数字农科院2.0

Quantitative regulation of the thermal stability of enveloped virus vaccines by surface charge engineering to prevent the self-aggregation of attachment glycoproteins

文献类型： 外文期刊

作者： Yu Shang;Li Li;Tengfei Zhang;Qingping Luo;Qingzhong Yu;Zhe Zeng;Lintao Li;Miaomiao Jia;Guoyi Tang;Sanlin Fan;Qin Lu;Wenting Zhang;Yuhan Xue;Hongling Wang;Wei Liu;Hongcai Wang;Rongrong Zhang;Chan Ding;Huabin Shao;Guoyuan Wen

作者机构：

期刊名称： PLoS pathogens

ISSN： 1553-7374

年卷期： 2022 年 18 卷 6 期

页码：

摘要： The development of thermostable vaccines can relieve the bottleneck of existing vaccines caused by thermal instability and subsequent poor efficacy, which is one of the predominant reasons for the millions of deaths caused by vaccine-preventable diseases. Research into the mechanism of viral thermostability may provide strategies for developing thermostable vaccines. Using Newcastle disease virus (NDV) as model, we identified the negative surface charge of attachment glycoprotein as a novel determinant of viral thermostability. It prevented the temperature-induced aggregation of glycoprotein and subsequent detachment from virion surface. Then structural stability of virion surface was improved and virus could bind to and infect cells efficiently after heat-treatment. Employing the approach of surface charge engineering, thermal stability of NDV and influenza A virus (IAV) vaccines was successfully improved. The increase in the level of vaccine thermal stability was determined by the value-added in the negative surface charge of the attachment glycoprotein. The engineered live and inactivated vaccines could be used efficiently after storage at 37°C for at least 10 and 60 days, respectively. Thus, our results revealed a novel surface-charge-mediated link between HN protein and NDV thermostability, which could be used to design thermal stable NDV and IAV vaccines rationally.

分类号：

  • 相关文献
作者其他论文 更多>>