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Mapping glycoprotein structure reveals Flaviviridae evolutionary history.
Mifsud, Jonathon C O; Lytras, Spyros; Oliver, Michael R; Toon, Kamilla; Costa, Vincenzo A; Holmes, Edward C; Grove, Joe.
Afiliação
  • Mifsud JCO; Sydney Institute for Infectious Diseases, School of Medical Sciences, The University of Sydney, Sydney, New South Wales, Australia.
  • Lytras S; MRC-University of Glasgow Centre for Virus Research, Glasgow, UK.
  • Oliver MR; Division of Systems Virology, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
  • Toon K; MRC-University of Glasgow Centre for Virus Research, Glasgow, UK.
  • Costa VA; MRC-University of Glasgow Centre for Virus Research, Glasgow, UK.
  • Holmes EC; Sydney Institute for Infectious Diseases, School of Medical Sciences, The University of Sydney, Sydney, New South Wales, Australia.
  • Grove J; Sydney Institute for Infectious Diseases, School of Medical Sciences, The University of Sydney, Sydney, New South Wales, Australia.
Nature ; 633(8030): 695-703, 2024 Sep.
Article em En | MEDLINE | ID: mdl-39232167
ABSTRACT
Viral glycoproteins drive membrane fusion in enveloped viruses and determine host range, tissue tropism and pathogenesis1. Despite their importance, there is a fragmentary understanding of glycoproteins within the Flaviviridae2, a large virus family that include pathogens such as hepatitis C, dengue and Zika viruses, and numerous other human, animal and emergent viruses. For many flaviviruses the glycoproteins have not yet been identified, for others, such as the hepaciviruses, the molecular mechanisms of membrane fusion remain uncharacterized3. Here we combine phylogenetic analyses with protein structure prediction to survey glycoproteins across the entire Flaviviridae. We find class II fusion systems, homologous to the Orthoflavivirus E glycoprotein in most species, including highly divergent jingmenviruses and large genome flaviviruses. However, the E1E2 glycoproteins of the hepaciviruses, pegiviruses and pestiviruses are structurally distinct, may represent a novel class of fusion mechanism, and are strictly associated with infection of vertebrate hosts. By mapping glycoprotein distribution onto the underlying phylogeny, we reveal a complex evolutionary history marked by the capture of bacterial genes and potentially inter-genus recombination. These insights, made possible through protein structure prediction, refine our understanding of viral fusion mechanisms and reveal the events that have shaped the diverse virology and ecology of the Flaviviridae.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Filogenia / Glicoproteínas / Proteínas do Envelope Viral / Flaviviridae / Evolução Molecular Limite: Animals / Humans Idioma: En Revista: Nature Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Austrália País de publicação: Reino Unido
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Filogenia / Glicoproteínas / Proteínas do Envelope Viral / Flaviviridae / Evolução Molecular Limite: Animals / Humans Idioma: En Revista: Nature Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Austrália País de publicação: Reino Unido