Distinct conformational states of SARS-CoV-2 spike protein
Yongfei Cai,Yongfei Cai,Jun Zhang,Jun Zhang,Tianshu Xiao,Tianshu Xiao,Hanqin Peng,Sarah M. Sterling,Richard M. Walsh,Shaun Rawson,Sophia Rits-Volloch,Bing Chen,Bing Chen +12 more
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TLDR
Two cryo–electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion and postfusion conformations, are reported, advancing the understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.Abstract:
Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.read more
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Journal ArticleDOI
SARS-CoV-2 Variants Increase Kinetic Stability of Open Spike Conformations as an Evolutionary Strategy
TL;DR: SARS-CoV-2 surface S glycoprotein is responsible for binding to the cellular receptor hACE2 as discussed by the authors , which triggers structural rearrangements of S from closed to open conformations prerequisite for virus entry.
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Structural definition of a pan-sarbecovirus neutralizing epitope on the spike S2 subunit
TL;DR: In this article , a neutralizing monoclonal antibody, CV3-25, was proposed to neutralize the SARS-CoV-2 spike and neutralize SARS CoV-1 spike.
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Molecular characteristics, immune evasion, and impact of SARS-CoV-2 variants
TL;DR: This review summarized the molecular characteristics, immune evasion, and impacts of the SARS-CoV-2 variants and focused on the parallel comparison of different variants in mutational profile, transmissibility and tropism alteration, treatment effectiveness, and clinical manifestations, in order to provide a comprehensive landscape for SARs-Cov-2 variant research.
Journal ArticleDOI
Interaction of Human ACE2 to Membrane-Bound SARS-CoV-1 and SARS-CoV-2 S Glycoproteins
Sai Priya Anand,Yaozong Chen,Jérémie Prévost,Romain Gasser,Guillaume Beaudoin-Bussières,Cameron F. Abrams,Marzena Pazgier,Andrés Finzi,Andrés Finzi +8 more
TL;DR: It is shown that there exist differential inter-protomer conformational transitions between both spike trimers, and Interestingly, the SARS-CoV-2 spike exhibits a positive cooperativity for monomeric soluble ACE2 binding when compared to the SARV-1 spike, which might have more structural restraints.
Posted ContentDOI
Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies
Renhong Yan,Ruoke Wang,Bin Ju,Jinfang Yu,Yuanyuan Zhang,Nan Liu,Jia Wang,Qi Zhang,Peng Chen,Bing Zhou,Yaning Li,Shuyuan Zhang,Long Tian,Xinyue Zhong,Lin Cheng,Xiangyang Ge,Juanjuan Zhao,Hong-Wei Wang,Xinquan Wang,Zheng Zhang,Linqi Zhang,Qiang Zhou +21 more
TL;DR: Cryo-EM structures of the ten most potent nAbs in their native full-length IgG or Fab forms bound to the trimeric S protein of SARS-CoV-2 reveal the bivalent binding and their correlation with more potent neutralization and the shedding of S1 subunit.
References
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