Abstract
Abstract Antiviral protein RSAD2 (radical S-adenosyl methionine domain-containing protein 2), also known as viperin, has been recognized as a highly inducible ER (endoplasmic reticulum) protein in response to a wide range of viruses and microbial products such as LPS and double-stranded RNA. However, the functions of RSAD2 other than its antiviral activity have remained unexplored. The present studies showed that RSAD2 mRNA and protein expression was highly induced by LPS treatment in both primary microglia and BV2 cells. To investigate the function of RSAD2 in activated microglia, BV2 cells were depleted RSAD2 by using a short hairpin RNA (shRNA) plasmid. TNF-α and IL-6 production in RSAD2 depleted cells was remarkably reduced after stimulation with LPS. However, mRNA expression of TNF-α and IL-6 did not reveal significant differences between RSAD2-shRNA transfected cells and cont-shRNA transfected cells after stimulation with LPS. The intracellular distribution and trafficking of TNF-α was demonstrated by immunofluorescence staining. Non-transfected control cells showed strong intracellular staining of TNF-α in a perinuclear Golgi complex after LPS treatment. However, depletion of RSAD2 inhibited the Golgi trafficking of TNF-α. These results suggest that RSAD2 play an important role in microglia activation, especially regulation of Golgi trafficking of secretary molecules such as TNF-α.
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