id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-314679-lmfalzni	Sangith, Nikhil	Unique Fibrinogen-binding motifs in the Nucleocapsid Phosphoprotein of SARS CoV-2: Potential Implications in Host-Pathogen Interactions	2020-06-24		.txt	text/plain	585	43	43	title: Unique Fibrinogen-binding motifs in the Nucleocapsid Phosphoprotein of SARS CoV-2: Potential Implications in Host-Pathogen Interactions This report describes the presence of two unique motifs in the SARS CoV-2 nucleocapsid phosphoprotein (N-protein) that can potentially interact with fibrinogen and possibly prothrombin. aureus)coagulase, Efb (Extracellular fibrinogen binding) and vWBP (von Willebrand factor Binding Protein), which are known to regulate the blood clotting cascade and the functions of host immune response. aureus proteins, the N-protein of this virus can mimic their functions, which may in turn play a crucial role in formation of blood clots in the host and help the virus evade host immune response. The role of the fibrinogen-binding motif of N-protein in formation of blood clots and 142 mimicking functions of Efb for pathogen survival in host will be investigated. Staphylococcus aureus secretes coagulase 187 and von Willebrand factor binding protein to modify the coagulation cascade and establish 188 host infections	./cache/cord-314679-lmfalzni.txt	./txt/cord-314679-lmfalzni.txt