Mutational Analysis of the Assembly Domain of the HIV-1 Envelope Glycoprotein

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Abstract
The amino-terminal 129 amino acids of gp41 of the human immunodeficiency virus type 1 (HIV-1) envelope (Env) glycoprotein constitute the assembly domain required for efficient oligomer formation and stability. Point mutations in highly conserved structural features including cysteine residues, potential N-linked glycosylation sites, and a leucine zipper motif have been made in a soluble secreted form of Env (Envsec). No single point mutation had adverse effects on Env protein oligomerization. However, truncation of the C terminus of gp41 from 129 amino acids to 68 amino acids drastically reduced oligomerization efficiency, indicating that amino acids 68-129 are essential for assembly.