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- W4383092885 abstract "The target for humoral immunity, SARS-CoV-2 spike glycoprotein, has become the focus of vaccine research and development. Previous work demonstrated that the N-terminal domain (NTD) of SARS-CoV-2 spike binds biliverdin-a product of heme catabolism-causing a strong allosteric effect on the activity of a subset of neutralizing antibodies. Herein, we show that the spike glycoprotein is also able to bind heme (KD = 0.5 ± 0.2 μM). Molecular modeling indicated that the heme group fits well within the same pocket on the SARS-CoV-2 spike NTD. Lined by aromatic and hydrophobic residues (W104, V126, I129, F192, F194, I203, and L226), the pocket provides a suitable environment to stabilize the hydrophobic heme. Mutagenesis of N121 has a substantive effect on heme binding (KD = 3000 ± 220 μM), confirming the pocket as a major heme binding location of the viral glycoprotein. Coupled oxidation experiments in the presence of ascorbate indicated that the SARS-CoV-2 glycoprotein can catalyze the slow conversion of heme to biliverdin. The heme trapping and oxidation activities of the spike may allow the virus to reduce levels of free heme during infection to facilitate evasion of the adaptive and innate immunity." @default.
- W4383092885 created "2023-07-05" @default.
- W4383092885 creator A5010028189 @default.
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- W4383092885 date "2023-08-01" @default.
- W4383092885 modified "2023-09-30" @default.
- W4383092885 title "Heme binding to the SARS-CoV-2 spike glycoprotein" @default.
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- W4383092885 doi "https://doi.org/10.1016/j.jbc.2023.105014" @default.
- W4383092885 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37414149" @default.
- W4383092885 hasPublicationYear "2023" @default.
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