Virus-Induced Shut-Off of Host Specific Protein Synthesis

Koch, Friedrich; Koch, Gebhard; Kruppa, Joachim

doi:10.1007/978-1-4684-4124-6_14

Cited by 7 publications

(2 citation statements)

References 91 publications

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“…Our data clearly demonstrate that protein synthesis is inhibited before the reduction in amino acid uptake. Earlier results indicated a parallel decrease in uptake and incorporation of amino acids when either centrifugation or rapid washing of cells collected on filters was used and may be due to more rapid efflux of amino acids in infected cells or to other experimental conditions (14,16). The breakdown of the Na+-K+ gradient and the reduction in membrane potential which occurs at 3 h p.i.…”

Section: Discussionmentioning

confidence: 99%

Poliovirus-induced alterations in HeLa cell membrane functions

Schaefer¹,

Kühne²,

Zibirre³

et al. 1982

J Virol

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Protein synthesis, amino acid uptake, membrane potential, cell volume, Na+ and K+ levels, and ATPase (Na+,K+ activated; EC 3.6.1.3) activity were investigated in control and poliovirus-infected HeLa cells. Inhibition of protein synthesis was first observed 60 min postinfection and reached a maximum at 120 min. The onset of protein synthesis inhibition coincided with a decrease in cell volume and with an elevation of ATPase activity in isolated HeLa cell membranes. Some 3 h after virus adsorption, ATPase activity was inhibited, the Na+-K+ gradient of the cell collapsed, both membrane potential-dependent tetraphenylphosphonium ion uptake and amino acid uptake were reduced, and the cell volume increased. These results provide further experimental support for the hypothesis that modification of the cell membrane plays an important role in the strategy of cytopathogenic viruses in the shutoff of host metabolism and cell death.

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Section: Discussionmentioning

confidence: 99%

Poliovirus-induced alterations in HeLa cell membrane functions

Schaefer¹,

Kühne²,

Zibirre³

et al. 1982

J Virol

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“…It has been suggested that protein phosphorylation may be involved in virus-host interactions and virus-mediated modifications of host cell metabolism. Infection of tissue culture cells by polioviruses leads to a rapid inhibition of cellular macromolecular synthesis, usually referred to as 'shut-off' (for review, see Koch et al, 1982). After specific adsorption of polioviruses to receptors on the host cell membrane, approximately 50 ~ of the viral capsid proteins are detectable intracellularly and remain there in a rather stable form (Habermehl et al, 1974).…”

Section: Discussionmentioning

confidence: 99%

Protein Kinase Activity in Purified Poliovirus Particles and Empty Viral Capsid Preparations

Schârli¹,

Koch²

1984

Journal of General Virology

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SUMMARYPreparations of purified poliovirus type 1, strain Mahoney, and empty viral capsids contain a protein kinase activity. The y-phosphoryl group of [32p]AT P is transferred to all of the capsid proteins. Viral proteins phosphorylated in vitro are recognized by antiserum directed against isolated viral capsid proteins, indicating that phosphorylation does not alter the antigenic sites to such an extent that the recognition by antibodies is abolished. Viral capsid protein phosphorylation exposes new antigenic sites and leads to a destabilization of the virions. The transfer of 32p to viral proteins is linear for 90 min at 37 °C in the presence of 10 mM-Mg 2 + at pH 8-1. Reducing agents or virus-stabilizing agents (such as arildone) reduce the kinase activity and result in a different pattern of capsid protein phosphorylation.

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Protein kinase in nondiabetogenic coxsackievirus B4

Chatterjee

Nejman

1986

Journal of Medical Virology

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Alkali-dissociated, purified preparations of prototype coxsackievirus B4 release a protein kinase that catalyzes the incorporation of gamma-phosphate from 32P-labeled ATP into three virus capsid proteins (VP1, VP3, VP4), several additional proteins of the particle, and exogenous acceptor proteins. Using protamine sulfate as an acceptor protein, we detected nearly 20-fold more enzyme activity in membrane-bound virions (MBV) than in virions of the virus. The activity in the MBV is cyclic nucleotide-independent, divalent cation-dependent, and has a pH optimum of 8.0. Phosphoserine is labeled with 32P. The enzyme activity sediments at about 5S and is separated into at least two peaks of heterogeneous proteins by ion-exchange chromatography. The patterns of phosphorylation by these enzyme peaks are somewhat similar. Coxsackievirus-associated protein kinase appears to be located internally in the virus and may be host-cell-coded. The enzyme appears to be lacking in a variant of the virus that produced diabetes in mice.

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Virus-Induced Shut-Off of Host Specific Protein Synthesis

Cited by 7 publications

References 91 publications

Poliovirus-induced alterations in HeLa cell membrane functions

Poliovirus-induced alterations in HeLa cell membrane functions

Protein Kinase Activity in Purified Poliovirus Particles and Empty Viral Capsid Preparations

Protein kinase in nondiabetogenic coxsackievirus B4

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