Journal of Proteomics & Bioinformatics
Open Access

Cation roles in the structure of a fish nodavirus observed in electron cryo-microscopy and X-ray diffraction

6^th International Conference on Structural Biology

August 22-23, 2016 New Orleans, USA

Chan-Shing Lin, Chia-Yu Lin, Chun-Hsiung Wang, Yen-Fu Lin, Chiu-Hao Chen, Ruei-Chi Wang, Ying-Rong Lin, Wangta Liu, Wei-Hau Chang and R Holland Cheng

National Sun Yat-sen University, Taiwan
Institute of Chemistry and Institute of Physics, Taiwan
Kaohsiung Medical University, Taiwan
Wenzao Ursuline University of Languages, Taiwan
University of California, USA

Posters & Accepted Abstracts: J Proteomics Bioinform

Abstract :

The virus-like particle (VLP) assembled from capsid subunits of the dragon grouper nervous necrosis virus (DGNNV) is very similar to its native T=3 virion, in addition that the VLPs can enter fish cells with macropinocytosis way. Furthermore, the disulfide bounds are not essential for the VLP formation, whereas cations are involved in the VLP stability in vitro. At pH 8.0, the VLPs can be precipitated with EDTA at room temperature. In weak basic condition, cryoEM model of the capsid protein (52-213th amino acids) at 3.56 �?�? resolution reveals calcium-ion bridges and unique cation-�? interactions. Submersion of VLP crystals in cations provide sharper diffraction intensity than control and enhanced the radiation damage. All together supports that cations stabilize the viral particle by holding three subunits in an asymmetric unit of trimer.

Biography :

Chan-Shing Lin has completed his PhD at University of California, Irvine, in 1992. He has published more than 65 papers in reputed journals and has been serving as an Editorial Board Member of Archive of Virology and Frontier journals. He has also consulted biotechnology companies in building the cGMP processes for manufacturing vaccines and bio-medicals.

Email: shinlin@faculty.nsysu.edu.tw