Small hydrophobic protein ectodomain, human respiratory syncytial virus (SH protein (RSV))

The **small hydrophobic (SH) protein** of respiratory syncytial virus is a minor envelope protein, distinct from the major fusion (F) and attachment (G) glycoproteins of RSV. Structurally, the SH protein contains an ectodomain, a single transmembrane α-helix, and small cytoplasmic domains. The SH protein oligomerizes to form a pentameric channel (viroporin) in membranes, increasing membrane permeability and functioning as a nonselective cation channel[3][6]. It is postulated to modulate the host immune response by inhibiting TNF-α signaling through interference with NF-κB activation[5]. Unlike the F and G proteins, the SH protein is **not essential for virus entry or replication** in vitro and is often absent or at much lower abundance in budding viral filaments[4][6]. Despite this, SH proteins are conserved among pneumoviruses and may play a role in virus pathogenicity and immune evasion. There are currently no licensed drugs specifically targeting the SH protein, but it has been explored as a potential antiviral target due to its role in membrane permeability and immune modulation[5][6]. **Note:** This entry does not refer to a host (human) receptor, but rather to a viral protein expressed on the virion surface. The "ectodomain" refers to the external portion of the SH protein exposed on the virus surface, but the SH protein functions mainly as a viroporin (ion channel) rather than as a classic attachment or entry receptor[3][5][6].

Other names

SH proteinSmall hydrophobic glycoprotein (RSV SH)RSV SH protein

For potential drugs: viroporin inhibition, disruption of channel activity, immune modulation