Dark Proteome of Newly Emerged SARS-CoV-2 in Comparison with Human and Bat Coronaviruses

Rajanish Giri; Taniya Bhardwaj; Meenakshi Shegane; Bhuvaneshwari R. Gehi; Prateek Kumar; Kundlik Gadhave

The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.13.990598 doi: bioRxiv preprint Non-structural protein 2 (Nsp2). This protein functions by disrupting the host survival pathway via interaction with the host proteins Prohibitin-1 and Prohibitin-2 [128] . Reverse genetic deletion in the coding sequence of Nsp2 of the SARS virus attenuated little viral growth and replication and allowed the recovery of mutant virulent viruses. This indicates the dispensable nature of the Nsp2 protein for SARS viruses [129] . The sequence identity of the Nsp2 protein from SARS-CoV-2 with Nsp2s of Human SARS CoV and Bat CoV amounts to 68.34% and 68.97%, respectively (Supplementary Figure S2A) . We have estimated the mean PPIDs of Nsp2s of SARS-CoV-2, Human SARS CoV, and Bat CoV to be 5.17%, 2.04%, and 2.03% respectively (see Table 3 ). The per-residues predisposition for the intrinsic disorder of Nsp2s from SARS-CoV-2, Human SARS CoV, and Bat CoV are depicted in Figures 20A, 20B, and 20C . According to this analysis, the following regions in Nsp2 proteins are predicted to be disordered, residues 570-595 (SARS-CoV-2), residues 110-115 (Human SARS), and residues 112-116 (Bat CoV). As listed in Table 2 , and Supplementary Tables 7 and 8, Human SARS CoV does not contain MoRF while SARS-CoV-2 and Bat CoV have an N-terminally located MoRF region predicted by MoRFchibi_web.