Irreversible furin cleavage site exposure renders immature tick-borne flaviviruses fully infectious

• Published in: Nature communications Vol. 16; no. 1; pp. 7491 - 17
• Main Authors: Holoubek, Jiří, Salát, Jiří, Matkovic, Milos, Bednář, Petr, Novotný, Pavel, Hradilek, Martin, Majerová, Taťána, Rosendal, Ebba, Eyer, Luděk, Fořtová, Andrea, Beránková, Michaela, Bell-Sakyi, Lesley, Överby, Anna K., Cavalli, Andrea, Bonomi, Massimiliano, Rey, Félix A., Růžek, Daniel
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 12.08.2025; Nature Publishing Group; Nature Portfolio
• Subjects: 13/1; 13/106; 13/51; 14/1; 14/63; 631/326/596/2555; 631/326/596/2557; 64; 64/60; Animals; Aquatic insects; Arachnids; Cleavage; Dengue fever; Dimers; Encephalitis; Encephalitis Viruses, Tick-Borne - genetics; Encephalitis Viruses, Tick-Borne - metabolism; Encephalitis Viruses, Tick-Borne - pathogenicity; Encephalitis Viruses, Tick-Borne - physiology; Endoplasmic reticulum; Experiments; Exposure; Female; Flaviviridae; Flavivirus - genetics; Flavivirus - pathogenicity; Flavivirus - physiology; Furin; Furin - genetics; Furin - metabolism; Genomes; Glycoproteins; Golgi apparatus; Humanities and Social Sciences; Humans; Hydrogen-Ion Concentration; Infections; Infectivity; Maturation; Mice; Mice, Inbred BALB C; Modelling; Molecular dynamics; Mosquitoes; multidisciplinary; pH effects; Phenotypes; Proteins; Proteolysis; Science; Science (multidisciplinary); Site-directed mutagenesis; Tick-borne encephalitis; Vector-borne diseases; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - genetics; Viral Envelope Proteins - metabolism; Virions; Virus Assembly; Viruses; West Nile virus

Flavivirus assembly is driven by the envelope glycoproteins pre-membrane (prM) and envelope (E) in the neutral pH environment of the endoplasmic reticulum. Newly budded, spiky particles are exported through the Golgi apparatus, where mildly acidic pH induces a major surface rearrangement. The glycop...