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. 2021 Apr 20;82:104503. doi: 10.1016/j.jff.2021.104503

Table 1.

Description of the viral proteins encoded by SARS-CoV-2 genome highlighting their role in the viral lifecycle and immune pathogenicity.

Viral proteins Characteristics Molecular functions References
Structural protein Spike-like surface glycoprotein MW ~ 150 kDa; 1273 amino acids; Rich in glutamine, asparagine, leucine, phenylalanine and serine amino acids S1 subunit facilitates hACE2-mediated virus attachment; S2 subunit promotes membrane fusion process into the host cell; help in promoting adhesion of infected cells with adjacent non-infected cells Astuti & Ysrafil, 2020; Bianchi et al., 2020; Chen et al., 2020; Satarker & Nampoothiri, 2020
Envelope glycoprotein MW ~ 8–12 kDa; 76–109 amino acids; Contains N Terminal Domain (NTD) and hydrophilic C Terminal Domain (CTD) Forms viriporins which is required for virion assembly and release
Membrane glycoprotein 220–260 amino acids; Contains hydrophilic C terminal and amphipathic N terminal Determine the shape of the virus envelope; helps to stabilize nucleocapsids and promotes completion of viral assembly by stabilizing N protein-RNA complex, inside the internal virion
Nucleocapsid protein Composed of a serine-rich linker region between NTD and CTD NTD forms orthorhombic crystals and binds to the viral genome; linker region regulate self- functioning; CTD promotes nucleocapsid formation; promotes the activation of COX-2 leading to inflammation in the lungs; inhibits IFN-1 causing restrictions in immune responses
Non-structural proteins NSP1 (Leader protein) Inhibit host mRNA translation, antagonize IFN signalling and induce inflammatory cytokines and chemokines Astuti & Ysrafil, 2020; Min et al., 2020; Samaddar et al., 2020; Yoshimoto, 2020, Zhang et al., 2020
NSP2 Binding to prohibitin-1 (PHB1) and prohibitin-2 (PHB2) leads to disruption of the host cell environment
NSP3 Encode papain-like protease (PLpro) that helps to cleave the site between NSP2 and NSP3 and release essential viral proteins for viral activity
NSP4 (Transmembrane domain 2) Interacting with NSP3 causes rearrangement of the host cell membrane
NSP5 Encode chymotrypsin-like protease (3CLpro/Mpro) that cleaves at 11 different sites to produce mature and intermediate viral polyproteins
NSP6 (Putative Transmembrane domain) Restricting autophagolysosome development cause hindrance of autophagosomes from transporting viral components for degradation in lysosomes
NSP7 (Peptide cofactor) Forms a complex NSP8 and NSP12 to yield RNA polymerase activity
NSP8 (Peptide cofactor) Forms hexadecameric complex of RNA polymerase
NSP9 Encode RNA-binding protein phosphatase that helps in viral genome replication and transcription
NSP10 Interacting with NSP14 and NSP16 to stimulate SAM-dependent methyltransferase activity and 2′-O-Ribosemethyltransferase activity respectively
NSP11 Unknown activity yet
NSP12 (RdRP) Encodes RNA-dependent RNA polymerase that replicates viral RNA
NSP13 (Helicase) Unwinds duplex RNA; elicits 5′-triphosphatase activity to introduce a 5′-terminal cap of mRNA
NSP14 (N7-methyltransferase) Proofreading of viral genome by endonuclease and methyltransferase activity
NSP15 (Endoribonuclease) Cleaves RNA at 3′-uridylates to form a 2′-3′ cyclic phosphodiester product that protects viral RNA from host recognition and inhibit innate response
NSP16 (2′-O-Ribosemethyltransferase) Methylate 2′-hydroxyadenine using SAM as methyl pool thereby avoid MDA5 recognition of viral RNA and inhibit innate immunity regulation