7C2S

Helical reconstruction of Dengue virus serotype 3 complexed with Fab C10

Summary for 7C2S

• Entry DOI: 10.2210/pdb7c2s/pdb
• EMDB information: 30278
• Descriptor: envelope protein, Heavy chain of Fab C10, light chain of Fab C10 (3 entities in total)
• Functional Keywords: antibody, neutralization, virus
• Biological source: Homo sapiens; More
• Total number of polymer chains: 6
• Total formula weight: 138215.75

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

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: 32561757
DOI: 10.1038/s41467-020-16925-y

Experimental method

ELECTRON MICROSCOPY (10.4 Å)