Molecular characterization of the porcine S100A6 gene and analysis of its expression in pigs infected with highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV)

Abstract

Our previous microarray study revealed that S100A6 was significantly upregulated in porcine alveolar macrophages (PAMs) infected with highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV). In the present study, we cloned both cDNA and genomic DNA sequences of the gene. Transient transfection indicated that the porcine S100A6 protein was located in the nucleus and cytoplasm. Reverse transcription polymerase chain reaction (RT-PCR) revealed that the porcine S100A6 gene was highly expressed in the kidney and subcutaneous fat. Polyinosinic-polycytidylic acid [poly (I:C)] induced porcine S100A6 gene expression in PK-15 cells. Quantitative real-time PCR (Q-PCR) analysis further showed that the porcine S100A6 gene was upregulated in different cells and tissues of Tongcheng pigs infected with HP-PRRSV. Chromosome walking obtained the porcine S100A6 promoter region and then luciferase reporter assays confirmed its regulatory activities. We observed a putative NF-κB binding site in the core promoter region, which may explain the upregulation of porcine S100A6 in response to PRRSV. Transfection of NF-κB (p65 subunit) intensely induced the promoter activity of the porcine S100A6 gene, while an NF-κB inhibitor, pyrrolidine dithiocarbamate (PDTC), inhibited this activity. Furthermore, compared to its wild type, the promoter activity was significantly reduced when it contained a mutant NF-κB binding site. All these results provide a solid foundation to further investigate how S100A6 is involved in PRRSV infection.

Whole‐genome sequencing reveals breed‐differential CNVs between Tongcheng and Large White pigs

“…1c). These CNVs can be inferred as the results of domestication and are in accordance with the different phenotypic features with regard to reproductive traits, carcass traits, coat color, disease resistance and behavior between TC pigs and LW pigs (Wang et al 2015a;Zhou et al 2015;Liang et al 2017). In particular, the CNV overlapping with the KIT gene in the pigmentation GO term had different copy numbers in the TC (two copies) pigs and LW (four copies) pigs, and differential expression level in the RNA-seq data, which was consistent with the two-ended black coat in TC and the white coat in LW (Fig.…”

“…Large differences in terms of growth, carcass properties, reproduction, disease resistance and coat color are observed between Tongcheng (TC) pigs (a Chinese native breed) and Large White (LW) pigs (Zhou et al 2015;Liang et al 2017). However, little is known about the genetic basis underlying their phenotypic differences.…”

Toxoplasma gondii SAG1 targeting host cell S100A6 for parasite invasion and host immunity

“…Extracellular role of S100A6 might be exerted through its binding to the transmembrane receptor for advanced glycation end products (RAGE) for signal transduction ( Leclerc et al., 2007 ). In porcine alveolar macrophages infected with highly pathogenic porcine reproductive and respiratory syndrome virus or Haemophilus parasuis , the expression of S100A6 was significantly upregulated ( Wang et al., 2012 ; Zhou et al., 2015 ). Similarly, we found the protein level of S100A6 was highly co-related to T. gondii infection efficiency that a higher level of S100A6 protein resulted in a higher infection rate, and a lower level of S100A6 resulted in a lower infection rate ( Figures 4 and 5 ).…”

S100A9 regulates porcine reproductive and respiratory syndrome virus replication by interacting with the viral nucleocapsid protein

“…A recent study revealed that some DAMPs are also involved in the regulation of PRRSV replication. For example, HP-PRRSV infection promotes S100A6 expression in PAMs, which is related to the activity of NF-κB activation by HP-PRRSV (Zhou et al, 2015). Additionally, the inhibition of endogenous HSP70 and HSP90 can attenuate PRRSV replication Gao et al, 2014); however, there are few reports investigating the role of S100A9 in viral infection.…”