SARS-CoV-2 infectivity

ORF8 of SARS-CoV-2 as a promising target protein for COVID 19 treatment; Open Reading Frame 8 (ORF 8 as a unique protein is known to play key roles in host immune regulation and immune evasion Most striking of them are interaction with Major Histocompatibility Complex 1 (MHC 1), Interleukin 6 production and, the antagonistic effect on Interferon Regulatory transcription Factor 3 (IRF 3). We explore the molecular features of ORF 8 to find the potential hotspot binding sites of the protein for proposing appropriate inhibitors, especially among natural products.

NPs binding to ORF8 dimer, Mostafa Bagherifar et al. 2021

S494 O-glycoslation site on SARS-CoV-2 RBD; Since the COVID-19 outbreak, structural effects of glycosylation in the virion-host cell complex has been among the main subjects of my research work. In a collaborative project, molecular modeling tools were used to show that appearance of a novel glycosylation site on the Receptor Binding Domain of SARS-CoV-2 results in the increased affinity between the virion and the human ACE2 receptor.

S494 O-glycosylation site on the SARS-COV-2 RBD Affects the Virus Affinity to ACE2 and its Infectivity; A Molecular Dynamics Study; Shadi Rahnama et al. 2021.
N-glycosylated SARS-CoV-2 RBD and
N-glycosylated SARS-CoV RBD. The N glycans are distant from the ACE2 binding site.

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