Human T-cell leukemia virus 1 envelope glycoprotein gp46 (gp46)

Human T-cell leukemia virus 1 envelope glycoprotein gp46 is the surface subunit (SU) of the HTLV-1 envelope complex, which is critical for the virus's ability to infect host T-cells. It is produced by the proteolytic cleavage of the gp62 precursor protein into gp46 and the transmembrane subunit gp21. The gp46 protein mediates viral attachment and entry by sequentially binding to host cell receptors, including heparan sulfate proteoglycans (HSPG), neuropilin-1 (NRP1), and glucose transporter-1 (GLUT-1). This binding triggers conformational changes that lead to the fusion of viral and cellular membranes, or syncytium formation between cells. As a primary target for the host's humoral immune response, gp46 is the focus of various therapeutic and prophylactic strategies. Neutralizing antibodies against gp46 can block viral entry, while others can induce antibody-dependent cellular cytotoxicity (ADCC) to eliminate infected cells. Although no drugs targeting gp46 are currently approved, experimental monoclonal antibodies like hu-LAT-27 and novel approaches such as near-infrared photoimmuno-antimicrobial strategy (NIR-PIAS) are being developed to treat HTLV-1-associated diseases, including adult T-cell leukemia/lymphoma (ATL) and HTLV-1-associated myelopathy (HAM/TSP).

Other names

HTLV-1 surface subunitHTLV-1 SUHTLV-1 Env SUgp46HTLV-1 envelope surface glycoprotein

Neutralization of viral entry, induction of antibody-dependent cellular cytotoxicity (ADCC), and inhibition of syncytium formation by blocking receptor interactions with HSPG, NRP1, and GLUT-1.