PMC:7299399 / 44430-45884 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7299399","sourcedb":"PMC","sourceid":"7299399","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7299399","text":"Gold NPs capped with mercaptoethanesulfonate are effective inhibitors of HSV type 1 infection as they mimic cell-surface-receptor heparan sulfate and, therefore, competitively bind to the virus. Interestingly, polyvalent sulfated Au NPs inhibit virus binding to the host cell dependent on their size. Nanoparticles of diameters equal to and larger than the virus diameter (in this case, the stomatitis virus) more efficiently inhibit the binding to cells than smaller particles. Most likely, larger NPs efficiently cross-link virions, whereas smaller NPs simply decorate the viral surface.126 Papp et al. found that gold NPs decorated with SA effectively inhibited the binding of influenza virus to the target cells. In this case, viral recognition via its surface protein hemagglutinin of SA on the host cell membrane was a prerequisite for cellular entry.127 More recently, Cagno et al. reported antiviral NPs (Au and iron oxide core) with long and flexible linkers mimicking HS that strongly bind and inactivate viruses such as respiratory syncytial virus in vitro and in vivo in a lung infection model and even led to irreversible viral deformation.53 Hence, there is ample evidence that biocompatible, functionalized NPs can act as broad-spectrum antivirals. Notably, the receptor-binding domain of the spike S1 protein of SARS-CoV-2 binds not only to ACE2 but also to heparin128 and, thus, might be targeted by similar approaches as outlined 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