8pab
Structures of the ectodomains of Atypical porcine pestivirus solved by long wavelength sulphur SADStructures of the ectodomains of Atypical porcine pestivirus solved by long wavelength sulphur SAD
Structural highlights
FunctionA0A1B1M0D5_9FLAV Acts as a cofactor for the NS3 protease activity.[ARBA:ARBA00023576] Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Also plays a role in transcription regulation. Protects the incoming virus against IFN-induced effectors.[ARBA:ARBA00034097] Plays a role in the regulation of viral RNA replication.[ARBA:ARBA00023574] Publication Abstract from PubMedPestiviruses, 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 beta-hairpin reported to be involved in host receptor binding. Functional analysis of this beta-hairpin in the context of BVDV revealed its ability to rescue viral infectivity. Structural comparison of typical and atypical E2 pestivirus glycoproteins.,Aitkenhead H, Riedel C, Cowieson N, Rumenapf HT, Stuart DI, El Omari K Structure. 2024 Mar 7;32(3):273-281.e4. doi: 10.1016/j.str.2023.12.003. Epub 2024 , Jan 3. PMID:38176409[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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