Negatively charged residues in the membrane ordering activity of SARS-CoV-1 and -2 fusion peptides.

ABSTRACT: Entry of coronaviruses into host cells is mediated by the viral spike protein. Previously, we identified the bona fide fusion peptides (FPs) for severe acute respiratory syndrome coronavirus ("SARS-1") and severe acute respiratory syndrome coronavirus-2 ("SARS-2") using electron spin resonance spectroscopy. We also found that their FPs induce membrane ordering in a Ca²⁺-dependent fashion. Here we study which negatively charged residues in SARS-1 FP are involved in this binding, to build a topological model and clarify the role of Ca²⁺. Our systematic mutation study on the SARS-1 FP shows that all six negatively charged residues contribute to the FP's membrane ordering activity, with D812 the dominant residue. The corresponding SARS-2 residue D830 plays an equivalent r

SUBMITTER: Lai AL 

PROVIDER: S-EPMC8683214 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature