Stassen, LieselHuismans, H. (Henk), 1942-Theron, Jacques2012-02-272012-02-272011-04Stassen, L, Huismans, H & Theron, J 2011, 'Membrane permeabilization of the African horse sickness virus VP5 protein is mediated by two N-terminal amphipathic α-helices', Archives of Virology, vol. 156, no. 4, pp. 711-715.0304-8608 (print)1432-8798 (online)10.1007/s00705-010-0897-4http://hdl.handle.net/2263/18231The VP5 outer capsid protein of African horse sickness virus (AHSV) is cytotoxic when expressed in Spodoptera frugiperda (Sf-9) cells. Secondary structure analysis of the VP5 amino acid sequence of AHSV-9 identified two N-terminal amphipathic α-helices within the first 43 amino acids. Baculovirus expression of N- and C-terminal truncated VP5 proteins in Sf-9 cells indicated that the N-terminal 43 amino acids correlated with low levels of protein expression and with increased membrane permeabilization and cytotoxicity. Exogenous addition of chemically synthesized VP5 peptides indicated that both N-terminal amphipathic α-helices are required for membrane permeabilization of Sf-9 cells. These findings suggest that AHSV VP5 is a membrane-destabilizing proteinen© Springer-Verlag 2010. The original publication is available at www.springerlink.com,VP5 proteinMembrane permeabilizationN-terminal amphipathic α-helicesAfrican horse sickness virusMembrane proteinsMembranes (Biology) -- PermeabilityPostprint Article