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The structure of immature tick-borne encephalitis virus supports the collapse model of flavivirus maturation.
Anastasina, Maria; Füzik, Tibor; Domanska, Ausra; Pulkkinen, Lauri Ilmari Aurelius; Smerdová, Lenka; Formanová, Petra Pokorná; Straková, Petra; Novácek, Jirí; Ruzek, Daniel; Plevka, Pavel; Butcher, Sarah Jane.
Afiliação
  • Anastasina M; Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, Helsinki, Finland.
  • Füzik T; Helsinki Institute of Life Sciences-Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
  • Domanska A; Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
  • Pulkkinen LIA; Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, Helsinki, Finland.
  • Smerdová L; Helsinki Institute of Life Sciences-Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
  • Formanová PP; Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, Helsinki, Finland.
  • Straková P; Helsinki Institute of Life Sciences-Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
  • Novácek J; Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
  • Ruzek D; Laboratory of Emerging Viral Infections, Veterinary Research Institute, Brno, Czech Republic.
  • Plevka P; Laboratory of Emerging Viral Infections, Veterinary Research Institute, Brno, Czech Republic.
  • Butcher SJ; Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czech Republic.
Sci Adv ; 10(27): eadl1888, 2024 Jul 05.
Article em En | MEDLINE | ID: mdl-38959313
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.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas do Envelope Viral / Vírus da Encefalite Transmitidos por Carrapatos Limite: Animals / Humans Idioma: En Revista: Sci Adv Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Finlândia País de publicação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas do Envelope Viral / Vírus da Encefalite Transmitidos por Carrapatos Limite: Animals / Humans Idioma: En Revista: Sci Adv Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Finlândia País de publicação: Estados Unidos