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Title: Poliovirus-associated protein kinase: Destabilization of the virus capsid and stimulation of the phosphorylation reaction by Zn sup 2+

Abstract

The previously described poliovirus-associated protein kinase activity phosphorylates viral proteins VP0 and VP2 as well as exogenous proteins in the presence of Mg{sup 2+}. In this paper, the effect of Zn{sup 2+} on the phosphorylation reaction and the stability of the poliovirus capsid has been studied in detail and compared to that of Mg{sup 2+}. In the presence of Zn{sup 2+}, phosphorylation of capsid proteins VP2 and VP4 is significantly higher while phosphorylation of VP0 and exogenous phosphate acceptor proteins is not detected. The results indicate the activation of more than one virus-associated protein kinase by Zn{sup 2+}. The ion-dependent behavior of the enzyme activities is observed independently of whether the virus was obtained from HeLa or green monkey kidney cells. The poliovirus capsid is destabilized by Zn{sup 2+}. This alteration of the poliovirus capsid structure is a prerequisite for effective phosphorylation of viral capsid proteins. The increased level of phosphorylation of viral capsid proteins results in further destabilization of the viral capsid. As a result of the conformational changes, poliovirus-associated protein kinase activities dissociate from the virus particle. The authors suggest that the destabilizing effect of phosphorylation on the viral capsid plays a role in uncoating of poliovirus.

Authors:
; ; ; ;  [1]
  1. (Univ. of Hamburg (West Germany))
Publication Date:
OSTI Identifier:
7067115
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Virology; (USA); Journal Volume: 63:9
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; PHOSPHOTRANSFERASES; BIOCHEMISTRY; PROTEINS; CONFORMATIONAL CHANGES; ZINC COMPOUNDS; BIOLOGICAL EFFECTS; CATIONS; MAGNESIUM COMPOUNDS; PHOSPHORUS 32; POLIO VIRUS; ALKALINE EARTH METAL COMPOUNDS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; CHARGED PARTICLES; CHEMISTRY; DAYS LIVING RADIOISOTOPES; ENZYMES; IONS; ISOTOPES; LIGHT NUCLEI; MICROORGANISMS; NUCLEI; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; PARASITES; PHOSPHORUS ISOTOPES; PHOSPHORUS-GROUP TRANSFERASES; RADIOISOTOPES; TRANSFERASES; VIRUSES; 550201* - Biochemistry- Tracer Techniques; 560300 - Chemicals Metabolism & Toxicology

Citation Formats

Ratka, M., Lackmann, M., Ueckermann, C., Karlins, U., and Koch, G. Poliovirus-associated protein kinase: Destabilization of the virus capsid and stimulation of the phosphorylation reaction by Zn sup 2+. United States: N. p., 1989. Web.
Ratka, M., Lackmann, M., Ueckermann, C., Karlins, U., & Koch, G. Poliovirus-associated protein kinase: Destabilization of the virus capsid and stimulation of the phosphorylation reaction by Zn sup 2+. United States.
Ratka, M., Lackmann, M., Ueckermann, C., Karlins, U., and Koch, G. Fri . "Poliovirus-associated protein kinase: Destabilization of the virus capsid and stimulation of the phosphorylation reaction by Zn sup 2+". United States.
@article{osti_7067115,
title = {Poliovirus-associated protein kinase: Destabilization of the virus capsid and stimulation of the phosphorylation reaction by Zn sup 2+},
author = {Ratka, M. and Lackmann, M. and Ueckermann, C. and Karlins, U. and Koch, G.},
abstractNote = {The previously described poliovirus-associated protein kinase activity phosphorylates viral proteins VP0 and VP2 as well as exogenous proteins in the presence of Mg{sup 2+}. In this paper, the effect of Zn{sup 2+} on the phosphorylation reaction and the stability of the poliovirus capsid has been studied in detail and compared to that of Mg{sup 2+}. In the presence of Zn{sup 2+}, phosphorylation of capsid proteins VP2 and VP4 is significantly higher while phosphorylation of VP0 and exogenous phosphate acceptor proteins is not detected. The results indicate the activation of more than one virus-associated protein kinase by Zn{sup 2+}. The ion-dependent behavior of the enzyme activities is observed independently of whether the virus was obtained from HeLa or green monkey kidney cells. The poliovirus capsid is destabilized by Zn{sup 2+}. This alteration of the poliovirus capsid structure is a prerequisite for effective phosphorylation of viral capsid proteins. The increased level of phosphorylation of viral capsid proteins results in further destabilization of the viral capsid. As a result of the conformational changes, poliovirus-associated protein kinase activities dissociate from the virus particle. The authors suggest that the destabilizing effect of phosphorylation on the viral capsid plays a role in uncoating of poliovirus.},
doi = {},
journal = {Journal of Virology; (USA)},
number = ,
volume = 63:9,
place = {United States},
year = {Fri Sep 01 00:00:00 EDT 1989},
month = {Fri Sep 01 00:00:00 EDT 1989}
}