National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI152275
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI121349
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI160953
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI114736
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI160961
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM133598
米国
引用
ジャーナル: Sci Adv / 年: 2023 タイトル: Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms. 著者: Tara C Marcink / Gillian Zipursky / Wenjing Cheng / Kyle Stearns / Shari Stenglein / Kate Golub / Frances Cohen / Francesca Bovier / Daniel Pfalmer / Alexander L Greninger / Matteo Porotto / ...著者: Tara C Marcink / Gillian Zipursky / Wenjing Cheng / Kyle Stearns / Shari Stenglein / Kate Golub / Frances Cohen / Francesca Bovier / Daniel Pfalmer / Alexander L Greninger / Matteo Porotto / Amedee des Georges / Anne Moscona / 要旨: Paramyxoviruses-including important pathogens like parainfluenza, measles, and Nipah viruses-use a receptor binding protein [hemagglutinin-neuraminidase (HN) for parainfluenza] and a fusion protein ...Paramyxoviruses-including important pathogens like parainfluenza, measles, and Nipah viruses-use a receptor binding protein [hemagglutinin-neuraminidase (HN) for parainfluenza] and a fusion protein (F), acting in a complex, to enter cells. We use cryo-electron tomography to visualize the fusion complex of human parainfluenza virus 3 (HN/F) on the surface of authentic clinical viruses at a subnanometer resolution sufficient to answer mechanistic questions. An HN loop inserts in a pocket on F, showing how the fusion complex remains in a ready but quiescent state until activation. The globular HN heads are rotated with respect to each other: one downward to contact F, and the other upward to grapple cellular receptors, demonstrating how HN/F performs distinct steps before F activation. This depiction of viral fusion illuminates potentially druggable targets for paramyxoviruses and sheds light on fusion processes that underpin wide-ranging biological processes but have not been visualized in situ or at the present resolution.