Corrigendum: Orf Virus 002 Protein Targets Ovine Protein S100A4 and Inhibits NF-κB Signaling
Year: 2017
Type: erratum
Abstract: Orf virus (ORFV), a member of Parapoxvirus, has evolved various strategies to modulate the immune responses of host cells. The ORFV-encoded protein ORFV002, a regulator factor, has been found to inhibit the acetylation of NF-kB-p65 by blocking phosphorylation of NF-kB-p65 at Ser276 and also to disrupt the binding of NF-kB-p65 and p300. To explore the mechanism by which ORFV002 regulates NF-kB signaling, the understanding of ORFV002 potential binding partners in host cells is critical. In this study, ovine S100 calcium binding protein A4 (S100A4), prolyl endopeptidase-like (PREPL) and NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 8 (NDUFA8) werefound to interact with ORFV002 based on the yeast two-hybrid (Y2H) assay using a cDNA library derived from primary ovine fetal turbinate cells (OFTu). GST pull-down and bidirectional co-immunoprecipitation assay results demonstrate that ORFV002 interacts with S100A4 directly. Following the pEGFP-ORFV002 (p002GFP) transfection, we found that cytoplasmic S100A4 translocates into the nucleus and co-localizes with ORFV002. Furthermore, the inhibitory effect of ORFV002 on NF-kB signaling was significantly restored by S100A4 knock-down phenotype, suggesting that ovine S100A4 participates in the ORFV002-mediated NF-kB signaling. These data demonstrate that ORFV002 inhibits the NF-kB activation through its interaction with S100A4 along with its nucleus translocation.
Source: Frontiers in Microbiology
Authors: Daxiang Chen, Zewei Zheng, Bin Xiao, Wei Li, Mingjian Long, Huiqin Chen, Ming Li, Daniel L. Rock, Wenbo Hao, Shuhong Luo
Language: English
Subfield: Virology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,801
OpenAlex ID: W2587084429