Respiratory syncytial virus small hydrophobic protein extracellular domain (SHe) (SHe)

The Respiratory syncytial virus small hydrophobic protein extracellular domain (SHe) is the highly conserved C-terminal ectodomain of the viral small hydrophobic (SH) protein. While the full-length SH protein functions primarily as a viroporin that permeabilizes host membranes and blocks TNF-alpha-mediated apoptosis to facilitate viral replication, the SHe domain is specifically targeted for its role as a stable antigen exposed on the surface of infected cells. Unlike the RSV F and G proteins, which are the primary targets for neutralizing antibodies, SHe is remarkably conserved across both RSV A and B subgroups, offering potential for a universal vaccine approach. Antibodies targeting SHe do not neutralize the virus particles directly; instead, they provide protection by triggering the destruction of infected cells via Fc-mediated effector functions, such as antibody-dependent cellular cytotoxicity (ADCC). This mechanism effectively reduces viral replication and shedding, making SHe a promising candidate for next-generation RSV vaccines and immunotherapies intended to provide broad-spectrum protection against varying viral strains.

Other names

RSV SHe antigenSmall hydrophobic protein ectodomainRespiratory syncytial virus SH protein extracellular domainRSV SH C-terminal domainSmall hydrophobic protein (SH) extracellular domain

Induction of antibody-dependent cellular cytotoxicity (ADCC) and antibody-dependent cellular phagocytosis (ADCP) to clear RSV-infected host cells.