8PUV

Trimeric prM/E spike of Tick-borne encephalitis virus immature particle

Summary for 8PUV

• Entry DOI: 10.2210/pdb8puv/pdb
• EMDB information: 17947
• Descriptor: Envelope protein E, Protein prM, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: immature particle, tick-borne, flavivirus, spike trimer, virus
• Biological source: Tick-borne encephalitis virus; More
• Total number of polymer chains: 6
• Total formula weight: 215610.53

Authors

Fuzik, T.,Plevka, P.,Smerdova, L.,Novacek, J. (deposition date: 2023-07-17, release date: 2024-07-17, Last modification date: 2024-10-23)

Primary citation

Anastasina, M.,Fuzik, T.,Domanska, A.,Pulkkinen, L.I.A.,Smerdova, L.,Formanova, P.P.,Strakova, P.,Novacek, J.,Ruzek, D.,Plevka, P.,Butcher, S.J.
The structure of immature tick-borne encephalitis virus supports the collapse model of flavivirus maturation.
Sci Adv, 10:eadl1888-eadl1888, 2024

PubMed Abstract: We present structures of three immature tick-borne encephalitis virus (TBEV) isolates. Our atomic models of the major viral components, the E and prM proteins, indicate that the pr domains of prM have a critical role in holding the heterohexameric prM3E3 spikes in a metastable conformation. Destabilization of the prM furin-sensitive loop at acidic pH facilitates its processing. The prM topology and domain assignment in TBEV is similar to the mosquito-borne Binjari virus, but is in contrast to other immature flavivirus models. These results support that prM cleavage, the collapse of E protein ectodomains onto the virion surface, the large movement of the membrane domains of both E and M, and the release of the pr fragment from the particle render the virus mature and infectious. Our work favors the collapse model of flavivirus maturation warranting further studies of immature flaviviruses to determine the sequence of events and mechanistic details driving flavivirus maturation.

PubMed: 38959313
DOI: 10.1126/sciadv.adl1888

Experimental method

ELECTRON MICROSCOPY (4 Å)