IUBMB Life | 2021

Issue Highlights



Special approaches are necessitated for overcoming difficult viruses such as SARS-CoV-2, if rampant morbidity and mortality is to be prevented. In this issue, a decoy strategy is hypothesized, in which a fusion protein is created between the Hepatitis B surface antigen (HBsAg) and the N-terminal helix (NTH) of Angiotensin Converting Enzyme-2 (ACE2), the receptor for SARS-CoV-2. For vaccination, this decoy protein is to be administered together with whole inactivated virus. The NTH would bind to the Receptor Binding Domain of the inactivated SARS-CoV-2. Pre-existing or fresh neutralizing antibodies would bind to HBsAg. This antigen-antibody binding event closely linked to the inactivated virus would trigger immunity mechanisms to be developed efficaciously against the virus. The described decoy tactic could be a platform technology, in which HBsAg can be linked to the part of the cellular receptor that any new intractable virus binds to. The central mechanism for immune activation using the decoy fusion protein. A. The decoy fusion protein. Green: N-terminal helix of ACE2; Ochre: Peptide linker; Pink: The portion of HBsAg used in the recombinant Hepatitis B vaccine. B. Neutralizing antibodies against HBsAg. Yellow: Memory B cells or freshly primed B cells; Blue: Neutralizing antibodies, pre-existing or fresh. C. The binding events. Red: SARS-CoV-2 with spike protein having RBD which binds to NTH of ACE2.

Volume 73
Pages None
DOI 10.1002/iub.2556
Language English
Journal IUBMB Life

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