| Autor: |
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 |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Biophysical chemistry. 293 |
| ISSN: |
1873-4200 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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