Clade-specific differences between human immunodeficiency virus type 1 clades B and C: diversity and correlations in C3-V4 regions of gp120.
Current knowledge of human immunodeficiency virus type 1 envelope (Env) glycoprotein structure and function is based on studies of clade B viruses. We present evidence of sequence and structural differences in viral glycoprotein gp120 between clades B and C. In clade C, the C3 region alpha2-helix exhibits high sequence entropy at the polar face but maintains its amphipathicity, whereas in clade B it accommodates hydrophobic residues. The V4 hypervariable domain in clade C is shorter than that in clade B. Generally, shorter V4 loops are incompatible with a glycine occurring in the alpha2-helix in clade C, an intriguing association that could be exploited to inform Env immunogen design.
Gnanakaran
S
S
Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Lang
Dorothy
D
Daniels
Marcus
M
Bhattacharya
Tanmoy
T
Derdeyn
Cynthia A
CA
Korber
Bette
B
D014644:Genetic Variation; D015699:HIV Envelope Protein gp120 / Q000737:chemistry*; D015497:HIV-1 / Q000145:classification* / Q000235:genetics*; D008958:Models, Molecular; D010802:Phylogeny; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D015699:HIV Envelope Protein gp120