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-Structure paper
タイトル | Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate. |
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ジャーナル・号・ページ | Science, Vol. 370, Issue 6520, Page 1089-1094, Year 2020 |
掲載日 | 2020年11月27日 |
著者 | 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 / |
PubMed 要旨 | 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- ...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. |
リンク | Science / PubMed:33082295 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 - 8.0 Å |
構造データ | EMDB-22352, PDB-7jji: EMDB-22353: EMDB-22354, PDB-7jjj: EMDB-22355: EMDB-22356: |
化合物 | ChemComp-NAG: ChemComp-VCG: ChemComp-EIC: |
由来 |
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キーワード | VIRAL PROTEIN / SARS-CoV-2 / Glycoprotein / Immunogen / vaccine |