期刊
JOURNAL OF VIROLOGY
卷 81, 期 9, 页码 4886-4891出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01954-06
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资金
- NIAID NIH HHS [U01 AI067854, AI 067854, U19 AI067854, P01 AI 061734-01, P01 AI061734, R01 AI058706, R01 AI 58706] Funding Source: Medline
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 alpha 2-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 alpha 2-helix in clade C, an intriguing association that could be exploited to inform Env immunogen design.
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