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Proteomic analysis of the Spodoptera frugiperda ascovirus 1a virion reveals 21 proteins

Yeping Tan^1,

Dennis K. Bideshi^1,2,

¹ Department of Entomology, University of California, Riverside, Riverside, CA 92521, USA
² California Baptist University, Department of Natural and Mathematical Sciences, 8432 Magnolia Avenue Riverside, CA 92504, USA
³ CNRS, UMR 6239, Génétique, Immunothérapie, Chimie et Cancer, Université Francois Rabelais, UFR des Sciences & Techniques, Parc de Grandmont, 37200 Tours, France
⁴ CHRU de Tours, Université Francois Rabelais, UFR des Sciences & Techniques, Parc de Grandmont, 37200 Tours, France
⁵ Interdepartmental Graduate Programs in Genetics and Cell, Molecular & Developmental Biology, University of California Riverside, Riverside, CA 92521, USA

Correspondence
Brian A. Federici
brian.federici{at}ucr.edu

The Spodoptera frugiperda ascovirus 1a (SfAV-1a) is a double-stranded DNA virus that attacks lepidopteran larvae, in which it produces enveloped virions with complex symmetry which have an average diameter of 130 nm and length of 400 nm. Here, we report identification of 21 SfAV-1a-encoded proteins that occur in the virion, as determined by nano-liquid chromatography/tandem mass spectrometry. These included a helicase (ORF009), nuclease (ORF075), ATPase (ORF047), serine/threonine-like protein kinase (ORF064), inhibitor of apoptosis-like protein (ORF015), thiol oxidoreductase-like protein (ORF061), CTD phosphatase (ORF109), major capsid protein (ORF041) and a highly basic protein, P64 (ORF048). The latter two were the most abundant. Apart from ascoviruses, the closest orthologues were found in iridoviruses, providing further evidence that ascoviruses evolved from invertebrate iridoviruses. These results establish a foundation for investigating how ascovirus virion proteins interact to form their complex asymmetrical structure, as well as for elucidating the mechanisms involved in SfAV-1a virion morphogenesis.

These authors contributed equally to this work.

This article has been cited by other articles:

				Y. Tan, T. Spears, D. K. Bideshi, J. J. Johnson, R. Hice, Y. Bigot, and B. A. Federici P64, a Novel Major Virion DNA-Binding Protein Potentially Involved in Condensing the Spodoptera frugiperda Ascovirus 1a Genome J. Virol., March 15, 2009; 83(6): 2708 - 2714. [Abstract] [Full Text] [PDF]