School of Life and Medical Sciences, University of Hertfordshire, Hatfield AL10 9AB, UK.
School of Life and Medical Sciences, University of Hertfordshire, Hatfield AL10 9AB, UK.
Virology. 2014 Apr;454-455:40-7. doi: 10.1016/j.virol.2014.01.023. Epub 2014 Feb 22.
The nucleoprotein (NP) of the influenza A virus encapsidates the viral RNA and participates in the infectious life cycle of the virus. The aims of this study were to find the degree of conservation of NP among all virus subtypes and hosts and to identify conserved binding sites, which may be utilised as potential drug target sites. The analysis of conservation based on 4430 amino acid sequences identified high conservation in known functional regions as well as novel highly conserved sites. Highly variable clusters identified on the surface of NP may be associated with adaptation to different hosts and avoidance of the host immune defence. Ligand binding potential overlapping with high conservation was found in the tail-loop binding site and near the putative RNA binding region. The results provide the basis for developing antivirals that may be universally effective and have a reduced potential to induce resistance through mutations.
甲型流感病毒的核蛋白（NP）包裹着病毒 RNA，并参与病毒的传染性生命周期。本研究的目的是确定 NP 在所有病毒亚型和宿主中的保守程度，并鉴定保守的结合位点，这些结合位点可能被用作潜在的药物靶标。基于 4430 个氨基酸序列的保守性分析，确定了已知功能区域以及新的高度保守的结合位点的高度保守性。NP 表面高度可变的簇可能与适应不同宿主和逃避宿主免疫防御有关。在尾环结合位点和假定的 RNA 结合区域附近发现了与高保守性重叠的配体结合潜力。研究结果为开发可能普遍有效的抗病毒药物提供了基础，这些药物通过突变诱导耐药的潜力可能降低。
