One of the routes by which HIV-1 is able to escape the immune response is by immunosuppression. The gp41 fusion protein of the HIV-1 envelope mediates virus entry by membrane fusion and also functions as an inhibitor of T cell activation. Here, we review the recent studies suggesting that some of the gp41 immunosuppressive processes are initiated by novel motifs, located within the hydrophobic regions of the protein. This indicates that the immunosuppressive process mediated by gp41 is much more complex than initially thought. Additionally, we propose a model illustrating the interactions and interferences of these regions with the T cell receptor complex.
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