期刊
VIROLOGY JOURNAL
卷 8, 期 -, 页码 -出版社
BMC
DOI: 10.1186/1743-422X-8-298
关键词
NS1; PSD-95; influenza virus; nitric oxide; neurons
类别
资金
- National Natural Science Foundation of China [81001322, 30972766]
- Guangdong Natural Science Foundation [9451503102003499]
- Specialized Research Fund for the Doctoral Program of Higher Education [20094402110004]
- State Key Lab of Agriculture Microbiology Open Foundation [AML200910]
- Shantou University Medical College Research Foundation
- 211 Project of Guangdong Province (Mechanism and Prevention of Emerging infectious Diseases)
Background: The NS1 protein of influenza A virus is able to bind with many proteins that affect cellular signal transduction and protein synthesis in infected cells. The NS1 protein consists of approximately 230 amino acids and the last 4 amino acids of the NS1 C-terminal form a PDZ binding motif. Postsynaptic Density Protein-95 (PSD-95), which is mainly expressed in neurons, has 3 PDZ domains. We hypothesise that NS1 binds to PSD-95, and this binding is able to affect neuronal function. Result: We conducted a yeast two-hybrid analysis, GST-pull down assays and co-immunoprecipitations to detect the interaction between NS1 and PSD-95. The results showed that NS1 of avian influenza virus H5N1 (A/chicken/Guangdong/1/2005) is able to bind to PSD-95, whereas NS1 of human influenza virus H1N1 (A/Shantou/169/2006) is unable to do so. The results also revealed that NS1 of H5N1 significantly reduces the production of nitric oxide (NO) in rat hippocampal neurons. Conclusion: In summary, our study indicates that NS1 of influenza A virus can bind with neuronal PSD-95, and the avian H5N1 and human H1N1 influenza A viruses possess distinct binding properties.
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