Giuseppe
Emeritus
Interaction of influenza virus NS1 protein with growth arrest-specific protein 8 (BMC, abstract, edited)
[Source Full PDF Document: LINK. EDITED.]
Interaction of influenza virus NS1 protein with growth arrest-specific protein 8
Lixia Zhao 1, 2, Long Xu 1, Xiaowei Zhou 1, Qingyu Zhu 2, Zhixin Yang 1, Chuanfu Zhang 1, Xudong Zhu 1, Mengbin Yu 1,Yingying Zhang 1, Xinghui Zhao 2, Peitang Huang 1*
1Laboratory of protein engineering, Beijing Institute of Biotechnology, Beijing 100071, China
2State key laboratory of pathogen and biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China
* To whom correspondence should be addressed.
Tel: +86 10 6381 0272; Fax: +86 10 6381 0272; E-mail: h-pt@hotmail.com
Lixia Zhao and Long Xu are joint first authors. They contributed equally to this work.
Email
LZ - happylisa2008@yahoo.com.cn; LX - xu_long@126.com; XZ - amms832@126.com; QZ - qingyzh@yahoo.com.cn; ZY - yy_xiao@126.com; CZ - hnzcf@126.com; XZ - xd_zhu@263.net; MY - xinwen23@163.com; YZ - xray19@126.com; XZ - hao4work@yahoo.com.cn; PH - h-pt@hotmail.com
Abstract
NS1 protein is the only non-structural protein encoded by the influenza A virus, and it contributes significantly to disease pathogenesis by modulating many virus and host cell processes. A two-hybrid screen for proteins that interact with NS1 from influenza A yielded growth arrest-specific protein 8. Gas8 associated with NS1 in vitro and in vivo. Deletion analysis revealed that the N-terminal 260 amino acids of Gas8 were able to interact with NS1, and neither the RNA-binding domain nor the effector domain of NS1 was sufficient for the NS1 interaction. We also found that actin, myosin, and drebrin interact with Gas8. NS1 and β-actin proteins could be coimmunoprecipitated from extracts of transfected cells. Furthermore, actin and Gas8 co-localized at the plasma membrane. These results are discussed in relation to the possible functions of Gas8 protein and their relevance in influenza virus release.
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[Source Full PDF Document: LINK. EDITED.]
Interaction of influenza virus NS1 protein with growth arrest-specific protein 8
Lixia Zhao 1, 2, Long Xu 1, Xiaowei Zhou 1, Qingyu Zhu 2, Zhixin Yang 1, Chuanfu Zhang 1, Xudong Zhu 1, Mengbin Yu 1,Yingying Zhang 1, Xinghui Zhao 2, Peitang Huang 1*
1Laboratory of protein engineering, Beijing Institute of Biotechnology, Beijing 100071, China
2State key laboratory of pathogen and biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China
* To whom correspondence should be addressed.
Tel: +86 10 6381 0272; Fax: +86 10 6381 0272; E-mail: h-pt@hotmail.com
Lixia Zhao and Long Xu are joint first authors. They contributed equally to this work.
LZ - happylisa2008@yahoo.com.cn; LX - xu_long@126.com; XZ - amms832@126.com; QZ - qingyzh@yahoo.com.cn; ZY - yy_xiao@126.com; CZ - hnzcf@126.com; XZ - xd_zhu@263.net; MY - xinwen23@163.com; YZ - xray19@126.com; XZ - hao4work@yahoo.com.cn; PH - h-pt@hotmail.com
Abstract
NS1 protein is the only non-structural protein encoded by the influenza A virus, and it contributes significantly to disease pathogenesis by modulating many virus and host cell processes. A two-hybrid screen for proteins that interact with NS1 from influenza A yielded growth arrest-specific protein 8. Gas8 associated with NS1 in vitro and in vivo. Deletion analysis revealed that the N-terminal 260 amino acids of Gas8 were able to interact with NS1, and neither the RNA-binding domain nor the effector domain of NS1 was sufficient for the NS1 interaction. We also found that actin, myosin, and drebrin interact with Gas8. NS1 and β-actin proteins could be coimmunoprecipitated from extracts of transfected cells. Furthermore, actin and Gas8 co-localized at the plasma membrane. These results are discussed in relation to the possible functions of Gas8 protein and their relevance in influenza virus release.
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