Envelope Glycoprotein D (gD) His Tag Protein, HSV-2 (strain 333)

HSV-2 (strain 333) Envelope Glycoprotein D (gD) His Tag Protein is a critical envelope glycoprotein on the surface of herpes simplex virus type 2, recombinantly expressed with a His-tag for convenient purification and detection. Structurally, gD is a type I transmembrane glycoprotein comprising an N-terminal immunoglobulin-like fold domain, a flexible hinge region, and a C-terminal hydrophobic anchor; the His-tag is typically fused at the C-terminus to preserve N-terminal receptor-binding activity. Functionally, gD serves as the "molecular key" for viral entry, specifically recognizing and binding host cell surface receptors (HVEM, nectin-1, or 3-OS HS) to trigger the gB/gH-gL-mediated membrane fusion cascade, while also representing the primary target for neutralizing antibodies. Clinically, it holds significant importance: as a specific antigen for HSV-2 infection diagnosis supporting serological testing; as the core candidate molecule for subunit vaccines, exemplified by GSK's Herpevac vaccine developed based on gD; and its epitope mapping provides structural foundations for therapeutic monoclonal antibodies and entry inhibitor design, carrying substantial translational value for controlling genital herpes and neonatal herpes infections.