Effects of mutations in hyperconserved regions of the extracellular glycoprotein of human immunodeficiency virus type 1 on receptor binding.
Sequence comparison of the human immunodeficiency virus type 1 and type 2 env genes revealed the presence of six linear regions in the extracellular glycoprotein that are highly conserved. To investigate the functional significance of these regions, we made short deletions in each and assayed the ability of the mutated proteins to bind CD4 antigen. Small deletions in four of the highly conserved regions drastically reduced receptor binding. Some deletions interfered with the maturation of the envelope glycoprotein, but maturation did not necessarily correlate with the ability to bind CD4 antigen.
Cordonnier
A
A
Unité d'Oncologie Virale (Centre National de la Recherche Scientifique, UA1157), Institut Pasteur, Paris, France.
Rivière
Y
Y
Montagnier
L
L
Emerman
M
M
D000595:Amino Acid Sequence; D006031:Glycosylation; D006678:HIV / Q000235:genetics*; D015699:HIV Envelope Protein gp120; D019302:HIV Envelope Protein gp160; D009154:Mutation; D015728:Receptors, HIV; D011991:Receptors, Virus / Q000378:metabolism*; D012191:Retroviridae Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D014616:Vaccinia virus / Q000235:genetics; D014759:Viral Envelope Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*
D015699:HIV Envelope Protein gp120; D019302:HIV Envelope Protein gp160; D015728:Receptors, HIV; D011991:Receptors, Virus; D012191:Retroviridae Proteins; D014759:Viral Envelope Proteins