The flexible, extended coil of the pdz-binding motif of the three deadly human coronavirus e proteins plays a role in pathogenicity

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dc.contributor.authorSchoeman, Dewald
dc.contributor.authorCloete, Ruben
dc.contributor.authorFielding, Burtram C.
dc.date.accessioned2022-09-06T10:05:52Z
dc.date.available2022-09-06T10:05:52Z
dc.date.issued2022
dc.description.abstractThe 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.en_US
dc.identifier.citationSchoeman, D. et al. (2022). The flexible, extended coil of the pdz-binding motif of the three deadly human coronavirus e proteins plays a role in pathogenicity. Viruses, 14(8), 1707. https://doi.org/10.3390/v14081707en_US
dc.identifier.issn1999-4915
dc.identifier.urihttps://doi.org/10.3390/v14081707
dc.identifier.urihttp://hdl.handle.net/10566/7816
dc.language.isoenen_US
dc.publisherMDPIen_US
dc.subjectHuman coronavirusesen_US
dc.subjectCovid-19en_US
dc.subjectSARS-CoV-2en_US
dc.subjectProteinen_US
dc.subjectBioscienceen_US
dc.titleThe flexible, extended coil of the pdz-binding motif of the three deadly human coronavirus e proteins plays a role in pathogenicityen_US
dc.typeArticleen_US

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