NMR studies of active N-terminal peptides of stromal cell-derived factor-1: structural basis for receptor binding

2000 ◽  
Author(s):  
E. L. Elisseeva
Keyword(s):  
Receptor Binding ◽  
Stromal Cell ◽  
Structural Basis ◽  
Nmr Studies ◽  
Stromal Cell Derived Factor

scholarly journals NMR Studies of Active N-terminal Peptides of Stromal Cell-derived Factor-1

2000 ◽  
Vol 275 (35) ◽  
pp. 26799-26805
Author(s):  
Elena L. Elisseeva ◽  
Carolyn M. Slupsky ◽  
Matthew P. Crump ◽  
Ian Clark-Lewis ◽  
Brian D. Sykes
Keyword(s):  
Stromal Cell ◽  
Nmr Studies ◽  
Stromal Cell Derived Factor

scholarly journals Structural Basis of the Interaction between Chemokine Stromal Cell-derived Factor-1/CXCL12 and Its G-protein-coupled Receptor CXCR4

2009 ◽  
Vol 284 (50) ◽  
pp. 35240-35250 ◽  
Author(s):  
Yutaka Kofuku ◽  
Chie Yoshiura ◽  
Takumi Ueda ◽  
Hiroaki Terasawa ◽  
Takahiro Hirai ◽  
...  
Keyword(s):  
G Protein ◽  
Stromal Cell ◽  
Structural Basis ◽  
G Protein Coupled Receptor ◽  
Stromal Cell Derived Factor ◽  
G Protein Coupled

scholarly journals Stromal Cell-Derived Factor-1 Is Essential for Photoreceptor Cell Protection in Retinal Detachment

2010 ◽  
Vol 177 (5) ◽  
pp. 2268-2277 ◽  
Author(s):  
Hiroki Otsuka ◽  
Noboru Arimura ◽  
Shozo Sonoda ◽  
Makoto Nakamura ◽  
Teruto Hashiguchi ◽  
...  
Keyword(s):  
Retinal Detachment ◽  
Stromal Cell ◽  
Photoreceptor Cell ◽  
Cell Protection ◽  
Stromal Cell Derived Factor

scholarly journals Heparin Inhibits Cellular Invasion by SARS-CoV-2: Structural Dependence of the Interaction of the Spike S1 Receptor-Binding Domain with Heparin

2020 ◽  
Vol 120 (12) ◽  
pp. 1700-1715
Author(s):  
Courtney J. Mycroft-West ◽  
Dunhao Su ◽  
Isabel Pagani ◽  
Timothy R. Rudd ◽  
Stefano Elli ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Structural Changes ◽  
Rapid Development ◽  
Antiviral Agents ◽  
Vero Cells ◽  
Binding Domain ◽  
Microbial Pathogens ◽  
Minimum Size ◽  
Structural Basis ◽  
Receptor Binding Domain

AbstractThe dependence of development and homeostasis in animals on the interaction of hundreds of extracellular regulatory proteins with the peri- and extracellular glycosaminoglycan heparan sulfate (HS) is exploited by many microbial pathogens as a means of adherence and invasion. Heparin, a widely used anticoagulant drug, is structurally similar to HS and is a common experimental proxy. Exogenous heparin prevents infection by a range of viruses, including S-associated coronavirus isolate HSR1. Here, we show that heparin inhibits severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) invasion of Vero cells by up to 80% at doses achievable through prophylaxis and, particularly relevant, within the range deliverable by nebulisation. Surface plasmon resonance and circular dichroism spectroscopy demonstrate that heparin and enoxaparin, a low-molecular-weight heparin which is a clinical anticoagulant, bind and induce a conformational change in the spike (S1) protein receptor-binding domain (S1 RBD) of SARS-CoV-2. A library of heparin derivatives and size-defined fragments were used to probe the structural basis of this interaction. Binding to the RBD is more strongly dependent on the presence of 2-O or 6-O sulfate groups than on N-sulfation and a hexasaccharide is the minimum size required for secondary structural changes to be induced in the RBD. It is likely that inhibition of viral infection arises from an overlap between the binding sites of heparin/HS on S1 RBD and that of the angiotensin-converting enzyme 2. The results suggest a route for the rapid development of a first-line therapeutic by repurposing heparin and its derivatives as antiviral agents against SARS-CoV-2 and other members of the Coronaviridae.

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