摘要
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.
Non-structural protein 1(NS1) of the influenza virus plays a crucial role in modulating the host immune response and facilitating virus replication.The formation of a homodimer or an oligomer is necessary for NS1 to exert its function efficiently.In the present study,the NS1 protein from the A/Shantou/602/06(H3N2) virus(herein abbreviated as NS32) was found to interact with NS1 from A/Shantou/169/06(H1N1),A/Chicken/Guangdong/1/05(H5N1) and A/Quail/Hong Kong/G1/97(H9N2)(abbreviated 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 subtypes/strains may be a common event during co-infection.
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)
Scientific Research Foundation of Shantou University Medical College(Grant No.LC0401)
211 Project of Guangdong Province(Mechanism and Prevention of Emerging Infectious Diseases)
