Abstract
Nervous necrosis virus (NNV) is a non-enveloped virus that causes massive mortality in aquaculture fish production worldwide. Recently X-ray crystallography and single particle cryo-EM have independently determined the icosahedral capsid of NNV to near-atomic resolutions to show the capsid protein is composed of a S-domain (shell) and a P-domain (protrusion) connected by a linker. However, the structure of the spike on NNV capsid made of trimeric P-domains was poorly resolved by cryo-EM. In addition, comparing the spike in the cryo-EM with that by X-ray suggests that the P-domain can move drastically relative to the shell, implicating an underlying structural mechanism during the infectious process. Yet, it remains unclear that such structural re-arrangement is ascribed to the change of the conformation of individual P-domain or in the association among P-domains. Given that molecular structure of the P-domain in solution phase is still lacking, we aim to determine the structure of the P-domain by solution NMR spectroscopy. In this communication, we report backbone and side chain 1H, 13C and 15N chemical shifts of the P-domain (residues 221–338) together with the linker region (residues 214–220), revealing ten β-strands via chemical shift propensity analysis. Our findings are consistent with the X-ray crystal structure of the P-domain reported elsewhere. The current study provides a framework towards further structural analyses of the P-domain in various solution conditions.
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Acknowledgements
We gratefully thank Claire Yang (Institute of Chemistry, Academia Sinica) for preparing the manuscript. NMR spectra were collected at the High-field NMR Center (HFNMRC), Academia Sinica, supported by Academia Sinica Core Facility and Innovative Instrument Project (AS-CFII-108-112). This research is funded by Grant MOST 103-2321-B-001-048, 104-2321-B-001-019, 105-2321-B-001-009 (WHC) and 107-2113-M-001-017 (DLT) from the Ministry of Science and Technology of Taiwan.
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Štěrbová, P., Wu, D., Lou, YC. et al. NMR assignments of protrusion domain of capsid protein from dragon grouper nervous necrosis virus. Biomol NMR Assign 14, 63–66 (2020). https://doi.org/10.1007/s12104-019-09921-x
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DOI: https://doi.org/10.1007/s12104-019-09921-x