JCVI: In Vitro Inhibition of Vesicular Stomatitis Virus Replication by Purified Porcine Mx1 Protein Fused to HIV-1 Tat Protein Transduction Domain (PTD).
 
 
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Zhang XM, He DN, Zhou B, Pang R, Liu K, Zhao J, Chen PY

In Vitro Inhibition of Vesicular Stomatitis Virus Replication by Purified Porcine Mx1 Protein Fused to HIV-1 Tat Protein Transduction Domain (PTD).

Antiviral Research. 2013 May 28;

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Abstract

Vesicular stomatitis virus (VSV) is the causative agent of Vesicular Stomatitis (VS), a highly contagious fatal disease of human and pigs. Few effective anti viral drugs are currently available against VSV infection. Mx proteins are interferon (IFN)-induced dynamin-like GTPases present in all vertebrates with a range of anti viral activities. Previous studies have shown that the transfected cell lines expressing either pocine Mx1 or human MxA acquired a high degree of resistance to VSV. To explore the feasibility of taking porcine Mx1 protein expressed in E.coli as an anti viral agent, we applied the pCold system to express this fusion protein(PTD-poMx1), which consisted of an N-terminal HIV-1 Tat protein transduction domain (PTD) and the full-length porcine Mx1, and investigated its effects on the replication of VSV in Vero cells. The results demonstrated that the purified PTD-poMx1 fusion proteins could transduct into cells after incubated for 5h and had no cytotoxic. Furthermore, plaque reduction assay, determination of TCID50, real-time PCR and Western blot analyses were carried out to confirm the anti viral activity of purified fusion proteins in VSV-infected Vero cells. Altogether, these data suggested that PTD-poMx1 fusion proteins might be applicable to inhibit VSV replication as a novel anti viral therapeutic agent.