氨基酸取代对人类免疫缺陷病毒1型跨膜蛋白LLP-1肽段钙调蛋白结合及细胞溶解特性的影响
Effect of amino acid substitutions on calmodulin binding and cytolytic properties of the LLP-1 peptide segment of human immunodeficiency virus type 1 transmembrane protein.
作者信息
Tencza S B, Miller M A, Islam K, Mietzner T A, Montelaro R C
机构信息
Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pennsylvania 15261, USA.
出版信息
J Virol. 1995 Aug;69(8):5199-202. doi: 10.1128/JVI.69.8.5199-5202.1995.
Abstract
Previous studies have identified two highly basic amphipathic helical regions in the human immunodeficiency virus type 1 transmembrane protein that, in vitro, display both cytolytic and calmodulin-binding and -inhibitory properties that could contribute to cellular dysfunctions and cytopathogenesis during a persistent viral infection. In the current study, the structural specificity of the cytolytic and calmodulin-binding activities of the human immunodeficiency virus type 1 lentivirus lytic peptide (LLP-1) are examined with synthetic peptide homologs and analogs. The results of these studies demonstrate that even minor changes in LLP-1 amino acid content can markedly affect these properties, suggesting that sequence variation in these highly conserved LLP sequences may correlate with alterations in viral cytopathic properties.
摘要
先前的研究已在人类免疫缺陷病毒1型跨膜蛋白中鉴定出两个高度碱性的两亲性螺旋区域，在体外，它们表现出细胞溶解、钙调蛋白结合及抑制特性，这些特性可能在持续性病毒感染期间导致细胞功能障碍和细胞病变发生。在本研究中，利用合成肽同系物和类似物检测了人类免疫缺陷病毒1型慢病毒裂解肽（LLP-1）的细胞溶解和钙调蛋白结合活性的结构特异性。这些研究结果表明，即使LLP-1氨基酸含量发生微小变化也会显著影响这些特性，这表明这些高度保守的LLP序列中的序列变异可能与病毒细胞病变特性的改变相关。
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