Poliovirus serotype 1 capsid protein (PV1 capsid protein)

Poliovirus serotype 1 capsid protein is the major structural component of the poliovirus type 1 virion. The capsid is composed of 60 copies each of four polypeptides—VP1, VP2, VP3, and VP4—arranged with icosahedral symmetry to form a protective shell around the viral RNA genome[2][5]. These proteins determine the virus’s antigenicity and mediate host cell recognition and entry by undergoing conformational changes after binding to the poliovirus receptor (CD155, also known as PVR)[3][5]. Mutations in capsid protein regions—especially in exposed loops—alter antigenic properties and may generate neutralization-resistant variants[1][2]. The VP1 protein, in particular, is involved in membrane penetration and uncoating of the genome. Viral assembly and particle stability rely on intricate interactions between N- and C-termini of the capsid subunits and their connecting loops[2][4]. Capsid proteins are targets for antiviral drug development, though no capsid-binding drugs are currently licensed for human use; experimental molecules like pleconaril bind within a hydrophobic pocket in VP1 to stabilize the capsid and prevent uncoating[6]. The proteins are immunodominant antigens, making them the focus of vaccine development and serological assays for monitoring immunity and infection[1][3][5][6].

Other names

Poliovirus type 1 capsid proteinPoliovirus capsid protein 1PV-1 capsid proteinVP1VP2VP3VP4 (subunit components)

Inhibition of viral uncoating, Inhibition of cell entry by stabilizing capsid or blocking conformational changes