Vaccinia virus surface antigens (VACV surface antigens)

Vaccinia virus surface antigens are a complex set of proteins embedded in the viral envelopes of the intracellular mature virus (IMV) and the extracellular enveloped virus (EEV) (Moss, B., 2012, PMID: 22233676). These proteins, such as L1, A27, B5, and A33, play critical roles in the viral life cycle, including host cell attachment, membrane fusion, and the efficient spread of the virus between cells (Schmidt, F. I., et al., 2012, PMID: 22933282). As the primary interface between the virus and the host immune system, these antigens are the principal targets for neutralizing antibodies and the basis for most orthopoxvirus vaccines, including those for smallpox and mpox (CDC, 2022). Therapeutic interventions often focus on these antigens; for instance, the antiviral drug tecovirimat inhibits the F13 protein (VP37) to prevent the wrapping of the virus in a secondary membrane, thereby blocking the formation of the EEV (Grosenbach, D. W., et al., 2018, PMID: 29972742). Consequently, these surface antigens are pivotal for both the pathogenesis of vaccinia-related infections and the development of medical countermeasures. Neutralizing antibodies directed against these antigens, particularly L1 and B5, are essential for protective immunity following vaccination (He, S., et al., 2007, PMID: 17507483). The structural diversity of these antigens allows the virus to utilize multiple pathways for entry and spread, making them challenging yet effective targets for broad-spectrum orthopoxvirus therapies.

Other names

Poxvirus surface proteinsVACV envelope proteinsVaccinia virus membrane proteinsOrthopoxvirus surface antigens

Inhibition of viral egress via VP37 (F13L) protein blockade and antibody-mediated neutralization of viral particles (Grosenbach, D. W., et al., 2018, PMID: 29972742; Moss, B., 2012, PMID: 22233676).