Poliovirus type 2 (Sabin) capsid protein VP1 (VP1)

The Sabin poliovirus type 2 VP1 capsid protein is a primary structural component of the attenuated poliovirus strain used in oral vaccines. It forms part of the icosahedral capsid that protects the viral RNA genome and is responsible for recognizing and binding to the host cell receptor, CD155 (Poliovirus Receptor) [1.4.1, 1.4.4]. VP1 is highly immunogenic, containing major epitopes that elicit neutralizing antibodies, which are critical for vaccine-induced immunity [1.1.3]. In the context of drug development, VP1 is a target for capsid-binding inhibitors like pocapavir and pleconaril, which fit into a hydrophobic pocket to stabilize the capsid and prevent the uncoating process required for viral replication [1.1.4, 1.2.1]. These inhibitors prevent the conformational transition from the 160S mature virion to the 135S expanded particle, effectively blocking viral entry [1.4.4]. Understanding the structure and mutations of Sabin 2 VP1 is essential for monitoring vaccine-derived poliovirus (VDPV) outbreaks, as specific amino acid changes in this protein, such as at residue 143, can lead to the reversion of the attenuated strain to a neurovirulent phenotype [1.3.1, 1.3.3]. This protein's role in both viral entry and immune recognition makes it a central focus for both preventative vaccine strategies and therapeutic antiviral interventions [1.1.3, 1.4.3].

Other names

Viral protein 11D proteinP1-1DSabin 2 VP1Capsid protein VP1

Capsid-binding inhibitors bind to a hydrophobic pocket within the VP1 protein, stabilizing the viral capsid to prevent the conformational changes necessary for genome uncoating and entry into the host cell.