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Lab.Equipment has curated a new article from the Biotech industry for you. This one is published by GEN:
The sugary coatings on viral proteins aren’t just for decoration. They influence how the proteins fold, thus contributing to protein function. They can also protect viral proteins, shielding them from the immune system. If these sugary coatings could be “seen,” the entire protein-sugar confection—the glycoprotein—could be targeted by designers of antiviral drugs and vaccines. Unfortunately, glycoproteins keep their glycans hidden from cryo-electron microscopy or X-ray crystallography, which are most adept at seeing proteins. To espy a protein’s glycans, another technique is needed: mass spectrometry.
All these techniques have been used to investigate SARS-CoV-2, the causative agent of COVID-19. Special attention has been paid to SARS-CoV-2’s “spike,” a protein complex that is composed of three protomers. It protrudes from the virus and binds to the ACE2 receptor on the surfaces of human cells.
Each protomer harbors 22 chemical sites that can undergo glycosylation, a biochemical reaction that adds a glycan compound to a protein. How these sites are glycosylated may affect which cells the virus can infect. The same processes could also shield some regions on the spike from being neutralized by antibodies.
Much has been learned about the spike through cryo-electron microscopy or X-ray crystallography, but studies taking advantage of mass spectrometry have lagged. Thus, a lot more is known about the spike’s proteins than its sugars. To help close the protein-sugar gap, scientists based at the University of Southampton, the University of Oxford, and the University of Texas at Austin have resorted to mass spectrometry.
These scientists, led by the University of Southampton’s Max Crispin, PhD, described their work in a paper (“Site-specific glycan analysis of the SARS-CoV-2 spike”) that appeared May 4 in... Want to read more? Visit the GEN – Genetic Engineering and Biotechnology News Blog.
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