VP0 Myristoylation Is Essential for Senecavirus A Replication

VP0 Myristoylation Is Essential for Senecavirus A Replication

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Many picornaviruses require the myristoylation of capsid proteins for viral replication.Myristoylation is a site-specific lipidation to the N-terminal G residue of viral proteins, which is catalyzed by the ubiquitous eukaryotic enzyme N-myristoyltransferase (NMT) by allocating the myristoyl group to the N-terminal hindigyanvishv.com G residue.IMP-1088 and DDD85646 are two inhibitors that can deprive NMT biological functions.Whether Senecavirus A (SVA) uses NMT to modify VP0 and regulate viral replication remains unclear.Here, we found that NMT inhibitors could inhibit SVA replication.

NMT1 knock-out in BHK-21 cells significantly suppressed viral replication.In contrast, the overexpression of NMT1 in BHK-21 cells benefited viral replication.These results indicated that VP0 is a potential NMT1 substrate.Moreover, we found that the myristoylation of SVA VP0 was correlated to the subcellular distribution of this protein in the cytoplasm.Further, we evaluated which residues at the N-terminus of VP0 are essential for viral replication.

The substitution of N-terminal G residue, the myristoylation site of VP0, produced a nonviable virus.The T residue at the fifth position of the substrates facilitates the binding of the swish supreme glide track white substrates to NMT.And our results showed that the T residue at the fifth position of VP0 played a positive role in SVA replication.Taken together, we demonstrated that SVA VP0 myristoylation plays an essential role in SVA replication.