Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Programmable polymorphism of a virus-like particle.
Journal, issue, pages	Commun Mater, Vol. 3, Page 7, Year 2022
Publish date	Feb 7, 2022
Authors	Artur P Biela / Antonina Naskalska / Farzad Fatehi / Reidun Twarock / Jonathan G Heddle /
PubMed Abstract	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.
External links	Commun Mater / PubMed:35284827 / PubMed Central
Methods	EM (single particle)
Resolution	2.35 - 4.22 Å
Structure data	EMDB-12778: MS2 coat protein dimer with 145-AHIVMVDAYKPTKGT-159 SpyTag insertion VLP displaying icosahedral T=3 symmetry Method: EM (single particle) / Resolution: 2.79 Å EMDB-12779: MS2 coat protein dimer with 145-AHIVMVDAYKPTKGT-159 SpyTag insertion VLP displaying icosahedral T=4 symmetry Method: EM (single particle) / Resolution: 3.36 Å EMDB-12780: MS2 coat protein dimer with 145-AHIVMVDAYKPTKGT-159 SpyTag insertion VLP displaying fullerene C70-like D5 symmetry Method: EM (single particle) / Resolution: 4.22 Å EMDB-12781: MS2 coat protein dimer with 145-GGGSAHIVMVDAYKPTKGGGSGT-167 insertion VLP displaying icosahedral T=3 symmetry Method: EM (single particle) / Resolution: 2.51 Å EMDB-12782: MS2 coat protein dimer with 145-GGGSAHIVMVDAYKPTKGGGSGT-167 insertion VLP displaying icosahedral T=4 symmetry Method: EM (single particle) / Resolution: 2.76 Å EMDB-12783: MS2 coat protein dimer with 145-GGGSAHIVMVDAYKPTKGGGSGT-167 insertion VLP displaying fullerene C70-like D5 symmetry Method: EM (single particle) / Resolution: 3.25 Å EMDB-12784: MS2 coat protein dimer with 145-GGGSAHIVMVDAYKPTKGGGSGT-167 insertion VLP displaying fullerene C74-like D3 symmetry Method: EM (single particle) / Resolution: 3.72 Å EMDB-12785: MS2 coat protein dimer with 145-GGGSYATMPIAKHVKDVGGGSGT-167 insertion VLP displaying icosahedral T=3 symmetry Method: EM (single particle) / Resolution: 2.37 Å EMDB-12786: MS2 coat protein dimer with 145-GGGSYATMPIAKHVKDVGGGSGT-167 insertion VLP displaying icosahedral T=4 symmetry Method: EM (single particle) / Resolution: 2.71 Å EMDB-12787: MS2 coat protein dimer with 145-GGGSYATMPIAKHVKDVGGGSGT-167 insertion VLP displaying fullerene C70-like D5 symmetry Method: EM (single particle) / Resolution: 2.95 Å EMDB-12788: MS2 coat protein dimer with 145-GGGSYATMPIAKHVKDVGGGSGT-167 insertion VLP displaying fullerene C74-like D3 symmetry Method: EM (single particle) / Resolution: 3.34 Å EMDB-12789: MS2 coat protein dimer with 145-GGGSYATMPIAKHVKDVGGGSGT-167 insertion VLP displaying fullerene C78-like D3 symmetry Method: EM (single particle) / Resolution: 3.49 Å EMDB-12790: MS2 coat protein dimer with 145-GSGGGGSAHIVMVDAYKPTKGGGSGGSGT-173 insertion VLP displaying icosahedral T=3 symmetry Method: EM (single particle) / Resolution: 2.35 Å EMDB-12791: MS2 coat protein dimer with 145-GSGGGGSAHIVMVDAYKPTKGGGSGGSGT-173 insertion VLP displaying icosahedral T=4 symmetry Method: EM (single particle) / Resolution: 2.71 Å EMDB-12792: MS2 coat protein dimer with 145-GSGGGGSAHIVMVDAYKPTKGGGSGGSGT-173 insertion VLP displaying fullerene C70-like D5 symmetry Method: EM (single particle) / Resolution: 3.09 Å EMDB-12793: MS2 coat protein dimer with 145-GSGGGGSAHIVMVDAYKPTKGGGSGGSGT-173 insertion VLP displaying fullerene C74-like D3 symmetry Method: EM (single particle) / Resolution: 3.92 Å
Source	Escherichia virus MS2 Enterobacteria phage MS2 (virus) Escherichia phage MS2 (virus)