Respiratory syncytial virus small hydrophobic protein (RSV SH) (RSV SH)

The Respiratory Syncytial Virus (RSV) small hydrophobic (SH) protein is a 64-65 amino acid type II transmembrane protein that functions as a viroporin, forming pentameric ion channels in host cell membranes [UniProt P03425, Gan et al., 2012]. While the SH protein is not essential for viral entry or replication in vitro, it significantly enhances viral fitness and pathogenesis in vivo by modulating the host immune response [Schepens et al., 2014, Fuentes et al., 2007]. Specifically, it has been shown to inhibit TNF-alpha-induced apoptosis and interfere with signaling pathways, thereby facilitating viral persistence [Fuentes et al., 2007]. The extracellular domain of the protein, termed SHe, is highly conserved across different RSV strains and is the primary epitope for vaccine-induced antibodies [Schepens et al., 2014]. Unlike antibodies against the RSV F or G proteins, anti-SHe antibodies do not neutralize the virus directly; instead, they mediate protection by triggering antibody-dependent cellular cytotoxicity (ADCC) to eliminate infected cells [Schepens et al., 2014]. This unique mechanism of action makes the SH protein a promising candidate for inclusion in universal RSV vaccines, providing a layer of protection that is less susceptible to the antigenic drift seen in other surface proteins [Schepens et al., 2014].

Other names

Small hydrophobic proteinSH proteinViroporin SHSHe epitope

Induction of antibodies targeting the extracellular domain (SHe) to facilitate antibody-dependent cellular cytotoxicity (ADCC) against infected cells [Schepens et al., 2014].