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Expressed as polyprotein comprising of 16 Nsps (mentioned below) |
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Binds to host 40S ribosome and promotes host cell RNA degradation, Blocks RIG-1-dependent antiviral immune response |
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Binds to host cell prohibitin 1 and 2 (PHB1 and PHB2) to disrupt host cell environment |
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1.
Releases Nsp1, Nsp2, and Nsp3 from the N-terminal region of polyproteins 1a and 1ab from CoVs for virus replication
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2.
Nsp3 interacts with TBK1 to inhibit potent type-1 IFN-based antiviral immune response
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Binds to Nsp3 and helps in virus replication |
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Cleaves at 11 sites of (3C-like proteinase) NSP polyprotein |
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Forms complex with Nsp8 and Nsp12 to yield NSP8 RNA polymerase activity |
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1.
Forms complex with Nsp7 and Nsp12 to act as RNA polymerase
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2.
Binds to TRIM59 to inhibit pro-inflammatory immune response
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3.
Nsp8 binds to LC3-II to get into autophagosome and then to autolysosomes for virus replication
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Interacts with DEAD-box RNA helicase 5 (DDX5) of host cell to increase viral replication |
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Activates NSP14 and NSP16, which are methyltransferases |
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Unknown |
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RNA-dependent RNA polymerase, forms complex with Nsp7 and Nsp8 |
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1.
Acts as an Helicase to unwind the duplex RNA, Nsp12 binding enhances its helicase activity
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2.
Also exerts 5′-trophosphatase activity for introducing 5′-terminal cap in the viral RNA
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3.
Blocks type 1 IFN release via binding to TBK1 and TBKBP1
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4.
Interacts with TLE3 and TLE4 to inhibit IL-6 and IL-12 release
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Exerts 3′-5′ exoribonucleaseactivity and N7-methyltransferase activity |
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1.
Acts as an endoribonuclease that cleaves RNA at uridylates at the 3-position to form a 2-3′cyclic phosphodiester product by using manganese (Mn) as a cofactor
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2.
Targets specifically, viral polyuridine sequences to prevent the virus recognition by the host innate immune system
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3.
Degrades viral RNA to escape from cytosolic or endosomal PRR-mediated recognition
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4.
Binds to RNF41 (RING finger protein 41)/Nrdp1 (an E3 ubiquitin-protein ligase) to inhibit IRF-3-dependent Type 1 IFN release
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5.
Binds to neuregulin receptor degradation protein 1 (Nrdp1, a E3 ubiquitin-protein ligase) to aggravate TLR signaling-dependent pro-inflammatory cytokines release
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Acts as a 2′‑O‑Ribose‑Methyltransferase and methylates the 2′-hydroxy group of adenine using S-adenosylmethionine (SAM) as the methyl source |
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Recognizes and binds to ACE2 receptor of the host cells to enter for replication and productive infection |
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1.
Interacts with TRAF3 to activate ASC for caspase-1 activation required for NLRP3 inflammasome to release pro-inflammatory cytokines (IL-1β and IL-18)
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2.
Binds to TRIM59 and inhibits NF-κB and ISRE-dependent antiviral immune response
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1.
Can for ion channel
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2.
Virus assembly
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3.
Virion release
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4.
Infection pathogenesis
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Interacts with Nsp8 to promote RNA polymerase activity |
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Accessory protein acting as a type 1 trans-membrane protein |
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Accessory protein, localizes to Golgi apparatus, may help in virus assembly |
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Comprises of ORF8a and ORF8b, binds to IRF association domain (IAD) of IRF3 via ORF8b to inhibit type 1 IFNs release |
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Interacts with NLRX1 and inhibits RLR and NLRP3-mediated innate immune response, but promotes TLR signaling-dependent pro-inflammatory immune response |
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Unknown |
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1.
Binds to viral RNA to increase its stability
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2.
Antagonizes host antiviral RNAi
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3.
Inhibits cyclin-dependent kinase (CDK) to block the S-phase progression of the cell cycle progression
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