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

Author:

Bangaru Sandhya1ORCID,Ozorowski Gabriel1ORCID,Turner Hannah L.1,Antanasijevic Aleksandar1ORCID,Huang Deli2ORCID,Wang Xiaoning3ORCID,Torres Jonathan L.1ORCID,Diedrich Jolene K.3ORCID,Tian Jing-Hui4,Portnoff Alyse D.4,Patel Nita4,Massare Michael J.4,Yates John R.3ORCID,Nemazee David2ORCID,Paulson James C.23ORCID,Glenn Greg4ORCID,Smith Gale4,Ward Andrew B.1ORCID

Affiliation:

1. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

2. Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.

3. Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.

4. Novavax, Inc., 21 Firstfield Road, Gaithersburg, MD 20878, USA.

Abstract

Structure of a vaccine candidate 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

Funder

National Institutes of Health

Bill and Melinda Gates Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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