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Chemistry Archives | The Daily Galaxy
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Alien Molecules in Dark-Clouds of the Cosmos -- Never Before Seen in Space
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Summer Weight Gain Among Preschool-Aged Children With Obesity: An Observational Study in Head Start
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IMAGE: This model shows the structure of the spike protein in its closed configuration, in its original D614 form (left) and its mutant form (G614). In the mutant spike protein, the. view more
Credit: Bing Chen, PhD, Boston Children s Hospital
BOSTON - March 16, 2021 - The fast-spreading UK, South Africa, and Brazil coronavirus variants are raising both concerns and questions about whether COVID-19 vaccines will protect against them. New work led by Bing Chen, PhD, at Boston Children s Hospital analyzed how the structure of the coronavirus spike proteins changes with the D614G mutation carried by all three variants and showed why these variants are able to spread more quickly. The team reports its findings in
Abstract
Substitution for aspartic acid by glycine at position 614 in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 appears to facilitate rapid viral spread. The G614 strain and its recent variants are now the dominant circulating forms. We report here cryo-EM structures of a full-length G614 S trimer, which adopts three distinct prefusion conformations differing primarily by the position of one receptor-binding domain. A loop disordered in the D614 S trimer wedges between domains within a protomer in the G614 spike. This added interaction appears to prevent premature dissociation of the G614 trimer, effectively increasing the number of functional spikes and enhancing infectivity, and to modulate structural rearrangements for membrane fusion. These findings extend our understanding of viral entry and suggest an improved immunogen for vaccine development.