Why the study?
Structural glycoprotein E2 is an important component of CSFV involved in virus-host interactions, prompting characterization of its interaction with host protein Torsin-1A.
Does disrupting the E2-Torsin-1A interaction prevent CSFV replication?
Does disrupting the E2-Torsin-1A interaction prevent CSFV replication?
Disrupting the interaction between CSFV glycoprotein E2 and host Torsin-1A is lethal to the virus, identifying a potential target for novel countermeasures.
Disrupting E2-Torsin-1A interaction attenuates CSFV; leaves open in vivo antiviral potential in swine.
Structural glycoprotein E2 is an important structural component of the CSFV particle. E2 is involved in several virus functions, particularly virus-host interactions. Here, we characterized the interaction between CSFV E2 and swine protein Torsin-1A during virus infection. The critical amino acid residue in E2 mediating the interaction with Torsin-1A was identified and the effect of disrupting the E2-Torsin-1A protein-protein interaction was studied using reverse genetics. It is shown that the amino acid substitution abrogating E2-Torsin-1A interaction constitutes a lethal mutation, demonstrating that this virus-host protein-protein interaction is a critical factor during CSFV replication. This highlights the potential importance of the E2-Torsin-1A protein-protein interaction during CSFV replication and provides a potential pathway toward blocking virus replication, an important step toward the potential development of novel virus countermeasures.
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Vuono et al. (2021) studied this question.
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