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Matrix protein of Vesicular stomatitis virus harbours a cryptic mitochondrial-targeting motif

¹ Centre for Gene Therapeutics, McMaster University, 1200 Main Street W MDCL-5023, Hamilton, ON L8N 3Z5, Canada
² University of Ottawa Heart Institute, 40 Ruskin Street, Ottawa, ON, Canada
³ Ottawa Regional Cancer Centre, University of Ottawa, 503 Smyth Road, Ottawa, ON, Canada

Correspondence
Brian D. Lichty
lichtyb{at}mcmaster.ca

Vesicular stomatitis virus (VSV) is a rhabdovirus that has attracted attention of late as an oncolytic virus and as a vaccine vector. Mutations in the matrix (M) gene of VSV yield attenuated strains that may be very useful in both settings. As a result of this interest in the M protein, this study analysed various M–green fluorescent protein (GFP) fusion constructs. Remarkably, fusion of the N terminus of the M protein to GFP targeted the fluorescent protein to the surface of mitochondria. Mutational analysis indicated that a mitochondrial-targeting motif exists within aa 33–67. Expression of these fusion proteins led to loss of mitochondrial membrane permeability and to an alteration in mitochondrial organization mirroring that seen during viral infection. In addition, a portion of the M protein present in infected cells co-purified with mitochondria. This work may indicate a novel function for this multifunctional viral protein.

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