Key result
X-ray structures of APPV and NRPV E2 proteins reveal that despite high structural divergence, both dimerize through their C-terminal domain and contain a solvent-exposed β-hairpin involved in host receptor binding.
Why the study?
Despite E2 being the main target for neutralizing antibodies and essential for attachment and fusion, the pestivirus viral entry mechanism and E2 structural diversity remain elusive.
The study provides structural insights into the pestivirus E2 mechanism of action, revealing a conserved β-hairpin involved in host receptor binding despite highly divergent structures.
Highlights conserved β-hairpin for pestivirus entry; leaves open therapeutic targeting in animals or humans.
Pestiviruses, within the family Flaviviridae, are economically important viruses of livestock. In recent years, new pestiviruses have been reported in domestic animals and non-cloven-hoofed animals. Among them, atypical porcine pestivirus (APPV) and Norway rat pestivirus (NRPV) have relatively little sequence conservation in their surface glycoprotein E2. Despite E2 being the main target for neutralizing antibodies and necessary for cell attachment and viral fusion, the mechanism of viral entry remains elusive. To gain further insights into the pestivirus E2 mechanism of action and to assess its diversity within the genus, we report X-ray structures of the pestivirus E2 proteins from APPV and NRPV. Despite the highly divergent structures, both are able to dimerize through their C-terminal domain and contain a solvent-exposed β-hairpin reported to be involved in host receptor binding. Functional analysis of this β-hairpin in the context of BVDV revealed its ability to rescue viral infectivity.
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Aitkenhead et al. (2024) studied Pestivirus infection. X-ray crystallography of pestivirus E2 proteins was evaluated on Structural and functional analysis of pestivirus E2 proteins. X-ray structures of APPV and NRPV E2 proteins reveal that despite high structural divergence, both dimerize through their C-terminal domain and contain a solvent-exposed β-hairpin involved in host receptor binding.
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