A 37 kilodalton protein kinase associated with cauliflower mosaic virus

Geldreich, Angèle; Albrecht, Huguette; Lebeurier, G.

doi:10.1007/bf00684039

Cited by 6 publications

(2 citation statements)

References 27 publications

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“…The zinc finger motif is of particular importance, since mutations abolish not only the interaction with RNA but also CaMV infectivity. Two types of post‐translational modifications of capsid proteins were described: glycosylation of capsid mature polypeptides (DuPlessis and Smith, 1981) and phosphorylation of the CP precursor and the 42 kDa species by a particle‐associated kinase activity whose origin is still unknown (Geldreich et al ., 1988; Menissier de Murcia et al ., 1986). Recently, three instability determinants were characterized: two at both termini of the CP precursor and a third corresponding to a PEST degradation signal which subsists at the N‐terminus of the 42 kDa polypeptide (Karsies et al ., 2001).…”

Section: Functions Of Camv Proteinsmentioning

confidence: 99%

Cauliflower mosaic virus: still in the news

Haas

Bureau

Geldreich

et al. 2002

Molecular Plant Pathology

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SUMMARY Taxonomic relationship: Cauliflower mosaic virus (CaMV) is the type member of the Caulimovirus genus in the Caulimoviridae family, which comprises five other genera. CaMV replicates its DNA genome by reverse transcription of a pregenomic RNA and thus belongs to the pararetrovirus supergroup, which includes the Hepadnaviridae family infecting vertebrates. Physical properties: Virions are non-enveloped isometric particles, 53 nm in diameter (Fig. 1). They are constituted by 420 capsid protein subunits organized following T= 7 icosahedral symmetry (Cheng, R.H., Olson, N.H. and Baker, T.S. (1992) Cauliflower mosaic virus: a 420 subunit (T= 7), multilayer structure. Virology, 16, 655-668). The genome consists of a double-stranded circular DNA of approximately 8000 bp that is embedded in the inner surface of the capsid. Viral proteins: The CaMV genome encodes six proteins, a cell-to-cell movement protein (P1), two aphid transmission factors (P2 and P3), the precursor of the capsid proteins (P4), a polyprotein precursor of proteinase, reverse transcriptase and ribonuclease H (P5) and an inclusion body protein/translation transactivator (P6). Hosts: The host range of CaMV is limited to plants of the Cruciferae family, i.e. Brassicae species and Arabidopsis thaliana, but some viral strains can also infect solanaceous plants. In nature, CaMV is transmitted by aphids in a non-circulative manner.

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Section: Functions Of Camv Proteinsmentioning

confidence: 99%

Cauliflower mosaic virus: still in the news

Haas

Bureau

Geldreich

et al. 2002

Molecular Plant Pathology

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“…Protein kinase activity was also reported to contribute to a cascade of events controlling the definition of infectivity for a number of retroviruses and nonretroviruses. Many purified virions, including insect viruses, as granulosis virus (1), and plant viruses, including cauliflower mosaic virus (2), have been found to display protein kinase activity associated with their viral particles. For animal viruses, association of protein kinase activity with viral particles has been frequently reported, especially for enveloped virus particles (for review see Ref.…”

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confidence: 99%

Active cAMP-dependent Protein Kinase Incorporated within Highly Purified HIV-1 Particles Is Required for Viral Infectivity and Interacts with Viral Capsid Protein

Cartier¹,

Hemonnot²,

Gay

et al. 2003

Journal of Biological Chemistry

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Host cell components, including protein kinases such as ERK-2/mitogen-activated protein kinase, incorporated within human immunodeficiency virus type 1 (HIV-1) virions play a pivotal role in the ability of HIV to infect and replicate in permissive cells. The present work provides evidence that the catalytic subunit of cAMP-dependent protein kinase (C-PKA) is packaged within HIV-1 virions as demonstrated using purified subtilisin-digested viral particles. Virus-associated C-PKA was shown to be enzymatically active and able to phosphorylate synthetic substrate in vitro. Suppression of virion-associated C-PKA activity by specific synthetic inhibitor had no apparent effect on viral precursor maturation and virus assembly. However, virus-associated C-PKA activity was demonstrated to regulate HIV-1 infectivity as assessed by single round infection assays performed by using viruses produced from cells expressing an inactive form of C-PKA. In addition, virus-associated C-PKA was found to co-precipitate with and to phosphorylate the CAp24 gag protein. Altogether our results indicate that virus-associated C-PKA regulates HIV-1 infectivity, possibly by catalyzing phosphorylation of the viral CAp24 gag protein.

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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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A 37 kilodalton protein kinase associated with cauliflower mosaic virus

Cited by 6 publications

References 27 publications

Cauliflower mosaic virus: still in the news

Cauliflower mosaic virus: still in the news

Active cAMP-dependent Protein Kinase Incorporated within Highly Purified HIV-1 Particles Is Required for Viral Infectivity and Interacts with Viral Capsid Protein

Virion-associated protein kinases

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