The N15Y mutation in the E protein of severe acute respiratory syndrome coronavirus 2 affects the binding of doxycycline and rutin

Ali Adel Dawood; Bassam Ismael Jasim; Omar Al-jalily

2022, Number 3

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VacciMonitor 2022; 31 (3)

The N15Y mutation in the E protein of severe acute respiratory syndrome coronavirus 2 affects the binding of doxycycline and rutin

Dawood AA, Jasim BI, Al-jalily O

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Language: English
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ABSTRACT

The severe acute respiratory syndrome coronavirus 2 genetic variation must be closely monitored. Viral transmission can inevitably result from mutations in the viral genome and functional proteins that aid in the virus's adaptation to the host. This study aimed to look for mutations in the E protein and see how they affected the ligands' molecular docking. Mathematical saturation mutagenesis and other informatics techniques were used. Fourteen severe acute respiratory syndrome coronavirus 2 isolates from Iraq were selected. Doxycycline and rutin were chosen as ligands. In four strains of severe acute respiratory syndrome coronavirus 2, the N15Y mutation was detected in the envelope protein. Depending on the calculation of the amount of energy of the atoms, this mutation is critical in modifying the shape of the protein as well as increasing protein stability. In the single-chain mutation, one pocket was determined, while all pentamer chains had two pockets. The N15Y mutation altered the degree of doxycycline binding by affecting the residue of attachment of the ligands. It also altered the position of the rutin's attachment to the E protein, which has a clear impact on the virion particle.

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