Exploitation of nuclear functions by human rhinovirus, a cytoplasmic RNA virus
Fig 5
Splicing factor proline and glutamine rich (SFPQ) migrates from the nucleus to the cytoplasm following HRV16 infection.
(A) Tryptic peptides in Fig 2 that correspond to SFPQ are highlighted red as described in the legend for Fig 3. (B) HeLa cells were mock- or HRV16-infected (MOI 10) and fixed then imaged as described in the legend for Fig 4. (C) Western blot analysis of cytoplasmic (C) and nuclear (N) fractions of mock- or HRV16-infected HeLa cells. A C-terminal cleavage product (cp*) was detected in the cytoplasm at 8 hours post infection (hpi). A second cleavage fragment of SFPQ was detected in the nucleus at 8 hpi (cp*). HRV16 3D/3CD,VCL, LMNA, and GAPDH used as in Fig 4. (D) Schematic of SFPQ domains (adapted from [86]) with putative 3CD/3C cleavage sites. The proposed 3CD/3C cleavage site resulting in the fragment observed 4 hpi is indicated in red. The N-terminal portion of SFPQ includes the glycine, proline, and glutamine-rich (GPQ-rich) and DNA-binding domain (DBD). The C-terminal portion contains two RNA-recognition motifs (RRM1 and RRM2), a NonA/paraspeckle (NOPS) domain, a coiled-coiled domain, glycine-rich (G-rich) region, and nuclear localization signal (NLS).