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http://hdl.handle.net/123456789/1652
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DC Field | Value | Language |
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dc.contributor.author | Sangwan, J | - |
dc.contributor.author | Tripathi, S | - |
dc.contributor.author | Yadav, N | - |
dc.contributor.author | Kumar, Y | - |
dc.date.accessioned | 2024-10-14T06:51:14Z | - |
dc.date.available | 2024-10-14T06:51:14Z | - |
dc.date.issued | 2022-12 | - |
dc.identifier.uri | http://hdl.handle.net/123456789/1652 | - |
dc.description.abstract | SARS-nCoV was identifed as corona virus had spread worldwide very quickly and afected more than million people world wide. To halt this acceleration and for efcient control the knowledge on genomic information is of utmost importance. We attempted to determine the nature of variation i.e., insertion, deletion, substitution, among structural sequences required to code for membrane, spike, nucleocapsid, envelope protein and glycosylation variation between SARS CoV and SARS nCoV spike glycoproteins, respectively. Comparative sequence analysis was performed by using retrieved sequences from the NCBI database. The analyzed sequences revealed, that the sequences coding for envelope protein show minor substituting amino acids. SARS CoV showed 94.74 percent amino acid identities with SARS nCoV amino acid sequences coding for envelope protein. In comparison to SARS nCoV, distinct amino acid residues vary in SARS CoV sequences coding for membrane, nucleocapsid, and spike proteins, respectively. S protein coding sequences of SARS CoV exhibited one deletion, six inser tion and six hundred three substitutions in SARS nCoV sequence. Insertion of valine was found in receptor binding domain of SARS nCoV at position 487, and NSPR amino acid residues at position 683–686. Deletions and substitutions were also found in nucleotide sequences of strain B.1.617.2 of SARS nCoV. Additionally, binding interaction pattern of ACE2 receptor protein with original wild-type SARS-CoV-2 strain with the recently evolved Omicron variant was also evaluated. The dock ing results substantiated that the specifc variation in binding residues is likely to impact virulence pattern of both variant. | en_US |
dc.title | Comparative sequence analysis of SARS nCoV and SARS CoV genomes for variation in structural proteins | en_US |
Appears in Collections: | School of Interdisciplinary & Applied Sciences |
Files in This Item:
File | Description | Size | Format | |
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Comparative sequence analysis of SARS nCoV and SARS CoV genomes for variation in structural proteins.pdf | 3.28 MB | Adobe PDF | View/Open |
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