Table 2.
Different targets of SARS-CoV2 proteins. SARS-CoV2 is comprised of several proteins, which interact with diverse components in the host cell. Here is the summary of key protein interactors and functional deficits by different protein components of SARS-CoV2 [44]
| SARS-CoV-2 proteins | Key host protein interactors and functional perturbances |
|---|---|
| Spike protein | Palmitoylation of Spike protein through protein acyltransferase |
| Envelope protein | Epigenetic regulation of immunoregulatory genes and cell cycle by interacting with bromodomain extra terminal proteins (BET) |
| Membrane protein | Mitochondrial metabolism, solute transport, and ER morphology |
| Nucleocapsid protein | Regulation of stress granule |
| Nsp1 | Suppression of host antiviral response interacts with DNA polymerase and Plakophilin |
| Nsp2, Nsp3 | Translational repression |
| Nsp4 | Stabilization of double-membrane vesicle in the cytoplasm |
| Nsp5 | Epigenetic regulation of histones interacts with HDAC2 |
| Nsp6 | Dysregulation of autophagosome fusion with the lysosome |
| Nsp7 | Interacts with proteins of electron transport, membrane trafficking, and GPCR signaling. |
| Nsp8 | Interacts with the mitochondrial ribosome, signal recognition particle, and exosomes |
| Nsp9 | Interacts with Nuclear pore complex and Fibrillin |
| Nsp10 | Might hijack clathrin endocytosis processes, interacts with endoplasmic reticulum and Golgi apparatus |
| Nsp11 | Interacts with tubulin folding pathway proteins |
| Nsp12 | Interacts with proteins of the spliceosome |
| Nsp13 | Interacts with Golgi, centrosome, and Protein Kinase A signaling proteins |
| Nsp14 | Its methyltransferase activity assists in the capping of viral mRNA interact with the purine metabolism pathway |
| Nsp15 | Interacts with nuclear-cytoplasmic transport and protein trafficking |
| Nsp16 | Modifies the cap structure of viral mRNA, alters the antiviral response |
| Orf3a | Contributes to pulmonary pathology, disturbance of heme metabolism, autophagosome maturation, and ER stress |
| Orf3b | Interferon antagonist interacts with cardiolipin biosynthesis |
| Orf6 | Interferon antagonist interacts with nuclear pore proteins |
| Orf7a | Interacts with nuclear chaperone and transport of ribosomal proteins |
| Orf8 | Induces ER stress, interacts with ECM organization, glycosylation, and glycosaminoglycan synthesis |
| Orf9b | Dampens interferon response by degrading Mitochondrial antiviral-signaling protein (MAVS) |
| Orf9c | Interacts with proteins of electron transport and GPI-anchor biosynthesis |
| Orf10 | Degrades viral restriction factors through the hijacking of Cul2 complexes |