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Related Concept Videos

Conjugated Proteins02:50

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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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High-throughput Confocal Imaging of Quantum Dot-Conjugated SARS-CoV-2 Spike Trimers to Track Binding and Endocytosis in HEK293T Cells
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Controlling the SARS-CoV-2 spike glycoprotein conformation.

Rory Henderson1,2, Robert J Edwards3,4, Katayoun Mansouri3

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Summary

Researchers analyzed coronavirus spike (S) protein structures to understand mobility. They engineered SARS-CoV-2 S-protein constructs with controlled conformations for improved vaccine development.

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Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • The coronavirus (CoV) spike (S) protein is crucial for viral entry and a key target for vaccines.
  • S-protein's inherent flexibility and mobile domains create challenges for effective immune targeting and vaccine design.

Purpose of the Study:

  • To investigate the structural dynamics and conformational variability of beta-coronavirus (β-CoV) S-proteins.
  • To engineer SARS-CoV-2 S-protein constructs with stabilized conformations for enhanced vaccine potential.

Main Methods:

  • Structure-based vector analysis of available β-CoV S-protein structures.
  • Development of two soluble ectodomain constructs for the SARS-CoV-2 S-protein.

Main Results:

  • Distinct S-protein configurations were observed across different β-CoVs, despite conserved domain organization.
  • Engineered SARS-CoV-2 S-protein constructs demonstrated controlled locking of the receptor binding domain (RBD) in 'down' or stabilized 'up' states.

Conclusions:

  • S-protein conformation can be rationally controlled through protein engineering.
  • Engineered CoV S-proteins offer a promising framework for developing more effective vaccines against coronaviruses.