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Journal of Virology, November 2002, p. 11748-11752, Vol. 76, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.22.11748-11752.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Mutation of Capsid Protein Phosphorylation Sites Abolishes Cauliflower Mosaic Virus Infectivity

Yvan Chapdelaine,{dagger} David Kirk, Aletta Karsies, Thomas Hohn,* and Denis Leclerc{ddagger}

Friedrich-Miescher Institute, CH-4002 Basel, Switzerland

Received 12 June 2002/ Accepted 13 August 2002

The cauliflower mosaic virus (CaMV) capsid protein is derived by bidirectional processing of the precapsid protein (CP56). We expressed several derivatives of CP56 in Escherichia coli and used them as substrates for virus-associated kinase and casein kinase II purified from plant cells. Three serine residues located at the N terminus of the mature viral protein CP44 were identified as phosphorylation targets. A mutation of one of them in the viral context had little or no effect on viral infectivity, but a mutation of all three serines abolished infectivity. The mapping of phosphorylation sites in CP44, but not CP39 or CP37, and immunodetection of the Zn finger motif in CP44 and CP39, but not CP37, support the model that CP39 is produced from CP44 by N-terminal processing and CP37 is produced from CP39 by C-terminal processing. We discuss the possible role of phosphorylation in the processing and assembly of CaMV capsid protein.

* Corresponding author. Mailing address: Friedrich-Miescher Institute, P.O. Box 2543, CH-4002 Basel, Switzerland. Phone: 41-61-697-7266. Fax: 41-61-697-3976. E-mail: Hohn{at}FMI.CH.

{dagger} Present address: Institute for Biological Sciences, National Research Council Canada, Ottawa, Canada K1A 0R6.

{ddagger} Centre de Recherche en Infectiologie, Université Laval, Québec, Canada G1V 4G2.

Journal of Virology, November 2002, p. 11748-11752, Vol. 76, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.22.11748-11752.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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