at a distance of about 152 +/- 3 A from the viral center. This density had been assumed to be a Ca2+ ion, based on its shape, height, and the presence of Ca2+ ions in the crystallization solutions. Difference electron density maps between EGTA-soaked crystals of human rhinovirus 14 (HRV14), as well as HRV16, and their corresponding native structures show that this density is an EGTA-chelatable ion. Analysis of the coordination geometry indicates that the ions in HRV3, HRV14, and HRV1A could be Ca2+ and the ion in HRV16 might be Zn2+. These cations may play a role in regulation of rhinovirus stability, although the loss of the ion itself does not seem sufficient to lead to viral disassembly.

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Studies on the in vitro uncoating of poliovirus

Cited by 66 publications

References 25 publications

Mechanisms of inactivation of poliovirus by chlorine dioxide and iodine

Mechanisms of inactivation of poliovirus by chlorine dioxide and iodine

Uncoating of human rhinovirus serotype 2 from late endosomes

Cations in Human Rhinoviruses

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