6LNT

Cryo-EM structure of immature Zika virus in complex with human antibody DV62.5 Fab

Summary for 6LNT

• Entry DOI: 10.2210/pdb6lnt/pdb
• Related: 6LNU
• EMDB information: 0932 0934
• Descriptor: Envelope protein, pre-membrane protein, Fab DV62.5 heavy-chain variable region, ... (5 entities in total)
• Functional Keywords: immature zika virus, human antibody, virus
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 12
• Total formula weight: 293954.06

Authors

Tan, T.Y.,Fibriansah, G.,Kostyuchenko, V.A.,Ng, T.S.,Lim, X.X.,Lim, X.N.,Shi, J.,Morais, M.C.,Corti, D.,Lok, S.M. (deposition date: 2020-01-02, release date: 2020-02-26, Last modification date: 2024-03-27)

Primary citation

Tan, T.Y.,Fibriansah, G.,Kostyuchenko, V.A.,Ng, T.S.,Lim, X.X.,Zhang, S.,Lim, X.N.,Wang, J.,Shi, J.,Morais, M.C.,Corti, D.,Lok, S.M.
Capsid protein structure in Zika virus reveals the flavivirus assembly process.
Nat Commun, 11:895-895, 2020

PubMed Abstract: Structures of flavivirus (dengue virus and Zika virus) particles are known to near-atomic resolution and show detailed structure and arrangement of their surface proteins (E and prM in immature virus or M in mature virus). By contrast, the arrangement of the capsid proteins:RNA complex, which forms the core of the particle, is poorly understood, likely due to inherent dynamics. Here, we stabilize immature Zika virus via an antibody that binds across the E and prM proteins, resulting in a subnanometer resolution structure of capsid proteins within the virus particle. Fitting of the capsid protein into densities shows the presence of a helix previously thought to be removed via proteolysis. This structure illuminates capsid protein quaternary organization, including its orientation relative to the lipid membrane and the genomic RNA, and its interactions with the transmembrane regions of the surface proteins. Results show the capsid protein plays a central role in the flavivirus assembly process.

PubMed: 32060358
DOI: 10.1038/s41467-020-14647-9

Experimental method

ELECTRON MICROSCOPY (8 Å)