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| Title | Inside and outside of virus-like particles HBc and HBc/4M2e: A comprehensive study of the structure. |
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| Journal, issue, pages | Biophys Chem, Vol. 293, Page 106943, Year 2023 |
| Publish date | Dec 5, 2022 |
 Authors | V V Egorov / A V Shvetsov / E B Pichkur / A A Shaldzhyan / Ya A Zabrodskaya / D S Vinogradova / P A Nekrasov / A N Gorshkov / Yu P Garmay / A A Kovaleva / L A Stepanova / L M Tsybalova / T A Shtam / A G Myasnikov / A L Konevega /  |
| PubMed Abstract | Hepatitis B virus core antigen (HBc) with the insertion of four external domains of the influenza A M2 protein (HBc/4M2e) form virus-like particles whose structure was studied using a combination of ...Hepatitis B virus core antigen (HBc) with the insertion of four external domains of the influenza A M2 protein (HBc/4M2e) form virus-like particles whose structure was studied using a combination of molecular modeling and cryo-electron microscopy (cryo-EM). It was also shown that self-assembling of the particles occurs inside bacterial cells, but despite the big inner volume of the core shell particle, purified HBc/4M2e contain an insignificant amount of bacterial proteins. It was shown that a fragment of the M2e corresponding to 4M2e insertion is prone to formation of amyloid-like fibrils. However, as the part of the immunodominant loop, M2e insertion does not show a tendency to intermolecular interaction. A full-atomic HBc-4M2e model with the resolution of about 3 Å (3.13 Å for particles of Т = 4 symmetry, 3.7 Å for particles of Т = 3 symmetry) was obtained by molecular modeling methods based on cryo-EM data. |
 External links | Biophys Chem / PubMed:36495688 |
| Methods | EM (single particle) |
| Resolution | 3.13 - 4.0 Å |
| Structure data | EMDB-15995, PDB-8bdz: EMDB-16009, PDB-8ber: |
| Source |
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 Keywords |  VIRUS LIKE PARTICLE / HBc / M2e / VLP |
