Rotavirus NSP6 localizes to mitochondria via a predicted N-terminal alpha-helix
Gavan Holloway, Rebecca I Johnson, Yilin Kang, Vi T Dang, Diana Stojanovski, Barbara S Coulson
JOURNAL OF GENERAL VIROLOGY | SOC GENERAL MICROBIOLOGY | Published : 2015
Specific roles have been ascribed to each of the 12 known rotavirus proteins apart from the non-structural protein 6 (NSP6). However, NSP6 may be present at sites of viral replication within the cytoplasm. Here we report that NSP6 from diverse species of rotavirus A localizes to mitochondria via conserved sequences in a predicted N-terminal a-helix. This suggests that NSP6 may affect mitochondrial functions during rotavirus infection.
Awarded by National Health and Medical Research Council of Australia (NHMRC)
Awarded by NHMRC
We are most grateful to Ian H. Holmes for Ty-1 rotavirus, Malcolm McCrae for antibodies to NSP5 and Mike Ryan for antibodies to Sam50 (Humphries et al., 2005) and mitofusin 2. Microscopy was performed using the facilities of the Biological Optical Microscopy Platform at the University of Melbourne. This work was supported by the National Health and Medical Research Council of Australia (NHMRC; ID1023786). B. S. C. is a Senior Research Fellow of the NHMRC (ID628319).