Deletions in the fifth alpha helix of HIV-1 matrix block virus release.
Deletions in the fifth alpha helix of HIV-1 matrix block virus release.
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DOI：
10.1016/j.virol.2014.08.017
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发表时间：
2014-11
期刊：
影响因子：
3.7
通讯作者：
Belshan, Michael
中科院分区：
文献类型：
--
作者：
Sanford, Bridget;Li, Yan;Maly, Connor J.;Madson, Christian J.;Chen, Han;Zhou, You;Belshan, Michael
HIV-1的基质(MA)蛋白是Gag结构蛋白的N端成分，在病毒复制的早期和晚期都是至关重要的。MA含有5个α-螺旋(α1-α5)。α5 N端小至3个氨基酸的缺失会损害病毒的释放。1个缺失突变体(MAΔ96-12 0)的电子显微镜显示，其颗粒被膜柄拴在细胞表面。免疫印迹结果表明，所有突变体都被完全加工，但缺失较大的突变体有可供选择的加工中间产物。与EM数据一致，MAΔ96-120保留了膜缔合和多聚化能力。该突变体的共表达抑制了野生型颗粒的释放。该区域的丙氨酸扫描突变不影响病毒的释放，尽管后代病毒粒子的感染性很弱。综上所述，这些数据表明，MA的α5的结构消融抑制了病毒的释放。
The Matrix (MA) protein of HIV-1 is the N-terminal component of the Gag structural protein and is critical for the early and late stages of viral replication. MA contains five α-helices (α1-α5). Deletions in the N-terminus of α5 as small as three amino acids impaired virus release. Electron microscopy of one deletion mutant (MAΔ96-120) showed that its particles were tethered to the surface of cells by membranous stalks. Immunoblots indicated all mutants were processed completely, but mutants with large deletions had alternative processing intermediates. Consistent with the EM data, MAΔ96-120 retained membrane association and multimerization capability. Co-expression of this mutant inhibited wild type particle release. Alanine scanning mutation in this region did not affect virus release, although the progeny virions were poorly infectious. Combined, these data demonstrate that structural ablation of the α5 of MA inhibits virus release.
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