Proteomic analysis of the EhV-86 virion

Michael J Allen¹ , Julie A Howard² , Kathryn S Lilley² and William H Wilson¹^,3

¹Plymouth Marine Laboratory, Prospect Place, The Hoe, Plymouth, PL1 3DH, UK

²Cambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR, UK

³Bigelow Laboratory for Ocean Sciences, 180 McKown Point, PO Box 475, W. Boothbay Harbor, Maine, 04575-0475, USA

author email corresponding author email

Proteome Science 2008, 6:11doi:10.1186/1477-5956-6-11


Published:	17 March 2008

Abstract

Background

Emiliania huxleyi virus 86 (EhV-86) is the type species of the genus Coccolithovirus within the family Phycodnaviridae. The fully sequenced 407,339 bp genome is predicted to encode 473 protein coding sequences (CDSs) and is the largest Phycodnaviridae sequenced to date. The majority of EhV-86 CDSs exhibit no similarity to proteins in the public databases.

Results

Proteomic analysis by 1-DE and then LC-MS/MS determined that the virion of EhV-86 is composed of at least 28 proteins, 23 of which are predicted to be membrane proteins. Besides the major capsid protein, putative function can be assigned to 4 other components of the virion: two lectin proteins, a thioredoxin and a serine/threonine protein kinase.

Conclusion

This study represents the first steps toward the identification of the protein components that make up the EhV-86 virion. Aside from the major capsid protein, whose function in the virion is well known and defined, the nature of the other proteins suggest roles involved with viral budding, caspase activation, signalling, anti-oxidation, virus adsorption and host range determination.