The L* protein of TMEV targets the mitochondrial outer membrane independently of other viral components, potentially involving Hsp70 chaperones.
Hypothesis-generating for TMEV L* mitochondrial function; extends localization data and leaves chaperone mechanisms open for validation.
The L* protein encoded by Theiler's murine encephalomyelitis virus (TMEV) is a unique example of a picornaviral protein encoded by an alternative open reading frame. This protein is an important determinant of TMEV persistence in the mouse central nervous system. We showed that in infected cells, L* is partitioned between the cytosol and the mitochondria. In mitochondria, L* is anchored in the outer membrane and exposed to the cytosol. The targeting of L* to mitochondria is independent of other viral components and likely depends on a conformational signal. L* targeting to mitochondria might involve chaperones of the Hsp70 family, as these proteins are shown to interact.
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Sorgeloos et al. (2011) studied this question.