Download In vitro analyses have found that SARS-COV-1 nsp1 may disrupt the host interferon defense response, by potentially affecting the downstream defense signaling. The nsp1 protein has been shown to bind the 40S Ribosomal subunit, which has been associated with degradation of host mRNA, and suppression of host mRNA translation, leaving the viral RNA unaffected. […]
Download The specific role of nsp2 has not been established; it may be that nsp2 assists other viral proteins in performing their function, such as regulating the autophagy defense response or promoting mitochondrial dysfunction, thereby helping viral replication or effecting disease severity. Some evidence links nsp2 to mitochondrial dysfunction and autophagy via prohibitin 1 (PHB1), […]
Download The nonstructural protein 3 (nsp3) acts as a phosphatase and its catalytic domain is conserved, sharing homology with yeast, archaea, and E. coli. The papain-like protease domain of nsp3 is implicated in inhibiting components of NF-κB, interferon-beta, and p53, thereby disrupting the host immune response. A substitution in SARS-CoV-2 likely intensifies the interaction with […]
Download The nonstructural protein 4 (nsp4) is essential for membrane rearrangements during viral replication in a mechanism involving nsp3. Nsp4 is thought to be a tetra spanning transmembrane protein and disruption in glycosylation sites within the luminal loop give rise to aberrant double membrane vesicles. Structural information about nsp4 is scarce, thus a low-resolution model […]
Download The nonstructural protein 5 (nsp5, also known as 3CLpro), is the main protease of the coronavirus genome, exhibiting as main known role the cleavage of the polyproteins translated from the viral RNA viral. Dimerization of SARS-CoV-1 3CLpro is essential to stabilize the catalytic site. The dimer interface is highly conserved within SARS-CoV-1 and -CoV-2, […]
Download Nsp6, along with nsp3 and nsp4, plays a critical role in membrane rearrangement. In SARS-CoV-1 nsp6 is known to activate autophagy by inducing perinuclear vesicles localized around the microtubule organization center. SARS-CoV-2 nsp6 is 87% identical to SARS-CoV-1 nsp6. Non-conservative mutations are located on the protein surface. Narrative Upon infection, corona viruses create signature […]
Download NSP7 Download NSP8 Download NSP12 The complex formed by nsp7, 8, 9, 10, and 12 is responsible for the replication and transcription of the viral genome. Nsp12 encodes the RNA-dependent RNA polymerase (RdRp) domain. Nsp7 forms a hexadecameric complex with nsp8 that may act as a processivity clamp for the RNA polymerase. When compared […]
Download Nsp9 is able to form dimers that bind either ssDNA and ssRNA and is thought to protect the coronavirus genome from degradation during replication. Deletion of nsp9 in the mouse β-coronavirus (hepatitis virus , MHV), impairs viral RNA synthesis and viral infection. SARS-CoV-1 and SARS-CoV-2 nsp9 sequences are highly conserved, but substitutions with potential […]
Download NSP10 Download NSP14 The exonuclease domain of nsp14 is imperative for replication fidelity within RNA viruses and has been shown to function as a proofreading exoribonuclease. Nsp14 associates with nsp10 that provides the ability to excise mismatched nucleotides, and disruption of this heterodimer was shown to decrease replication fidelity. SARS-CoV-1 and -CoV-21 nsp10 proteins […]
Download Nsp11 is a short peptide (13 a.a.) and is cleaved from both polyproteins pp1a and pp1ab. In SARS-CoV-1 nsp11 has been implicated in RNA synthesis. SARS-CoV-2 nsp11 has 85% sequence identity to SARS-CoV-1 nsp11. Narrative Nsp11 is a short protein only 13 a.a. in length and is translated from both polyproteins ORF1a and ORF1ab. […]
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