key: cord-0053023-bg3qny8w
authors: Kumar, Amit; Saxena, Ajit Kumar; Lee, Gwo Giun (Chris); Kashyap, Amita; Jyothsna, G.
title: Comparing Proteomics of NCoV 19 and MERS Corona Virus
date: 2020-09-27
journal: Novel Coronavirus 2019
DOI: 10.1007/978-981-15-7918-9_3
sha: 01a9a280ee549279b61066f77c2f25fce240f483
doc_id: 53023
cord_uid: bg3qny8w

In order to develop any diagnostic or therapeutic protocol for COVID19 it is necessary to study the genome and proteome of the NCoV and annotate the proteins to identify its phylogeny and evolutionary relation with the other known organisms. The SARS NCoV and MERS Corona Virus belong to the Corona group of viruses and both are known to cause Respiratory illness. There is a very close similarity in the disease manifestation and mode of transmission in MERS and COVID forming basis for the comparison between the two organisms. Hence the proteins of novel Corona virus are compared with those of MERS Corona Virus (Fig. 3.1).

The above is the Proteomic sequence of ORF1AB of NCoV where, Yellow residues-Corona Rpol N domain Green residues-Viral Helicase Yellow + cyan + Green residues-Region sharing identity to the MERS CoV Proteome (Fig. 3.2) . (Fig. 3.3 ).

Inference: The above result shows that the query M protein shares 45.05% identity to MERS CoV M protein. This can impart some minor variation in the Membrane protein structure between the two pathogens ( Fig. 3.4) .

Inference: From the above BLAST result it can be inferred that the E protein shares a considerable similarity with the E protein of MERS CoV with query coverage of 94% and identity being 40% (Fig. 3.5 ). Inference: The above result shows that MERS CoV Nucleocapsid shares 50.26% identity to the N protein query with coverage of 88% (Fig. 3.6 ).

From the above comparative analysis between the structural proteins and ORF1ab (being the longest protein in the virus) of NCoV and MERS Corona Virus, it can be concluded that both the organisms share a considerable similarity though not very high. However the ORF1ab is the longest protein in the Query proteome and is found to share a great similarity to that of MERS Corona Virus. Thus the study can be focused on the annotation of ORF1ab protein and targeting it for the Drug Docking studies. Further chapters of the book focus on the complete structural and functional characterization of the ORF1ab polyprotein of Novel Corona virus 2019.

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