AI Article Synopsis
- - Vaccine development against SARS-CoV-2 centers on targeting the spike glycoprotein to elicit neutralizing antibodies.
- - Researchers used cryo-EM and glycan analysis to study a leading Novavax subunit vaccine, revealing a stable form of the spike protein with slight variations.
- - The study identified unique interactions between spike trimers, contributing to the protein's structural integrity and offering insights into immune responses to the vaccine candidate.
Article Abstract
Vaccine efforts against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) responsible for the current COVID-19 pandemic are focused on SARS-CoV-2 spike glycoprotein, the primary target for neutralizing antibodies. Here, we performed cryo-EM and site-specific glycan analysis of one of the leading subunit vaccine candidates from Novavax based on a full-length spike protein formulated in polysorbate 80 (PS 80) detergent. Our studies reveal a stable prefusion conformation of the spike immunogen with slight differences in the S1 subunit compared to published spike ectodomain structures. Interestingly, we also observed novel 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.
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Source |
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7418715 | PMC |
| http://dx.doi.org/10.1101/2020.08.06.234674 | DOI Listing |
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