ORF3a, nucleocapsid phosphoprotein (N), and envelop protein (E) of SARS-CoV-2 (COVID-19) have been demonstrated by conserved domain analysis that they had heme-associated sites [1]. Ile304 of N, Cys44 of E, and Arg134 of ORF3a were the heme-iron-linked sites, whereas ORF3a possessed the conserved domains of bacterial EFeB protein and human cytochrome C reductase and could dissociate the iron of heme to form porphyrin [1]. ORF3a was specific and did not attack peroxide, normal cytochrome C, and blue blood protein and it would increasingly cause less hemoglobin levels, so developing manifestations of coagulation reaction, respiratory distress, and finally damaging many tissues and organs [1]. ORF3a, ORF10, and orf1ab could attack the 1-beta chain of hemoglobin, whereas some non-structural and structural viral proteins could bind porphyrin [1]. Heme-linked sites of N protein and E protein may be associated with virus replication and high virus infectivity, respectively [1].

References

1. Liu W and Li H. “COVID-19: attacks the 1-beta chain of hemoglobin and captures the porphyrin to inhibit heme metabolism”. ChemRxiv. Cambridge: Cambridge Open Engage (2020).
2. Fouad SH., et al. “Comparison of hemoglobin level and neutrophil to lymphocyte ratio as prognostic markers in patients with COVID-19”. Journal of International Medical Research7 (2021): 1-15.
3. Dinevari MF., et al. “Anemia predicts poor outcomes of COVID-19 in hospitalized patients: a prospective study in Iran”. BMC Infectious Diseases 21 (2021): 170.

Citation

Citation: Attapon Cheepsattayakorn., et al. “Prediction of COVID-19 Severity by Hematological Parameters" Acta Scientific Microbiology 4.11 (2021): 82-94.

Copyright

Copyright: © 2021 Ansab Akhtar. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.