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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Štěrbová P,Wu D,Lou YC,Wang CH,Chang WH,Tzou DMdoi
10.1007/s12104-019-09921-xsubject
Has Abstractpub_date
2020-04-01 00:00:00pages
63-66issue
1eissn
1874-2718issn
1874-270Xpii
10.1007/s12104-019-09921-xjournal_volume
14pub_type
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