Protein kinase in nondiabetogenic coxsackievirus B4

Chatterjee, Nando K.; Nejman, Catherine

doi:10.1002/jmv.1890190408

Cited by 8 publications

(2 citation statements)

References 29 publications

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“…The lack of a consensus sequence in the promoters of genes transactivated by the EIA 289R protein has suggested that this protein interacts with DNA only indirectly, a conclu-sion consistent with the binding of ElA proteins to cellular proteins demonstrated by immunoprecipitation (Yee et al, 1985;Harlow et al, 1986) and in cell fractionation studies (Feldman and Nevins, 1983;Chatterjee and Flint, 1986). Recently, a 289R ElA protein synthesized in Escherichia coli has been shown to be retained on DNA -cellulose columns (Ko et al, 1986) and to activate transcription from adenoviral DNA templates in vitro (Spangler et al, 1987).…”

Section: Introductionmentioning

confidence: 65%

DNA-binding properties of an adenovirus 289R E1A protein.

et al. 1988

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An adenovirus 2 289 amino acid (289R) E1A protein purified from Escherichia coli has been shown to interact with DNA by two independent methods. UV‐crosslinking of complexes containing unmodified, uniformly 32P‐labelled DNA and purified E1A protein induced efficient labelling of the protein with covalently attached oligonucleotides, indicating that the E1A protein itself contacts DNA. Discrete nucleoprotein species were also observed when E1A protein–DNA complexes were analysed by gel electrophoresis. Although the 289R E1A protein exhibited no significant binding to single‐stranded DNA or to RNA, no evidence for its sequence‐specific binding to double‐stranded DNA was obtained with either assay. Identification of the sites of covalent attachment of 32P‐labelled oligonucleotides by partial proteolysis of the crosslinked E1A protein indicated that the interaction of this protein with DNA is mediated via domain(s) in the C‐terminal half of the protein. Such previously unrecognized DNA‐binding activity is likely to contribute to the regulatory activities of this important adenoviral protein.

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Section: Introductionmentioning

confidence: 65%

DNA-binding properties of an adenovirus 289R E1A protein.

et al. 1988

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“…Sucrose gradient-purified FMDV was disrupted by dithiothreitol and Triton X-100 and three peaks of kinase activity (P2, D1, and D2) were identified by ion-exchange chromatography on DEAE-and PC-cellulose columns [116]. Coxsackievirus B4 (CVB4), another picornavirus, also contained a VAPK [117]. Members of the togavirus family (e. g., Sindbis virus and Semliki forest virus) have also been reported to contain VAPK [118,119].…”

Section: Picornaviridae-and Togaviridae-associated Kinasementioning

confidence: 99%

Virion-associated protein kinases

Hui¹

2002

CMLS, Cell. Mol. Life Sci.

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Many purified virions, particularly enveloped virus particles (such as retrovirus, hepadnavirus, herpesvirus, orthomyxovirus, and paramyxovirus), contain protein kinase (PK) activity. This type of PK has been called virion-associated protein kinase (VAPK). Even though some VAPKs are identified either as a cellular PK or viral-encoded kinase, many remain to be identified. Although the roles of VAPKs are not yet well characterized, there is ample evidence to suggest their importance in viral infectivity, uncoating, transcription, and replication.

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Purification and characterization of a strain of coxsackievirus b4 of human origin that induces diabetes in mice

Chatterjee

Nejman

Gerling

1988

Journal of Medical Virology

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A diabetogenic strain of coxsackievirus B4 of human origin has been purified to study its biochemistry and diabetogenicity. Tissue culture cells infected with the virus contain two distinct types of particles--virions and membrane-bound virions (MBV). MBVs are lighter (p = 1.29) than virions (p = 1.34), and they contain relatively more protein than RNA. Virons contain four capsid proteins, VPI-4, of various molecular weights: VP1, 37,500; VP2, 36,000; VP3, 26,000; and VP4, 5,500. MBVs contain three of these proteins and several additional proteins of molecular weights 45,000 to greater than 92,500, possibly of host or viral origin. The RNA in each type of particle is a 35S molecule; T1 oligonucleotide fingerprint profiles suggest minor differences in the two RNAs. Hybridization experiments show a great deal of sequence homology between the RNA of the diabetogenic strain and the RNA of prototype CB4, which does not induce overt diabetes. MBVs are 10-70 times less infective than virions, yet they are more pathogenic in mice and induce significantly higher glucose intolerance (hyperglycemia). The hyperglycemic response appears to be lower in mice infected with both types of particles than in mice infected with MBVs alone. Thus, the two subpopulations of virions present in the diabetogenic strain differ biochemically and in their ability to induce diabetes.

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Protein kinase in nondiabetogenic coxsackievirus B4

Cited by 8 publications

References 29 publications

DNA-binding properties of an adenovirus 289R E1A protein.

DNA-binding properties of an adenovirus 289R E1A protein.

Virion-associated protein kinases

Purification and characterization of a strain of coxsackievirus b4 of human origin that induces diabetes in mice

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