BST2 Protein, Cynomolgus (HEK293, His)

BST2 Protein, an IFN-induced antiviral host restriction factor, serves as a potent inhibitor of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Functioning as a direct physical tether, BST2 holds virions to the cell membrane, facilitating their linkage to each other. This unique mechanism restrains the release of virions, which can be internalized by endocytosis and subsequently degraded, or remain on the cell surface, limiting their spread as cell-free virions. Targeting viruses from various families, including retroviridae (e.g., HIV-1, MMTV, MLV), filoviridae (e.g., EBOV), arenaviridae (e.g., LASV), and rhabdoviridae (e.g., VSV), BST2 demonstrates broad antiviral activity. Beyond its role in viral restriction, BST2 also inhibits the cell surface proteolytic activity of MMP14, leading to decreased activation of MMP15 and consequent inhibition of cell growth and migration. Additionally, BST2 can stimulate signaling by LILRA4/ILT7, providing negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Furthermore, BST2 contributes to the organization of the subapical actin cytoskeleton in polarized epithelial cells. Structurally, BST2 forms a parallel homodimer that is disulfide-linked, and its dimerization is essential for its antiviral activity. The protein interacts with ARHGAP44, MMP14, and LILRA4/ILT7, revealing its involvement in diverse cellular processes and signaling pathways.