The Identification Of ABHD16A As A Depalmitoylase Of IFITM Protein

Interferon-induced transmembrane proteins(IFITMs)are a class of small molecular transmembrane proteins induced by Type Ⅰ interferon(IFN).Earlier studies have confirmed that IFITMs have broad-spectrum antiviral capabilities and are the first line of defensing against multiple viruses.Our laboratory confirmed that the transmembrane protein induced by porcine interferon(sIFITM1)had the effect of inhibiting Japanese encephalitis virus(JEV),and its palmitoylation sites were necessary for sIFITM1 to resist JEV.α/β hydrolase domain containing 16A(ABHD16A)is a typical metabolic serinase,which is mainly located in the major histocompatibility complex(MHC)Ⅲgene cluster.It is speculated that it may be related to immune and participates in the palmitoylation cycles.Early stage of our laboratory confirmed that human or pig ABHD16A interacts with IFITMs through yeast two-hybrid assay.This study used a new type of palmitoylation detection method Acyl-PEGyl exchange gel-shift(APEGS)and mutant construction,through plasmid transfection and gene knockout cell lines,to confirm that sIFITM1 has three palmitoylation sites and AHBD16A has the activity of depalmitoylase target IFITMs.Then,laser confocal microscopy technology confirmed that s ABHD16A regulates the subcellular localization of sIFITM1.Finally,quantitative RT-PCR was used to confirm the ability of ABHD16A to impact the capability of IFITMs against Japanese encephalitis virus.It is speculated that ABHD16A may negatively regulate the antiviral ability of IFITMs by affecting the palmitoylation cycle of IFITMs and affecting the positioning of IFITMs.