Yellow fever virus structural polyprotein (C-prM-E) (YFV structural proteins)

The Yellow fever virus (YFV) structural proteins—comprising the Capsid (C), precursor Membrane (prM), and Envelope (E) proteins—are essential components of the viral particle and primary targets for the host immune response [1]. The C protein facilitates the assembly of the nucleocapsid by packaging the viral RNA, while the prM protein acts as a chaperone to prevent the E protein from undergoing premature fusion during virus maturation [1, 4]. The E protein is the most significant therapeutic target as it mediates viral attachment to host cell receptors and subsequent membrane fusion within endocytic vesicles [4]. The highly successful 17D live-attenuated vaccine works by inducing long-lasting neutralizing antibodies specifically against the E protein [2, 3]. While no specific small-molecule antivirals are currently approved to target these proteins, they remain the focus of research into entry inhibitors and next-generation vaccine platforms [4, 5]. Understanding the structural transitions of these proteins is crucial for addressing safety concerns like vaccine-associated viscerotropic disease and for developing treatments for this severe hemorrhagic fever [2, 5].

Other names

YFV C-prM-EYellow fever virus envelope proteinYellow fever virus capsid proteinYellow fever virus membrane proteinYFV structural proteins

Induction of neutralizing antibodies that bind to the Envelope (E) protein to prevent viral attachment and pH-dependent membrane fusion with host cell membranes [2, 4].