Key result
Cellular vimentin interacts with foot-and-mouth disease virus nonstructural protein 3A, and overexpression of vimentin significantly suppresses viral replication.
Why the study?
To further understand the role of nonstructural protein 3A during foot-and-mouth disease virus infection, identification of interacting host cell factors was needed.
The interaction between cellular vimentin and FMDV 3A is critical for viral replication, offering a potential target for novel antiviral strategies.
Vimentin-FMDV 3A interaction impairs replication; hypothesis-generating for host-targeted antivirals pending in vivo validation.
Foot-and-mouth disease virus (FMDV) nonstructural protein 3A plays important roles in virus replication, host range, and virulence. To further understand the role of 3A during FMDV infection, identification of host cell factors that interact with FMDV 3A is needed. Here, we found that vimentin is a direct binding partner of FMDV 3A, and manipulation of vimentin has a negative effect on virus replication. We also demonstrated that amino acid residues 15 to 21 at the N-terminal region of the FMDV 3A are responsible for the interaction between 3A and vimentin and that the 3A-vimentin interaction is critical for viral replication since the full-length cDNA clone harboring mutations in 3A, which were disrupt 3A-vimentin reactivity, could not produce viable virus progeny. This study provides information that not only provides us a better understanding of the mechanism of FMDV replication but also helps in the development of novel antiviral strategies in the future.
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Ma et al. (2020) studied Foot-and-mouth disease virus (FMDV) infection. Vimentin manipulation (overexpression or knockdown) vs. Control (empty vector or non-targeting siRNA) was evaluated on Viral replication (viral RNA, protein levels, and virus titer). Cellular vimentin interacts with foot-and-mouth disease virus nonstructural protein 3A, and overexpression of vimentin significantly suppresses viral replication.
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