Becker Y
Department of Molecular Virology, Faculty of Medicine, Hebrew University of Jerusalem, Israel.
Virus Genes. 1991 Oct;5(4):287-312. doi: 10.1007/BF00271529.
Analysis of human immunodeficiency virus-1 (HIV-1) gp160 amino acid sequences by computer programs that provide information on the possible conformation, hydrophilicity, and surface probability was used to identify possible functional domains. Amino acid domains that serve as signals for transfer of the polypeptide chain through the cell membrane were identified. Stop-transfer amino acid domains present in gp160 made possible the identification of the membrane anchorage hydrophobic amino acid sequence. The characterization of amino acid domains that serve as signals for proteolytic cleavage suggest that gp41 might be cleaved in a number of positions in the polypeptide chain, releasing parts of the carboxy-terminus amino acid sequence from that part of gp41 anchored in the cell membrane. The computer analysis deals with the mode of insertion of gp160 into the cell membrane by the cellular signal recognition protein system and subsequent processing of the gp160 to gp120 and gp41 (and subpeptides). The model for the positioning of these peptides is used to predict the organization of the processed envelope proteins in the viral envelope. The possible function of domains in gp120 and gp41 during the interaction with host cells during virus infection is discussed.
利用能提供有关可能构象、亲水性和表面可能性信息的计算机程序，对人类免疫缺陷病毒1型（HIV-1）gp160氨基酸序列进行分析，以识别可能的功能域。确定了作为多肽链穿过细胞膜转运信号的氨基酸域。gp160中存在的终止转运氨基酸域使得能够识别膜锚定疏水氨基酸序列。对作为蛋白水解切割信号的氨基酸域的表征表明，gp41可能在多肽链的多个位置被切割，从而从锚定在细胞膜中的gp41部分释放出羧基末端氨基酸序列的部分片段。计算机分析涉及gp160通过细胞信号识别蛋白系统插入细胞膜的方式以及随后gp160加工为gp120和gp41（以及亚肽）的过程。这些肽定位的模型用于预测加工后的包膜蛋白在病毒包膜中的组织方式。讨论了gp120和gp41中的结构域在病毒感染期间与宿主细胞相互作用过程中的可能功能。
