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- Title
The atomic structures of shrimp nodaviruses reveal new dimeric spike structures and particle polymorphism.
- Authors
Chen, Nai-Chi; Yoshimura, Masato; Miyazaki, Naoyuki; Guan, Hong-Hsiang; Chuankhayan, Phimonphan; Lin, Chien-Chih; Chen, Shao-Kang; Lin, Pei-Ju; Huang, Yen-Chieh; Iwasaki, Kenji; Nakagawa, Atsushi; Chan, Sunney I.; Chen, Chun-Jung
- Abstract
Shrimp nodaviruses, including Penaeus vannamei (PvNV) and Macrobrachium rosenbergii nodaviruses (MrNV), cause white-tail disease in shrimps, with high mortality. The viral capsid structure determines viral assembly and host specificity during infections. Here, we show cryo-EM structures of T = 3 and T = 1 PvNV-like particles (PvNV-LPs), crystal structures of the protrusion-domains (P-domains) of PvNV and MrNV, and the crystal structure of the ∆N-ARM-PvNV shell-domain (S-domain) in T = 1 subviral particles. The capsid protein of PvNV reveals five domains: the P-domain with a new jelly-roll structure forming cuboid-like spikes; the jelly-roll S-domain with two calcium ions; the linker between the S- and P-domains exhibiting new cross and parallel conformations; the N-arm interacting with nucleotides organized along icosahedral two-fold axes; and a disordered region comprising the basic N-terminal arginine-rich motif (N-ARM) interacting with RNA. The N-ARM controls T = 3 and T = 1 assemblies. Increasing the N/C-termini flexibility leads to particle polymorphism. Linker flexibility may influence the dimeric-spike arrangement. Nai-Chi Chen et al. solved the structures of two shrimp nodaviruses, focusing on the major domains to improve understanding of capsid organization. By combining cryo-EM and x-ray crystallography, the authors were able to observe the structures at a high resolution.
- Subjects
ATOMIC structure; NODAVIRUSES; MACROBRACHIUM rosenbergii; MORTALITY; X-ray crystallography
- Publication
Communications Biology, 2019, Vol 2, Issue 1, pN.PAG
- ISSN
2399-3642
- Publication type
Article
- DOI
10.1038/s42003-019-0311-z