tailieunhanh - Báo cáo y học: "Interaction of mumps virus V protein variants with STAT1-STAT2 heterodimer: experimental and theoretical studies"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Interaction of mumps virus V protein variants with STAT1-STAT2 heterodimer: experimental and theoretical studies | Rosas-Murrieta et al. Virology Journal 2010 7 263 http content 7 1 263 VIROLOGY JOURNAL RESEARCH Open Access Interaction of mumps virus V protein variants with STAT1-STAT2 heterodimer experimental and theoretical studies Nora H Rosas-Murrieta 1 Irma Herrera-Camacho1 Helen Palma-Ocampo1 Gerardo Santos-Lopez2 Julio Reyes-Leyva2 Abstract Background Mumps virus V protein has the ability to inhibit the interferon-mediated antiviral response by inducing degradation of STAT proteins. Two virus variants purified from Urabe AM9 mumps virus vaccine differ in their replication and transcription efficiency in cells primed with interferon. Virus susceptibility to IFN was associated with insertion of a non-coded glycine at position 156 in the V protein VGly of one virus variant whereas resistance to IFN was associated with preservation of wild-type phenotype in the V protein VWT of the other variant. Results VWT and VGly variants of mumps virus were cloned and sequenced from Urabe AM9 vaccine strain. VGly differs from VWT protein because it possesses an amino acid change Gln103Pro Pro103 and the Gly156 insertion. The effect of V protein variants on components of the interferon-stimulated gene factor 3 ISGF3 STAT1 and STAT2 proteins were experimentally tested in cervical carcinoma cell lines. Expression of VWT protein decreased STAT1 phosphorylation whereas VGly had no inhibitory effect on either STAT1 or STAT2 phosphorylation. For theoretical analysis of the interaction between V proteins and STAT proteins 3D structural models of VWT and VGly were predicted by comparing with simian virus 5 SV5 V protein structure in complex with STAT1-STAT2 heterodimer. In silico analysis showed that VWT-STAT1-STAT2 complex occurs through the V protein Trp-motif W174 W178 W189 and Glu95 residue close to the Arg409 and Lys415 of the nuclear localization signal NLS of STAT2 Ippi inn pynncprl CTAT1 I VC rpcirli IPC rk85 k87 k296 k413 k525 k679 k685 A hinh prp Cl iccpntihlp tn .