Gnanakaran S, Lang Dorothy, Daniels Marcus, Bhattacharya Tanmoy, Derdeyn Cynthia A, Korber Bette
Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
J Virol. 2007 May;81(9):4886-91. doi: 10.1128/JVI.01954-06. Epub 2006 Dec 13.
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.
目前对1型人类免疫缺陷病毒包膜(Env)糖蛋白结构和功能的了解基于B亚型病毒的研究。我们提供了B亚型和C亚型病毒糖蛋白gp120在序列和结构上存在差异的证据。在C亚型中,C3区域的α2螺旋在极性面表现出高序列熵,但保持其两亲性,而在B亚型中它容纳疏水残基。C亚型中的V4高变区比B亚型中的短。一般来说,较短的V4环与C亚型α2螺旋中出现的甘氨酸不兼容,这一有趣的关联可用于指导Env免疫原设计。