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-Structure paper
タイトル | Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms. |
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ジャーナル・号・ページ | Sci Adv, Vol. 9, Issue 6, Page eade2727, Year 2023 |
掲載日 | 2023年2月10日 |
![]() | 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 / ![]() ![]() |
PubMed 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. |
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手法 | EM (サブトモグラム平均) |
解像度 | 10.2 - 16.5 Å |
構造データ | ![]() EMDB-27550: Subtomogram average of the HN/F fusion complex on authentic viral surfaces of HPIV3 ![]() EMDB-27551: Subtomogram average of the PIA174 Fab/F complex on authentic viral surfaces of HPIV3 |