Related Experiment Video
Updated: Nov 12, 2025
13:00
Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
2.5K
Structural impact on SARS-CoV-2 spike protein by D614G substitution
Jun Zhang1,2, Yongfei Cai1,2, Tianshu Xiao1,2
1Division of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
Science (New York, N.Y.)
|March 17, 2021
Summary
The G614 variant of SARS-CoV-2 spike protein enhances viral spread and infectivity. Structural analysis reveals a stabilizing loop interaction in the G614 spike, improving vaccine immunogen design.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- The G614 substitution in the SARS-CoV-2 spike protein is associated with increased viral transmissibility.
- Understanding the structural basis of G614's enhanced infectivity is crucial for developing effective vaccines and therapeutics.
Purpose of the Study:
- To determine the cryo-electron microscopy structures of the full-length G614 spike protein trimer.
- To elucidate the structural differences between the D614 and G614 spike proteins and their functional implications.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was used to resolve the structures of the G614 spike trimer.
- Comparative structural analysis was performed between D614 and G614 spike protein conformations.
Main Results:
- The G614 spike trimer adopts three distinct prefusion conformations, differing in receptor-binding domain positioning.
- A novel loop interaction in the G614 spike stabilizes the trimer, increasing functional spikes and infectivity.
- This stabilization modulates structural rearrangements essential for viral membrane fusion.
Conclusions:
- The G614 substitution enhances SARS-CoV-2 infectivity through increased trimer stability.
- Structural insights into the G614 spike protein can inform the design of improved immunogens for vaccine development.
Related Concept Videos
02:28Leaky Scanning
5.4K
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...
5.4K
02:50Conjugated Proteins
23.3K
Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
23.3K
01:05Single Nucleotide Polymorphisms-SNPs
17.3K
A single nucleotide polymorphism or SNP is a single nucleotide variation at a specific genomic position in a large population. It is the most prevalent type of sequence variation found in the human genome. Point mutations that occur in more than 1% of the population qualify as SNPs. These are present once every 1000 nucleotides on an average in the human genome. Replacement of a purine with another purine (A/G) or a pyrimidine with another pyrimidine (C/T) is known as a transition. In contrast,...
17.3K