Abstract:
: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.
journal_name
J Viroljournal_title
Journal of virologyauthors
Gnanakaran S,Lang D,Daniels M,Bhattacharya T,Derdeyn CA,Korber Bdoi
10.1128/JVI.01954-06subject
Has Abstractpub_date
2007-05-01 00:00:00pages
4886-91issue
9eissn
0022-538Xissn
1098-5514pii
JVI.01954-06journal_volume
81pub_type
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