7C2T
Helical reconstruction of Zika virus complexed with Fab C10
Summary for 7C2T
| Entry DOI | 10.2210/pdb7c2t/pdb |
| EMDB information | 30279 |
| Descriptor | envelope protein, M protein, Heavy chain from Fab C10, ... (4 entities in total) |
| Functional Keywords | antibody, neutralization, virus |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 8 |
| Total formula weight | 177452.71 |
| Authors | Morrone, S.,Chew, S.V.,Lim, X.N.,Ng, T.S.,Kostyuchenko, V.A.,Zhang, S.,Lok, S.M. (deposition date: 2020-05-09, release date: 2020-07-08, Last modification date: 2024-03-27) |
| Primary citation | Morrone, S.R.,Chew, V.S.Y.,Lim, X.N.,Ng, T.S.,Kostyuchenko, V.A.,Zhang, S.,Wirawan, M.,Chew, P.L.,Lee, J.,Tan, J.L.,Wang, J.,Tan, T.Y.,Shi, J.,Screaton, G.,Morais, M.C.,Lok, S.M. High flavivirus structural plasticity demonstrated by a non-spherical morphological variant. Nat Commun, 11:3112-3112, 2020 Cited by PubMed Abstract: Previous flavivirus (dengue and Zika viruses) studies showed largely spherical particles either with smooth or bumpy surfaces. Here, we demonstrate flavivirus particles have high structural plasticity by the induction of a non-spherical morphology at elevated temperatures: the club-shaped particle (clubSP), which contains a cylindrical tail and a disc-like head. Complex formation of DENV and ZIKV with Fab C10 stabilize the viruses allowing cryoEM structural determination to ~10 Å resolution. The caterpillar-shaped (catSP) Fab C10:ZIKV complex shows Fabs locking the E protein raft structure containing three E dimers. However, compared to the original spherical structure, the rafts have rotated relative to each other. The helical tail structure of Fab C10:DENV3 clubSP showed although the Fab locked an E protein dimer, the dimers have shifted laterally. Morphological diversity, including clubSP and the previously identified bumpy and smooth-surfaced spherical particles, may help flavivirus survival and immune evasion. PubMed: 32561757DOI: 10.1038/s41467-020-16925-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (9.4 Å) |
Structure validation
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