Fig. 5.4.

Autophagy-mediated restriction of viral replication. HCV NS5A protein interacts with the IFN-β-inducible protein SHISA5, which transfers NS5A to autophagosomes for further degradation. SMURF1 is indispensable for the co-localization of the SINV capsid protein to p62, which prompts virophagy by shuttling the viral capsid to autophagosomes. FANCC also interacts with SINV capsid protein (not known to be ubiquitinated) and enhance virophagy. Poliovirus breaks the endosomal membrane and releases its genome into the cytoplasm, and Galectin-8 detects the permeated endosomes and marks them for autophagic degradation, but PLA2G16 facilitates viral genome translocation and prevents clearance. Upon HIV viral fusion, TRIM5α induces the recruitment of Atg5 to the TRIM5α–Atg16L1–HIV-1p24 capsid complex, promoting lipidation of LC3 (LC3 II) and thereby mediating autophagosome formation. HIV Vif interacts with the HD6A/APOBEC3G complex to induce its rapid degradation. Autophagy selectively degrades the HIV-1 transactivator Tat, a protein that is essential for HIV-1 transcription and virion production