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In vitro inhibition of vesicular stomatitis virus replication by purified porcine Mx1 protein fused to HIV-1 Tat protein transduction domain (PTD).

Antiviral Res.. 2013-08;  99(2):149-57
Zhang XM, He DN, Zhou B, Pang R, Liu K, Zhao J, Chen PY. Key Laboratory of Animal Diseases Diagnosis and Immunology, Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095, China
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摘要

Vesicular stomatitis virus (VSV) is the causative agent of Vesicular stomatitis (VS), a highly contagious fatal disease of human and pigs. Few effective antiviral drugs are currently available against VSV infection. Mx proteins are interferon (IFN)-induced dynamin-like GTPases present in all vertebrates with a range of antiviral activities. Previous studies have shown that the transfected cell lines expressing either porcine Mx1 or human MxA acquired a high degree of resistance to VSV. To explore the feasibility of taking porcine Mx1 protein expressed in Escherichia coli as an antiviral agent, we applied the pCold system to express this fusion protein (PTD-poMx1), which consisted of an N-terminal HIV-1 Tat prot... More

关键词

Vesicular stomatitis virus (VSV); Porcine Mx1 (poMx1); Protein transduction domain (PTD); Antiviral activity