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The Human T-cell leukemia virus type 2 (HTLV-2) envelope glycoprotein gp46 is the surface (SU) subunit of the viral envelope complex, which is essential for the virus to infect host cells (UniProt: P03382). It mediates the initial attachment to the host cell by binding to specific receptors, most notably the glucose transporter 1 (GLUT1) (PubMed: 15140982). The conserved central region of gp46, particularly the domain spanning residues 160 to 200, is highly immunogenic and remains stable across different viral isolates (PubMed: 1722486). This specific region is a primary target for the host's neutralizing antibody response and is frequently utilized in diagnostic assays to distinguish HTLV-2 from the closely related HTLV-1 (PubMed: 8380611). Although HTLV-2 is generally considered less pathogenic than HTLV-1, gp46 is a critical focus for the development of vaccines and therapeutic antibodies aimed at preventing viral transmission and entry. Currently, there are no FDA-approved drugs that specifically target this protein, but research continues into entry inhibitors that could block the gp46-receptor interaction.
Viral entry inhibition
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