Human rhinovirus capsid protein VP4 (VP4)

Human rhinovirus capsid protein VP4 is a small, highly conserved internal structural protein of the human rhinovirus (HRV), a member of the Picornaviridae family [6, 7]. It is post-translationally modified by N-terminal myristoylation, which is essential for its ability to anchor to and penetrate host cell membranes [13, 16]. During the viral entry process, conformational changes in the capsid—triggered by receptor binding or acidic pH—lead to the externalization and release of VP4 [2, 3]. Once released, VP4 molecules multimerize to form size-selective pores in the host cell membrane, facilitating the translocation of the viral RNA genome into the cytoplasm [1, 6]. This protein is a critical mediator of viral infectivity and serves as a primary target for antiviral interventions [12]. Therapeutic strategies include capsid-binding small molecules, such as pleconaril and pirodavir, which stabilize the viral shell to prevent VP4 release and subsequent uncoating [3, 4, 5]. Additionally, neutralizing antibodies targeting the conserved N-terminus of VP4 have shown promise in blocking pore formation across multiple rhinovirus serotypes [2, 10, 11].

Other names

VP4 proteinCapsid protein VP4Internal capsid protein VP4Myristoylated capsid protein VP4

Capsid stabilization to prevent VP4 release and viral uncoating; inhibition of membrane pore formation by neutralizing antibodies; inhibition of N-myristoylation to prevent membrane anchoring.