Foot-and-mouth disease virus VP1 G-H loop (FMDV VP1 G-H loop)

The Foot-and-mouth disease virus (FMDV) VP1 G-H loop is a highly mobile and solvent-exposed structural element located on the surface of the viral capsid (Logan et al., 1993). It is characterized by a highly conserved Arginine-Glycine-Aspartic acid (RGD) motif, which serves as the primary ligand for host cell integrin receptors, specifically alpha-v beta-6, facilitating viral attachment and subsequent entry (Jackson et al., 2003). In addition to its role in pathogenesis, the G-H loop is the most prominent immunodominant epitope on the FMDV particle, eliciting the production of potent neutralizing antibodies during infection or vaccination (DiMarchi et al., 1986). Due to its exposure, the loop is subject to significant selective pressure, leading to high sequence variability across the seven FMDV serotypes, which complicates the development of universal vaccines. Therapeutic strategies often focus on synthetic peptides or recombinant proteins mimicking this loop to induce protective immunity or using monoclonal antibodies to block the RGD-integrin interaction (Blanco et al., 2013). Because this loop is central to both viral infectivity and the host immune response, it remains the primary target for the design of next-generation FMDV vaccines.

Other names

VP1 G-H loopFMDV RGD loopMajor antigenic site 1 of FMDVVP1 loop epitope

Neutralization of viral infectivity by blocking the interaction between the viral RGD motif and host cell integrin receptors.