The flexible, extended coil of the pdz-binding motif of the three deadly human coronavirus e proteins plays a role in pathogenicity
Abstract
The less virulent human (h) coronaviruses (CoVs) 229E, NL63, OC43, and HKU1 cause
mild, self-limiting respiratory tract infections, while the more virulent SARS-CoV-1, MERS-CoV, and
SARS-CoV-2 have caused severe outbreaks. The CoV envelope (E) protein, an important contributor
to the pathogenesis of severe hCoV infections, may provide insight into this disparate severity of the
disease. We, therefore, generated full-length E protein models for SARS-CoV-1 and -2, MERS-CoV,
HCoV-229E, and HCoV-NL63 and docked C-terminal peptides of each model to the PDZ domain
of the human PALS1 protein. The PDZ-binding motif (PBM) of the SARS-CoV-1 and -2 and MERSCoV
models adopted a more flexible, extended coil, while the HCoV-229E and HCoV-NL63 models
adopted a less flexible alpha helix.