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-Structure paper
タイトル | Programmable polymorphism of a virus-like particle. |
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ジャーナル・号・ページ | Commun Mater, Vol. 3, Page 7, Year 2022 |
掲載日 | 2022年2月7日 |
著者 | Artur P Biela / Antonina Naskalska / Farzad Fatehi / Reidun Twarock / Jonathan G Heddle / |
PubMed 要旨 | Virus-like particles (VLPs) have significant potential as artificial vaccines and drug delivery systems. The ability to control their size has wide ranging utility but achieving such controlled ...Virus-like particles (VLPs) have significant potential as artificial vaccines and drug delivery systems. The ability to control their size has wide ranging utility but achieving such controlled polymorphism using a single protein subunit is challenging as it requires altering VLP geometry. Here we achieve size control of MS2 bacteriophage VLPs via insertion of amino acid sequences in an external loop to shift morphology to significantly larger forms. The resulting VLP size and geometry is controlled by altering the length and type of the insert. Cryo electron microscopy structures of the new VLPs, in combination with a kinetic model of their assembly, show that the abundance of wild type ( = 3), = 4, D3 and D5 symmetrical VLPs can be biased in this way. We propose a mechanism whereby the insert leads to a change in the dynamic behavior of the capsid protein dimer, affecting the interconversion between the symmetric and asymmetric conformers and thus determining VLP size and morphology. |
リンク | Commun Mater / PubMed:35284827 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.35 - 4.22 Å |
構造データ | EMDB-12778: EMDB-12779: EMDB-12780: EMDB-12781: EMDB-12782: EMDB-12783: EMDB-12784: EMDB-12785: EMDB-12786: EMDB-12787: EMDB-12788: EMDB-12789: EMDB-12790: EMDB-12791: EMDB-12792: EMDB-12793: |
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