Non-structural protein 1 (NS1) of the influenza virus plays a crucial role in modulating the host immune response and facili- tating virus replication. The formation of a homodimer or an oligomer is necessary for NS...Non-structural protein 1 (NS1) of the influenza virus plays a crucial role in modulating the host immune response and facili- tating virus replication. The formation of a homodimer or an oligomer is necessary for NSI to exert its function efficiently. In the present study, the NS 1 protein from the A/Shantou/602/06(H3N2) virus (herein abbreviated as NS32) was found to interact with NS1 from A/Shantou/169/O6(H1N1), A/Chicken/Guangdong/1/05(HSN1) and A/Quail/Hong Kong/G1/97(H9N2) (abbre- viated as NS11, NS51 and NS92, respectively) viruses, although NS32 shares 17.4%-20.9% sequence diversity with NS11, NS51 and NS92. This indicates that the heterologous interactions between NS1 proteins from different influenza A virus sub- types/strains may be a common event during co-infection.展开更多
文摘声发射(acoustic emission,AE)检测就是利用采集和分析声发射现象所产生的信号从而实现对材料进行无损评价的技术,该技术具有实时监测并定位破坏源的能力但是由于检测过程中声发射源信号未知,因此评价检测可靠性的检测概率(probability of detection,POD)研究仍然是空白。进一步来说,在利用声发射监测损伤过程时,声发射波源直接决定其检测结果的可靠性,因此波源的检测概率可以成为量化声发射检测有效性的一个重要指标。为了确定声发射波源的检测概率,利用声子晶体(phononic crystals,PCs)的特性,通过部署声子晶体形成物理带隙,滤除噪声信号,从而获得铝合金试件在紧凑拉伸试验下由于疲劳裂缝活动而引起的声发射信号,最终确定声发射源的检测概率及其影响因素。结果表明,检测概率会随着疲劳裂缝扩展而提高,但裂缝长度达到一定值后开始下降,最终趋于一个平稳值,另外通过设置阈值和选择适当的滤波器,能有效提高检测概率,保证声发射评价结构损伤的有效性。该研究对声发射源识别和检测可靠性评价具有重要意义。
基金supported by the National Natural Science Foundation of China(Grant Nos.30972766,31170852,81001322,81172795,and 81072622)Specialized Research Fund for the Doctoral Program of Higher Education(Grant No.20094402110004)+1 种基金Scientific Research Foundation of Shantou University Medical College(Grant No.LC0401)211 Project of Guangdong Province(Mechanism and Prevention of Emerging Infectious Diseases)
文摘Non-structural protein 1 (NS1) of the influenza virus plays a crucial role in modulating the host immune response and facili- tating virus replication. The formation of a homodimer or an oligomer is necessary for NSI to exert its function efficiently. In the present study, the NS 1 protein from the A/Shantou/602/06(H3N2) virus (herein abbreviated as NS32) was found to interact with NS1 from A/Shantou/169/O6(H1N1), A/Chicken/Guangdong/1/05(HSN1) and A/Quail/Hong Kong/G1/97(H9N2) (abbre- viated as NS11, NS51 and NS92, respectively) viruses, although NS32 shares 17.4%-20.9% sequence diversity with NS11, NS51 and NS92. This indicates that the heterologous interactions between NS1 proteins from different influenza A virus sub- types/strains may be a common event during co-infection.