Capsid protein structure in Zika virus reveals the flavivirus assembly process

Ter Yong Tan, Guntur Fibriansah, Victor A. Kostyuchenko, Thiam-Seng Ng, Xin-Xiang Lim, Shuijun Zhang, Xin-Ni Lim, Jiaqi Wang, Jian Shi, Marc C. Morais, Davide Corti and Shee-Mei Lok ()
Additional contact information
Ter Yong Tan: Duke–National University of Singapore Medical School
Guntur Fibriansah: Duke–National University of Singapore Medical School
Victor A. Kostyuchenko: Duke–National University of Singapore Medical School
Thiam-Seng Ng: Duke–National University of Singapore Medical School
Xin-Xiang Lim: National University of Singapore
Shuijun Zhang: Duke–National University of Singapore Medical School
Xin-Ni Lim: Duke–National University of Singapore Medical School
Jiaqi Wang: Duke–National University of Singapore Medical School
Jian Shi: National University of Singapore
Marc C. Morais: University of Texas Medical Branch
Davide Corti: Humabs BioMed SA, a subsidiary of Vir Biotechnology, Inc.
Shee-Mei Lok: Duke–National University of Singapore Medical School

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: 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.

Date: 2020
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-020-14647-9 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14647-9

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-020-14647-9

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().