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病毒疫苗:蛋白质偏爱脯氨酸。

Virus vaccines: proteins prefer prolines.

机构信息

Department of Microbiology and Immunology, Weill Cornell Medicine, 1300 York Avenue, New York, NY 10065, USA; Department of Medical Microbiology and Infection Prevention, Amsterdam University Medical Centers, Location AMC, University of Amsterdam, Meibergdreef 15, 1105 AZ Amsterdam, the Netherlands.

Department of Microbiology and Immunology, Weill Cornell Medicine, 1300 York Avenue, New York, NY 10065, USA.

出版信息

Cell Host Microbe. 2021 Mar 10;29(3):327-333. doi: 10.1016/j.chom.2021.02.002.

Abstract

Most viral vaccines are based on inducing neutralizing antibodies (NAbs) against the virus envelope or spike glycoproteins. Many viral surface proteins exist as trimers that transition from a pre-fusion state when key NAb epitopes are exposed to a post-fusion form in which the potential for virus-cell fusion no longer exists. For optimal vaccine performance, these viral proteins are often engineered to enhance stability and presentation of these NAb epitopes. The method involves the structure-guided introduction of proline residues at key positions that maintain the trimer in the pre-fusion configuration. We review how this technique emerged during HIV-1 Env vaccine development and its subsequent wider application to other viral vaccines including SARS-CoV-2.

摘要

大多数病毒疫苗都是基于诱导针对病毒包膜或刺突糖蛋白的中和抗体(NAb)。许多病毒表面蛋白以三聚体形式存在,当关键的 NAb 表位暴露时,三聚体从预融合状态转变为不存在病毒-细胞融合潜力的融合后形式。为了获得最佳的疫苗效果,这些病毒蛋白通常经过工程改造以增强这些 NAb 表位的稳定性和呈现。该方法涉及在关键位置引入脯氨酸残基,以保持三聚体处于预融合构象,这是一种基于结构的方法。我们回顾了该技术在 HIV-1Env 疫苗开发过程中的出现及其随后在其他病毒疫苗(包括 SARS-CoV-2)中的更广泛应用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75f1/7945883/77bd97b1148b/gr1_lrg.jpg

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