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The copyright holder for this preprint (which was not peer-reviewed) is the .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 M protein of SARS-CoV-2 has a sequence similarity of 90.1% with Bat CoV and 89.6% with Human SARS M proteins ( Figure 5B ). Our analysis revealed that the intrinsic disorder levels in M proteins of SARS-COV-2, Human SARS CoV, and Bat CoV are relatively low since these proteins show the PPID values of 2.70%, 1.36%, and 1.36% respectively. This is in line with the previous publication by Goh et al. on Human SARS HKU4 where they found the mean PPID of 4% using additional predictors such as TopIDP and FoldIndex along with the predictors used in our study [74] . Figures 5C, 5D , and 5E represent per-residue disorder profiles generated for M proteins of SARS-CoV-2, Human SARS CoV, and Bat CoV and show that with the exception to their N-and C-terminal regions, these proteins are mostly ordered. The last 20 residues of MERS-CoV M protein are important for intracellular trafficking and contains a determinant that localizes it into the Golgi network [75] . Our results in Table 2 illustrates that the disordered C-tail of the M protein is predicted to have disorder based protein-binding region and therefore can serve as a binding site for its specific partner required for its localization inside the host cell. A long MoRF region (residues 186-220) at the C-terminal of M protein in all three viruses were observed by MoRFchibi_web. Two MoRF regions (one at N-terminus (residues 1-16) and one at C-terminus (residues 205-author/funder. All rights reserved. No reuse allowed without permission.