Ross River virus envelope glycoproteins E1 and E2 (RRV E1/E2)

The Ross River virus (RRV) envelope glycoproteins E1 and E2 are the primary structural proteins on the surface of the RRV virion, an alphavirus responsible for epidemic polyarthritis (UniProt P0C0S1, P0C0S2). These proteins are organized into 80 trimeric spikes, each consisting of E1-E2 heterodimers, which are essential for the viral infection process. The E2 glycoprotein is responsible for receptor binding, specifically interacting with the host cell receptor Mxra8, while the E1 glycoprotein is a class II fusion protein that mediates the fusion of the viral and host endosomal membranes (Zhang et al., 2021, Nature). In inactivated virus preparations, these glycoproteins are the principal antigens that elicit a protective immune response, primarily through the induction of neutralizing antibodies (Holzer et al., 2011, Vaccine). Because they are the most accessible components of the virus to the host immune system, E1 and E2 are the primary targets for vaccine development and the focus of diagnostic assays. Neutralizing antibodies typically target the E2 protein to block attachment or the E1 protein to prevent the conformational changes required for fusion. Therapeutic research often focuses on stabilizing these proteins in their prefusion state to enhance the immunogenicity of vaccine candidates. Understanding the structural biology of the E1-E2 complex is vital for addressing the public health impact of RRV in endemic regions.

Other names

RRV E1/E2Ross River virus surface proteinsRRV envelope spikesRRV E1 proteinRRV E2 protein

Induction of neutralizing antibodies that block viral attachment and fusion