title: Mutational analysis of the assembly domain of the HIV-1 envelope glycoprotein.
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.
authors.affiliation: Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892.
authors.forename: P L
authors.initials: PL
authors.lastname: Earl
authors.forename: B
authors.initials: B
authors.lastname: Moss
mesh_terms: D000818:Animals; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D015686:Gene Products, env / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015700:HIV Envelope Protein gp41 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015497:HIV-1 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017354:Point Mutation; D014162:Transfection; D014616:Vaccinia virus
chemical_list: D015686:Gene Products, env; D015700:HIV Envelope Protein gp41