Why the study?
Topological and structural data were required for a better understanding of the molecular interactions underlying pestiviral NS2 autoprotease activity and its temporal regulation.
Determination of the minimal NS2-protease domain and membrane topology provides a foundation for future structural studies of the pestiviral NS2 autoprotease complex.
Topology of minimal NS2 now mapped; leaves open functional validation and antiviral targeting.
Pestiviral NS2 is central to the regulation of RNA replication and virion morphogenesis via its autoprotease activity. This activity is temporally regulated by the cellular DNAJC14 as a cofactor: while free NS3 is required for RNA replication as a component of the viral replicase, only uncleaved NS2-3 supports virion morphogenesis. For a better understanding of the underlying molecular interactions, topological and structural data are required. The topology-based determination of the minimal NS2-protease domain in the present study will facilitate future attempts to determine the structure of this unusual protease cofactor complex. In the hepatitis C virus system, NS2 functions as a hub in virion morphogenesis by interacting with structural as well as non-structural proteins. Our knowledge of the membrane topology will significantly support future detailed interaction studies for pestiviral NS2.
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Walther et al. (2021) studied this question.
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