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Archives of Virology

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01.04.2011 | Brief Report

Membrane permeabilization of the African horse sickness virus VP5 protein is mediated by two N-terminal amphipathic α-helices

verfasst von: Liesel Stassen, Henk Huismans, Jacques Theron

Erschienen in: Archives of Virology | Ausgabe 4/2011

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Abstract

The 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 protein.

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Titel: Membrane permeabilization of the African horse sickness virus VP5 protein is mediated by two N-terminal amphipathic α-helices
verfasst von: Liesel Stassen
Henk Huismans
Jacques Theron
Publikationsdatum: 01.04.2011
Verlag: Springer Vienna
Erschienen in: Archives of Virology / Ausgabe 4/2011
Print ISSN: 0304-8608
Elektronische ISSN: 1432-8798
DOI: https://doi.org/10.1007/s00705-010-0897-4

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