مورد إلكتروني
Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain
| العنوان: | Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain |
|---|---|
| بيانات النشر: | Elsevier 2021-02-18T13:38:54Z 2021-02-18T13:38:54Z 2020-02-29 |
| تفاصيل مُضافة: | Kalbermatter, David Shrestha, Neeta Gall, Flavio Wyss, Marianne Riedl, Rainer Plattet, Philippe Fotiadis, Dimitrios |
| نوع الوثيقة: | Electronic Resource |
| مستخلص: | Measles virus (MeV) and canine distemper virus (CDV), two members of the Morbillivirus genus, are still causing important global diseases of humans and animals, respectively. To enter target cells, morbilliviruses rely on an envelope-anchored machinery, which is composed of two interacting glycoproteins: a tetrameric receptor binding (H) protein and a trimeric fusion (F) protein. To execute membrane fusion, the F protein initially adopts a metastable, prefusion state that refolds into a highly stable postfusion conformation as the result of a finely coordinated activation process mediated by the H protein. Here, we employed cryo-electron microscopy (cryo-EM) and single particle reconstruction to elucidate the structure of the prefusion state of the CDV F protein ectodomain (solF) at 4.3 Å resolution. Stabilization of the prefusion solF trimer was achieved by fusing the GCNt trimerization sequence at the C-terminal protein region, and expressing and purifying the recombinant protein in the presence of a morbilliviral fusion inhibitor class compound. The three-dimensional cryo-EM map of prefusion CDV solF in complex with the inhibitor clearly shows density for the ligand at the protein binding site suggesting common mechanisms of membrane fusion activation and inhibition employed by different morbillivirus members. |
| مصطلحات الفهرس: | CDV, canine distemper virus, Canine distemper virus, Cryo-electron microscopy, FP, fusion peptide, Fusion protein, MeV, measles virus, Morbillivirus cell entry, Single particle reconstruction, cryo-EM, cryo-electron microscopy, 579: Mikrobiologie, Beitrag in wissenschaftlicher Zeitschrift, Text |
| URL: | Journal of Structural Biology: X |
| الإتاحة: | Open access content. Open access content http://creativecommons.org/licenses/by/4.0 |
| ملاحظة: | application/pdf Journal of Structural Biology: X English |
| أرقام أخرى: | CHZHA oai:digitalcollection.zhaw.ch:11475/21812 https://doi.org/10.1016/j.yjsbx.2020.100021 https://doi.org/10.21256/zhaw-21812 info:doi/10.1016/j.yjsbx.2020.100021 info:doi/10.21256/zhaw-21812 https://hdl.handle.net/11475/21812 https://digitalcollection.zhaw.ch/handle/11475/21812 info:hdl/11475/21812 urn:issn:2590-1524 32647825 1362709053 |
| المصدر المساهم: | ZHAW UNIV LIBR From OAIster®, provided by the OCLC Cooperative. |
| رقم الأكسشن: | edsoai.on1362709053 |
| قاعدة البيانات: | OAIster |
| الوصف غير متاح. |