Structural comparison of typical and atypical E2 pestivirus glycoproteins

Hazel Aitkenhead; Christiane Riedel; NathanChristiane Cowieson; Hans Tillmann Rümenapf; David I. Stuart; Kamel El Omari

doi:10.1016/j.str.2023.12.003

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Title (eng)

Structural comparison of typical and atypical E2 pestivirus glycoproteins

Author

Hazel Aitkenhead

Christiane Riedel

NathanChristiane Cowieson

Hans Tillmann Rümenapf

University of Veterinary Medicine Vienna

David I. Stuart

Kamel El Omari

Abstract (eng)

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.

Keywords (eng)

Viral Diarrhea VirusSwine-Fever VirusPutative Fusion PeptideEntryPHTaxonomyReceptorFamilyOccursCells

Type (eng)

journal article

Language

[eng]

Persistent identifier

https://phaidra.vetmeduni.ac.at/o:4235

DOI

10.1016/j.str.2023.12.003

Is in series

Title (eng)