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Background The C-terminal tail (CTT) of HIV-1 envelope transmembrane protein has recently been the subject of an increasing number of studies to determine its role in the architecture of the HIV virion and in virus replication. Published studies from our lab have previously demonstrated that the lentivirus lytic peptides (LLP) domains contained in the CTT present highly characteristic and conserved physicochemical and structural properties, including a highly preferential incorporation of arginine over lysine at conserved sites.

The C-terminal tail of HIV-1 envelope: a unique role for conserved LLP arginines in Env functional properties