1. Reduction of hemagglutination induced by a SARS-CoV-2 spike protein fragment using an amyloid-binding benzothiazole amphiphile.
- Author
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Li, Meihan, Castro Lingl, Sascha, and Yang, Jerry
- Subjects
Spike Glycoprotein ,Coronavirus ,Humans ,Benzothiazoles ,SARS-CoV-2 ,COVID-19 ,Hemagglutination ,Amyloid ,Protein Binding ,Erythrocytes ,Peptide Fragments - Abstract
COVID-19 infection is associated with a variety of vascular occlusive morbidities. However, a comprehensive understanding of how this virus can induce vascular complications remains lacking. Here, we show that a peptide fragment of SARS-CoV-2 spike protein, S192 (sequence 192-211), is capable of forming amyloid-like aggregates that can induce agglutination of red blood cells, which was not observed with low- and non-aggregated S192 peptide. We subsequently screened eight amyloid-binding molecules and identified BAM1-EG6, a benzothiazole amphiphile, as a promising candidate capable of binding to aggregated S192 and partially inhibiting its agglutination activity. These results provide new insight into a potential molecular mechanism for the capability of spike protein metabolites to contribute to COVID-19-related blood complications and suggest a new therapeutic approach for combating microvascular morbidities in COVID-19 patients.
- Published
- 2024