Disulfide bonds stabilize JC virus capsid‐like structure by protecting calcium ions from chelation

FEBS Letters

Chang, Deching³  Lii, Chong-Kuei²  Ou, Wei-Chih³  Chen, Pei-Lain³  Wang, Meilin¹  Chen, Li-Sheng³ 

[1] Department of Microbiology and Immunology, Chung Shan Medical and Dental College, Taichung, Taiwan, ROC;Institute of Nutrition, Chung Shan Medical and Dental College, Taichung, Taiwan, ROC;Institute of Molecular Biology, National Chung Cheng University, No. 160, San-Hsing, Ming-Hsiung, Chia-Yi 621, Taiwan, ROC

关键词: JC virus;    Assembly;    Disulfide bond;    Calcium ion;    JCV;    JC virus;    VP1;    major capsid protein;    VLP;    virus-like particle;   

DOI  :  10.1016/S0014-5793(01)02598-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To investigate the role of disulfide bonds in the capsid structure, a recombinant JC virus-like particle (VLP) was used. The major capsid protein, VP1, of the JC virus was expressed in yeast cells. The yeast-expressed VP1 was self-assembled into a VLP. Disulfide bonds were found in the VLP which caused dimeric and trimeric VP1 linkages as demonstrated by non-reducing SDS–PAGE. The VLP remained intact when disulfide bonds were reduced by dithiothreitol. The VLP without disulfide bonds could be disassembled into capsomeres by EGTA alone, but those with disulfide bonds could not be disassembled by EGTA. Capsomeres were reassembled into VLPs in the presence of calcium ions. Capsomeres formed irregular aggregations instead of VLPs when treated with diamide to reconstitute the disulfide bonds. These results indicate that disulfide bonds play an important role in maintaining the integrity of the JC VLP by protecting calcium ions from chelation.

【 授权许可】

Unknown