Host translation initiation factor eIF4G binding to Sabin 2 poliovirus IRES domain V (eIF4G-Sabin 2 IRES dV interaction)

The interaction between the host eukaryotic initiation factor 4G (eIF4G) and domain V of the poliovirus internal ribosome entry site (IRES) is a fundamental requirement for the initiation of viral protein synthesis. In the Sabin 2 vaccine strain, a specific G-to-A point mutation at nucleotide 481 (G481A) within domain V significantly reduces the binding affinity of eIF4G, which is the primary mechanism for the strain's attenuated neurovirulence (Ochs et al., 2003; JBC, 2018). This interaction is essential for recruiting the 40S ribosomal subunit to the viral RNA, bypassing the need for a 5' cap (Sweeney et al., 2014). Because this interface is critical for viral replication but distinct from the mechanisms used for most host cell mRNAs, it represents a potential target for the development of specific antiviral agents. Small molecules like 4EGI-1 and hippuristanol have been used in research to study and inhibit this translational pathway, highlighting the therapeutic potential of disrupting the eIF4G-IRES complex (Cell, 2006; JBC, 2018).

Other names

eIF4G-PV IRES domain V interactioneIF4G-Sabin 2 IRES interactioneIF4G-Sabin 2 IRES dV complexeIF4G-Sabin 2 IRES domain V bindingeIF4G-PV2 IRES domain V binding

Inhibition of viral translation initiation by disrupting the recruitment of the 40S ribosomal subunit to the viral IRES.