Brasseur R, Cornet B, Burny A, Vandenbranden M, Ruysschaert J M
Laboratory of Macromolecules at Interfaces, Brussels, Belgium.
AIDS Res Hum Retroviruses. 1988 Apr;4(2):83-90. doi: 10.1089/aid.1988.4.83.
The complete amino-acid sequence of the gp160 polyprotein of HIV (strain WMJ1) has been analyzed by the Eisenberg procedure. The region surrounding the cleavage site between the gp120 and the gp41 subunit contains a receptor-like region immediately followed by a transmembrane-like region containing approximately 13 residues. These two regions are separated by the cleavage site between gp120 and gp41. Since the same arrangement exists in some paramyxoviruses (unpublished observation) and since the effective cleavage between a receptor-like region and the transmembrane-like region is required in paramyxoviruses to generate fusogenic segment (located at the N-terminal sequence of the transmembrane-like region), we have focused our analysis on the conformational properties of the N-terminal peptide segment of HIV gp41. This peptide segment, which consists of a helical structure according to Garnier prediction, was oriented at the lipid-water interface using a theoretical analysis method that we recently developed. Analysis of the transmembrane peptide determined by Eisenberg method shows that the helical segment orients itself in the lipid monolayer obliquely with respect to the lipid-water interface. Since this rather unusual orientation for a membrane segment of a protein is also found in the fusogenic peptide of the Newcastle Disease Virus (Virus Genes, in press) and seems to possess membrane destabilizing properties, it is in agreement with previous reports suggesting a fusogenic role for the N-terminal part of gp41.
已通过艾森伯格方法分析了HIV（WMJ1株）gp160多聚蛋白的完整氨基酸序列。gp120和gp41亚基之间的切割位点周围区域包含一个受体样区域，紧接着是一个跨膜样区域，该区域含有大约13个残基。这两个区域被gp120和gp41之间的切割位点隔开。由于在一些副粘病毒中也存在相同的排列方式（未发表的观察结果），并且由于副粘病毒中受体样区域和跨膜样区域之间的有效切割是产生融合片段（位于跨膜样区域的N端序列）所必需的，因此我们将分析重点放在了HIV gp41的N端肽段的构象特性上。根据加尼尔预测，该肽段由螺旋结构组成，我们使用最近开发的理论分析方法将其定位在脂质-水界面。通过艾森伯格方法确定的跨膜肽分析表明，螺旋段在脂质单层中相对于脂质-水界面倾斜排列。由于在新城疫病毒的融合肽中也发现了蛋白质膜段这种相当不寻常的取向（《病毒基因》，即将发表），并且似乎具有膜去稳定化特性，这与之前报道的gp41 N端部分具有融合作用一致。
