LAUSR.org creates dashboard-style pages of related content for over 1.5 million academic articles. Sign Up to like articles & get recommendations!

Sterile 20‐like kinase 3 promotes tick‐borne encephalitis virus assembly by interacting with NS2A and prM and enhancing the NS2A–NS4A association

Photo from wikipedia

Tick‐borne encephalitis virus (TBEV) is the causative agent of a potentially fatal neurological infection in humans. Investigating virus–host interaction is important for understanding the pathogenesis of TBEV and developing effective… Click to show full abstract

Tick‐borne encephalitis virus (TBEV) is the causative agent of a potentially fatal neurological infection in humans. Investigating virus–host interaction is important for understanding the pathogenesis of TBEV and developing effective antiviral drugs against this virus. Here, we report that mammalian ste20‐like kinase 3 (MST3) is involved in the regulation of TBEV infection. The knockdown or knockout of MST3, but not other mammalian ste20‐like kinase family members, inhibited TBEV replication. The knockdown of MST3 also significantly reduced TBEV replication in mouse primary astrocytes. Life cycle analysis indicated that MST3 remarkably impaired virion assembly efficiency and specific infectivity by respectively 59% and 95% in MST3‐knockout cells. We further found that MST3 interacts with the viral proteins NS2A and prM; and MST3 enhances the interaction of NS2A–NS4A. Thus, MST3‐NS2A complex plays a major role in recruiting prM–E heterodimers and NS4A and mediates the virion assembly. Additionally, we found that MST3 was biotinylated and combined with other proteins (e.g., ATG5, Sec24A, and SNX4) that are associated with the cellular membrane required for TBEV infection. Overall, our study revealed a novel function for MST3 in TBEV infection and identified as a novel host factor supporting TBEV assembly.

Keywords: borne encephalitis; like kinase; encephalitis virus; mst3; tick borne

Journal Title: Journal of Medical Virology
Year Published: 2023

Link to full text (if available)


Share on Social Media:                               Sign Up to like & get
recommendations!

Related content

More Information              News              Social Media              Video              Recommended



                Click one of the above tabs to view related content.