BREAKING NEWS! Scientist Discover That SARS-CoV-2 Also Has A PCSK9 Cleavage Site!
COVID-19 News - SARS-CoV-2 - PCSK9 Cleavage Site May 06, 2023 1 year, 7 months, 2 weeks, 2 days, 13 hours, 32 minutes ago
COVID-19 News: A groundbreaking study by a team of international researchers from India and the United States has unveiled a remarkable and distinct feature in the SARS-CoV-2 virus that sets it apart from its predecessors, SARS-CoV-1 and MERS.
This discovery could potentially revolutionize our understanding of the virus's pathogenicity and pave the way for more effective antiviral therapies.
The SARS-CoV-2 virus, responsible for the ongoing COVID-19 pandemic, has continued to confound scientists as it persistently evolves, becoming more virulent and harder to combat. While previous research has identified the presence of a furin cleavage site in the virus as covered in various journals and
COVID-19 News reports, a feature not found in SARS-CoV-1 and MERS, this new study reveals an additional proprotein convertase subtilisin kexin-9 (PCSK9) cleavage site within the Spike protein of SARS-CoV-2.
This unparalleled combination of PCSK9 and furin cleavage sites could hold the key to unlocking the virus's unique behavior and developing novel antiviral treatments.
The PCSK9 enzyme is predominantly expressed in the liver, small intestine, and kidneys and is involved in cholesterol and fatty acid homeostasis. Until now, the implications of PCSK9 in SARS-CoV-2 spike processing and viral entry have remained unexplored.
In the last three and a half years, despite many studies and research done, no one had detected the PCSK9 cleavage site in the SARS-CoV-2 virus's spike protein!
The discovery of the fact that SARS-CoV-2 has both the Furin and also the PCSK9 cleavage site, has profound implications for our understanding of SARS-CoV-2's pathogenicity and potential functional effects.
Proprotein convertases (PCs) are enzymes that cleave and activate precursor proteins, including those involved in viral infections. The furin protease, the most extensively studied PC, cleaves at specific sites in viral glycoproteins, facilitating viral envelope fusion with the host cell membrane and ultimately enabling the virus to deliver its genome into the host cell. Inhibiting this process can block viral replication, and PC inhibitors have shown promise as antiviral treatments for various severe infections.
The SARS-CoV-2 Spike protein is critical for the virus's ability to bind to host cell receptors ACE2 and CD26 and is a primary target for vaccine development. By uncovering the presence of the PCSK9 cleavage site alongside the furin cleavage site, this new research suggests that both sites could play a significant role in the virus's unique behavior and impact the development of antiviral drugs and vaccines.
The study conducted a comparative analysis of the Spike protein sequences from various coronaviruses, revealing that the non-basic PCSK9 cleavage site is also present in SARS-CoV-1, Bat CoV, and Rhinopus CoV. However, these distinctive amino acid residues are absent in Ruminant CoVs and Bovine CoVs.
This new finding challenges previous assumptions about the uniqueness of the furin cleavage site in SARS-CoV-2 and highlights the potential significance of the PCSK9 cleavage site in viral a
ctivation or infection.
In conclusion, this groundbreaking study has unveiled the presence of a unique PCSK9 cleavage site within the Spike protein of SARS-CoV-2, alongside the previously identified furin cleavage site. This unprecedented combination of cleavage sites suggests that SARS-CoV-2's pathogenicity, potential functional effects, and implications for antiviral drug development could be significantly influenced by these features. As the global scientific community continues to search for effective treatments and vaccines, understanding the complex interplay between these cleavage sites could be vital in combating the COVID-19 pandemic.
The study findings were published on a preprint server and are currently being peer reviewed.
https://www.biorxiv.org/content/10.1101/2023.05.04.539453v1
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