Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate

doi:10.1126/science.abe1502

GSTDTAP > 气候变化

DOI	10.1126/science.abe1502
	Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate
	Sandhya Bangaru; Gabriel Ozorowski; Hannah L. Turner; Aleksandar Antanasijevic; Deli Huang; Xiaoning Wang; Jonathan L. Torres; Jolene K. Diedrich; Jing-Hui Tian; Alyse D. Portnoff; Nita Patel; Michael J. Massare; John R. Yates; David Nemazee; James C. Paulson; Greg Glenn; Gale Smith; Andrew B. Ward
	2020-11-27
发表期刊	Science
出版年	2020
英文摘要	Much effort is being targeted at developing vaccines that will provide protection against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). A trimeric spike protein that decorates the virus is a primary target of the host immune system and the focus of vaccine development. Bangaru et al. present the structure of a leading vaccine candidate: a full-length spike protein with some modifications aimed at enhancing stability that is formulated in polysorbate 80 detergent. The study confirms that the full-length immunogen is in a stable prefusion conformation and provides a basis for understanding immune responses to the vaccine. Science , this issue p. [1089][1] Vaccine efforts to combat the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which is responsible for the current coronavirus disease 2019 (COVID-19) pandemic, are focused on SARS-CoV-2 spike glycoprotein, the primary target for neutralizing antibodies. We performed cryo–election microscopy and site-specific glycan analysis of one of the leading subunit vaccine candidates from Novavax, which is based on a full-length spike protein formulated in polysorbate 80 detergent. Our studies reveal a stable prefusion conformation of the spike immunogen with slight differences in the S1 subunit compared with published spike ectodomain structures. We also observed interactions between the spike trimers, allowing formation of higher-order spike complexes. This study confirms the structural integrity of the full-length spike protein immunogen and provides a basis for interpreting immune responses to this multivalent nanoparticle immunogen. [1]: /lookup/doi/10.1126/science.abe1502
领域	气候变化 ; 资源环境
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文献类型	期刊论文
条目标识符	http://119.78.100.173/C666/handle/2XK7JSWQ/304884
专题	气候变化资源环境科学
推荐引用方式 GB/T 7714	Sandhya Bangaru,Gabriel Ozorowski,Hannah L. Turner,et al. Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate[J]. Science,2020.
APA	Sandhya Bangaru.,Gabriel Ozorowski.,Hannah L. Turner.,Aleksandar Antanasijevic.,Deli Huang.,...&Andrew B. Ward.(2020).Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate.Science.
MLA	Sandhya Bangaru,et al."Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate".Science (2020).