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-Structure paper
タイトル | Production and Characterisation of Stabilised PV-3 Virus-like Particles Using . |
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ジャーナル・号・ページ | Viruses, Vol. 14, Issue 10, Year 2022 |
掲載日 | 2022年9月30日 |
![]() | Lee Sherry / Keith Grehan / Jessica J Swanson / Mohammad W Bahar / Claudine Porta / Elizabeth E Fry / David I Stuart / David J Rowlands / Nicola J Stonehouse / ![]() |
PubMed 要旨 | Following the success of global vaccination programmes using the live-attenuated oral and inactivated poliovirus vaccines (OPV and IPV), wild poliovirus (PV) is now only endemic in Afghanistan and ...Following the success of global vaccination programmes using the live-attenuated oral and inactivated poliovirus vaccines (OPV and IPV), wild poliovirus (PV) is now only endemic in Afghanistan and Pakistan. However, the continued use of these vaccines poses potential risks to the eradication of PV. The production of recombinant PV virus-like particles (VLPs), which lack the viral genome offer great potential as next-generation vaccines for the post-polio world. We have previously reported production of PV VLPs using , however, these VLPs were in the non-native conformation (C Ag), which would not produce effective protection against PV. Here, we build on this work and show that it is possible to produce wt PV-3 and thermally stabilised PV-3 (referred to as PV-3 SC8) VLPs in the native conformation (D Ag) using . We show that the PV-3 SC8 VLPs provide a much-improved D:C antigen ratio as compared to wt PV-3, whilst exhibiting greater thermostability than the current IPV vaccine. Finally, we determine the cryo-EM structure of the yeast-derived PV-3 SC8 VLPs and compare this to previously published PV-3 D Ag structures, highlighting the similarities between these recombinantly expressed VLPs and the infectious virus, further emphasising their potential as a next-generation vaccine candidate for PV. |
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手法 | EM (単粒子) |
解像度 | 2.7 Å |
構造データ | EMDB-15543, PDB-8anw: |
化合物 | ![]() ChemComp-SPH: |
由来 |
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![]() | VIRUS LIKE PARTICLE / Capsid protein |