Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein.
The N-terminal region of the envelope (env) transmembrane protein of human immunodeficiency virus type 1 (HIV-1) has a leucine zipper-like motif. This highly conserved zipper motif, which consists of a heptad repeat of leucine or isoleucine residues, has been suggested to play a role in HIV-1 env glycoprotein oligomerization. This hypothesis was tested by replacing the highly conserved leucine or isoleucine residues in the zipper motif with a strong alpha-helix breaker, proline. We report here that such substitutions did not abolish the ability of env protein to form oligomers, indicating that this highly conserved zipper motif does not have a crucial role in env protein oligomerization. However, the mutant viruses all showed impaired infectivity, suggesting that this conserved zipper motif can have an important role in the virus life cycle.
Department of Pediatrics, Harvard Medical School, Boston, Massachusetts.
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McIntosh
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D000595:Amino Acid Sequence; D001483:Base Sequence; D004252:DNA Mutational Analysis; D015700:HIV Envelope Protein gp41 / Q000235:genetics*; D015497:HIV-1 / Q000235:genetics*; D007532:Isoleucine / Q000235:genetics; D007930:Leucine / Q000235:genetics; D016350:Leucine Zippers / Q000235:genetics*; D008969:Molecular Sequence Data; D011392:Proline / Q000235:genetics; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D015700:HIV Envelope Protein gp41; D007532:Isoleucine; D011392:Proline; D007930:Leucine