Key result
Peptides analogous to the aromatic domains of the SARS-CoV, MHV, and human CoV OC43 S2 subunits strongly partitioned into lipid membranes and induced lipid vesicle permeabilization.
The aromatic domain of the CoV S protein partitions into lipid membranes and induces permeabilization, suggesting a functional role in viral entry.
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Does not support clinical targeting of CoV S2 domains; leaves open a mechanistic role in viral entry pending cellular validation.
Sáinz et al. (2004) studied Coronavirus (CoV) entry. Peptides analogous to the aromatic domains of SARS-CoV, MHV, and human CoV OC43 S2 subunits was evaluated on Lipid vesicle permeabilization and partitioning into lipid membranes. Peptides analogous to the aromatic domains of the SARS-CoV, MHV, and human CoV OC43 S2 subunits strongly partitioned into lipid membranes and induced lipid vesicle permeabilization.
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