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Nikhil Prasad  Fact checked by:Thailand Medical News Team Apr 21, 2024  1 week, 5 days, 13 hours, 36 minutes ago

Marine Sulfated Glycans Inhibit The Interaction Of Heparin With S-Protein Of SARS-CoV-2 Omicron XBB Variants

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Marine Sulfated Glycans Inhibit The Interaction Of Heparin With S-Protein Of SARS-CoV-2 Omicron XBB Variants
Nikhil Prasad  Fact checked by:Thailand Medical News Team Apr 21, 2024  1 week, 5 days, 13 hours, 36 minutes ago
COVID-19 News: The emergence of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has led to a global pandemic, resulting in millions of deaths worldwide. The virus's ability to mutate and produce variants, such as the Omicron XBB variant, poses significant challenges for public health efforts. One key aspect of SARS-CoV-2 infection is its interaction with host cells through heparan sulfate (HS) glycosaminoglycan (GAG), highlighting the importance of targeting this interaction for antiviral therapeutics.


Marine Sulfated Glycans Inhibit The Interaction Of Heparin With
S-Protein Of SARS-CoV-2 Omicron XBB Variants


Marine Sulfated Glycans: A Potential Solution
Marine organisms have long been studied for their bioactive compounds, including sulfated glycans, which exhibit diverse therapeutic properties. Researchers from Beibu Gulf University in China, Rensselaer Polytechnic Institute in the USA, Zhejiang University of Technology in China, Pusan National University in the Republic of Korea, and The University of Mississippi in the USA explored the potential of marine-sourced sulfated glycans as inhibitors of SARS-CoV-2's interaction with heparan sulfate HS. The findings of that study are covered in this COVID-19 News report.
 
Methodology: Evaluating Inhibitory Activity
The study focused on assessing the inhibitory activity of 10 marine-derived sulfated glycans on the interaction between the receptor-binding domain (RBD) of the S-protein of SARS-CoV-2 and heparin. These glycans, including sulfated fucans, fucosylated chondroitin sulfates, and fucoidans from various marine sources, were chosen for their structural similarity to HS and potential to interfere with viral entry.
 
Surface Plasmon Resonance (SPR): Uncovering Binding Affinities
Surface Plasmon Resonance (SPR) was employed as the analytical technique to evaluate the binding affinity between the SARS-CoV-2 S-protein variants (WT and XBB.1.5) and heparin, as well as the inhibitory effects of marine-sourced sulfated glycans. SPR provides real-time insights into biomolecular interactions, making it a valuable tool for drug discovery and development.
 
Results: Inhibition of Viral Binding
The study revealed strong binding between both WT and XBB.1.5 variants of the S-protein and heparin, indicating the critical role of HS in viral attachment. Importantly, all tested marine-sourced sulfated glycans exhibited significant inhibition of S-protein binding to heparin. This suggests that these compounds have the potential to disrupt viral entry into host cells, making them promising candidates for antiviral therapeutics.
 
Discussion: Implications for Antiviral Development
The findings underscore the potential of marine-derived sulfated glycans as inhibitors of SARS-CoV-2's interaction with host cells. By targeting the virion-HS interaction, these compounds offer a novel approach to comb ating the virus and its variants. Further research may focus on elucidating the mechanisms of action of these marine-derived inhibitors and optimizing their therapeutic efficacy.
 
Conclusion: Harnessing Marine Resources for Antiviral Strategies
In conclusion, the study highlights the promising role of marine-sourced sulfated glycans in inhibiting the interaction between SARS-CoV-2 S-proteins and HS. This research contributes to the ongoing efforts to develop effective antiviral therapeutics and underscores the value of exploring natural marine resources for novel drug discovery. Future studies may lead to the development of marine-derived inhibitors as part of a broader strategy to combat SARS-CoV-2 and other related viruses.
 
The study findings were published in the peer reviewed journal: Glycoconjugate Journal (Springer Link).
https://link.springer.com/article/10.1007/s10719-024-10150-1
 
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