Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulation.

Ozturk, Onur; Kilinc, Evren; Irez, Batuhan Gorkem; Timucin, Emel

The Coronavirus Disease (COVID-19) pandemic, caused by Severe Acute Respiratory Syndrome coronavirus-2 (SARS-CoV-2), highlighted significant gaps in our understanding of the virus’s molecular structure, its biological properties, and the interactions between viral proteins and host biological systems, which have underscored the critical need for further research in this area. Coagulation disorders, particularly those leading to thromboinflammation, have been linked to severe complications in COVID-19 cases. The occurrence of thromboinflammation has likewise been corroborated in cases of both Severe Acute Respiratory Syndrome (SARS) and Middle East Respiratory Syndrome (MERS). In this study, we investigated the protein-protein interactions between the SARS-CoV-2 spike protein and fibrinogen, a glycoprotein that plays a crucial role in blood coagulation. Molecular docking analysis revealed key interactions between the β and γ subunits of fibrinogen and the spike protein. The findings suggest that these interactions may contribute to the understanding of the coagulation disorders observed in COVID-19 patients. This study provides insights into the molecular mechanisms underlying these disorders and identifies potential targets for the development of therapeutic interventions.

SARS-CoV-2; MIDDLE East respiratory syndrome; SARS disease; MOLECULAR structure; COVID-19

Medicine Science, 2024, Vol 13, Issue 4, p803

2147-0634

Academic Journal

10.5455/medscience.2024.08.099