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Characterization of the equine infectious anaemia virus S2 protein

Retrovirus Molecular Biology Group, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK¹
Oxford BioMedica (UK) Ltd, Oxford Science Park, Oxford OX4 4GA, UK²
Department of Biomolecular Sciences, UMIST, PO Box 88, Manchester M60 1QD, UK³

Author for correspondence: Kyriacos Mitrophanous. Fax +44 1865 783001. e-mail k.mitrophanous{at}oxfordbiomedica.co.uk

S2 is an accessory protein of equine infectious anaemia virus (EIAV), the function of which is unknown. In order to gain insight into the function of S2, the intracellular localization of the protein, its interaction with viral proteins and its incorporation into viral particles have been investigated. Immunolocalization of S2 revealed punctate staining in the cytoplasm and the S2 protein co-precipitated with the EIAV Gag precursor. Despite overexpression of S2 through the use of a codon-optimized sequence, there was no preferential association of S2 with EIAV particles. These data suggest that S2 may function to organize the Gag protein during particle assembly in the cytoplasm but that it is unlikely to be involved in the early stages of the virus life-cycle.