Our findings demonstrate that it is possible for a single small molecule to inhibit the binding of viruses that depend on heparan sulfate or on sialic acid for attachment, which opens the possibility to develop truly broad-spectrum antivirals targeting primary attachment.
A Small Molecule Inhibits Virion Attachment to Heparan Sulfate- or Sialic Acid-Containing Glycans
Che C. Colpittsb,c and Luis M. Schang a,b,c
L. Hutt-Fletcher, Editor
aDepartment of Biochemistry, University of Alberta, Edmonton, AB, Canada
bLi Ka Shing Institute of Virology, University of Alberta, Edmonton, AB, Canada
cDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB, Canada
Corresponding author.
Address correspondence to Luis M. Schang, ac.atreblau@gnahcs.siul.
Author information Article notes Copyright and License information
ncbi.nlm.nih.gov
Broad spectrum! Just what I have been looking for all these years!!!!
BroadSpectrumCides - about to go IPO!!!!?
Epigallocatechin gallate (EGCG), a green tea catechin, is active against many unrelated viruses, including several that bind to heparan sulfate or to sialic acid. We sought to identify the basis for the broad-spectrum activity of EGCG. Here, we show that EGCG inhibits the infectivity of a diverse group of enveloped and nonenveloped human viruses. EGCG acts directly on the virions, without affecting the fluidity or integrity of the virion envelopes. Instead, EGCG interacts with virion surface proteins to inhibit the attachment of HSV-1, HCV, IAV, vaccinia virus, adenovirus, reovirus, and vesicular stomatitis virus (VSV) virions. We further show that EGCG competes with heparan sulfate for binding of HSV-1 and HCV virions and with sialic acid for binding of IAV virions. Therefore, EGCG inhibits unrelated viruses by a common mechanism. Most importantly, we have identified EGCG as the first broad-spectrum attachment inhibitor. Our results open the possibility for the development of small molecule broad-spectrum antivirals targeting virion attachment.
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