Small hydrophobic protein ectodomain of Respiratory Syncytial Virus subgroup A (SHe)

The Small Hydrophobic (SH) protein of Respiratory Syncytial Virus (RSV) subgroup A is a 64-65 amino acid type II transmembrane protein that functions as a viroporin, forming pentameric ion channels in host cell membranes (Gan et al., 2012, Protein & Cell). While the SH protein is not essential for viral replication in vitro, it plays a critical role in vivo by modulating host immune responses, such as inhibiting Tumor Necrosis Factor-alpha (TNF-alpha) signaling to prevent early apoptosis of infected cells (Fuentes et al., 2007, Journal of Virology). The extracellular C-terminal domain, known as SHe, consists of approximately 23 amino acids and is highly conserved within RSV subgroup A (Schepens et al., 2014, Nature Communications). SHe has become a significant therapeutic target because it is expressed on the surface of infected cells but is relatively shielded from the immune system during natural infection. Experimental vaccines targeting SHe do not induce neutralizing antibodies but instead trigger antibody-dependent cellular cytotoxicity (ADCC), leading to the clearance of infected cells and reduced viral load (Schepens et al., 2011, EMBO Molecular Medicine). This target is particularly relevant for developing broad-spectrum RSV prophylaxis to prevent severe lower respiratory tract infections like bronchiolitis and pneumonia.

Other names

RSV SHeSmall hydrophobic protein ectodomainSH proteinRSV-A SH protein

Induction of antibody-dependent cellular cytotoxicity (ADCC) against RSV-infected cells and potential inhibition of viroporin-mediated ion channel function (Schepens et al., 2011, EMBO Molecular Medicine).