Hepatitis C virus structural proteins (Core, E1, E2) (HCV structural proteins)

The Hepatitis C virus (HCV) structural proteins consist of the Core protein and the envelope glycoproteins E1 and E2 (Source 1.2.1, 1.4.1). The Core protein is a highly conserved nucleocapsid protein that encapsulates the viral RNA genome and facilitates viral assembly by associating with host lipid droplets and non-structural proteins (Source 1.3.1, 1.4.3). E1 and E2 form a non-covalent heterodimer on the viral surface, mediating attachment to host receptors such as CD81 and SR-BI and driving the fusion of the viral envelope with the host cell membrane (Source 1.1.2, 1.2.2). These proteins are the primary targets for neutralizing antibodies and are central to vaccine development efforts (Source 1.2.3, 1.5.4). While current direct-acting antivirals (DAAs) primarily target non-structural proteins like NS3/4A, NS5A, and NS5B, the structural proteins are being explored as targets for entry inhibitors and assembly disruptors to address therapeutic gaps and prevent reinfection (Source 1.3.2, 1.5.1). Experimental therapies include broadly neutralizing antibodies (e.g., AR4A, AR5A), entry inhibitors (e.g., Flunarizine), and small molecules that disrupt Core dimerization (Source 1.1.2, 1.2.1, 1.3.1).

Other names

Hepatitis C virus envelope proteinsHepatitis C virus capsid proteinE1/E2 glycoprotein complexHepatitis C virus nucleocapsid proteinHCV Core protein

The mechanism of action for drugs targeting HCV structural proteins involves the inhibition of viral entry by blocking the interaction between the E2 glycoprotein and host receptors like CD81, the inhibition of viral-host membrane fusion, and the disruption of viral assembly by preventing Core protein dimerization and nucleocapsid formation (Source 1.1.3, 1.2.1, 1.3.1).