tetano
Editor, Senior Moderator
Virus Genes. 2012 Nov 28. [Epub ahead of print]
Interaction of avian influenza virus NS1 protein and nucleolar and coiled-body phosphoprotein 1.
Zhu C, Zheng F, Sun T, Duan Y, Cao J, Feng H, Shang L, Zhu Y, Liu H.
Source
Key Laboratory of Animal Resource and Epidemic Disease Prevention, Life Science School of Liaoning University, Shenyang, 110036, China.
Abstract
Nonstructural protein 1 (NS1) is a non-structural protein of avian influenza virus. It can interact with a variety of proteins of the host cells, enhancing the expression of viral proteins and changing the growth and metabolism of the host cells, thereby enhancing the virus' pathogenicity and virulence. To investigate whether there are more host proteins that can interact with NS1 during viral infection, T7-phage display system was used to screen human lung cell cDNA library for proteins that could interact with NS1. One positive and specific clone was obtained and identified as nucleolar and coiled-body phosphoprotein 1(NOLC1). The interaction between these two proteins was further demonstrated by His-pull-down and co-immunoprecipitation experiments. Co-expression of both proteins in HeLa cell showed that NS1 and NOLC1 were co-localized in the cell's nucleus. Gene truncation experiments revealed that the effector domain of NS1 was sufficient to interact with NOLC1. The results demonstrated a positive interaction between a viral NS1 and NOLC1 of the host cells, and provided a new target for drug screening.
PMID:
23188192
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23188192
Interaction of avian influenza virus NS1 protein and nucleolar and coiled-body phosphoprotein 1.
Zhu C, Zheng F, Sun T, Duan Y, Cao J, Feng H, Shang L, Zhu Y, Liu H.
Source
Key Laboratory of Animal Resource and Epidemic Disease Prevention, Life Science School of Liaoning University, Shenyang, 110036, China.
Abstract
Nonstructural protein 1 (NS1) is a non-structural protein of avian influenza virus. It can interact with a variety of proteins of the host cells, enhancing the expression of viral proteins and changing the growth and metabolism of the host cells, thereby enhancing the virus' pathogenicity and virulence. To investigate whether there are more host proteins that can interact with NS1 during viral infection, T7-phage display system was used to screen human lung cell cDNA library for proteins that could interact with NS1. One positive and specific clone was obtained and identified as nucleolar and coiled-body phosphoprotein 1(NOLC1). The interaction between these two proteins was further demonstrated by His-pull-down and co-immunoprecipitation experiments. Co-expression of both proteins in HeLa cell showed that NS1 and NOLC1 were co-localized in the cell's nucleus. Gene truncation experiments revealed that the effector domain of NS1 was sufficient to interact with NOLC1. The results demonstrated a positive interaction between a viral NS1 and NOLC1 of the host cells, and provided a new target for drug screening.
PMID:
23188192
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23188192