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. 2021 Oct 23;14:5475–5487. doi: 10.2147/JIR.S329697

Table 2.

Comparing Protein Differences in Coronavirus

Types of Protein SARS-CoV MERS-CoV SARS-CoV-2
Spike protein (S) S protein can bind to ACE2 directly, and the binding sequence site is highly consistent with SARS-CoV-2.60 The core structure of the S2 gene of SARS-CoV is very similar, but the structure of the receptor-binding motif is quite different, so its receptor is dipeptidyl peptidase.57 Compared with SARS-CoV, the receptor-binding domain sequence homology of S protein is 76%.60 Its S protein also participates in the process of virus invasion by binding to the ACE2 receptor.61
Envelope protein (E) E protein acts as an ion channel in the form of a pentamer.58 Control virion assembly, deletion mutants lose pathogenicity.58,62 Compared with SARS-CoV, the sequence homology of E protein is as high as 95%.60 It is suggested that the functional diversity of E protein in the process of coronavirus replication and pathogenesis.
Membrane protein (M) M protein is only expressed in the endoplasmic reticulum and Golgi matrix. Its conserved domain participates in the process of virus assembly and budding through protein-protein interaction.53 Control virion assembly.63 Compared with SARS-CoV, the homology is as high as 91%.60 The specific function is not clear.
Nucleocapsid protein (N) Serum cross-reaction can occur through N protein.64 It can fold the coronavirus genome into a spiral ribonucleoprotein (RNP). At the same time, it can also enhance the efficiency of virus transcription and assembly.65 Compared with SARS-CoV, the homology is as high as 94%.60 It is possible to recognize the N protein of SARS-CoV in the COVID-19 patient’s serum and this can be used for clinical detection of asymptomatic patients.
Open reading frames (ORFs) ORF3b ORF3b protein is meaningless in the process of SARS-CoV replication.51 It can inhibit the IFN-β signal pathway and does not depend on protein nuclear localization.60 Nonstructural protein, no difference. A specific protein with four helical structures was found in the fragment of ORF3b protein, and there was no homologous sequence with SARS-CoV.60
ORF8 ORF8 protein can activate intracellular stress signals and cause an NOD-like receptor protein 3 (NLRP3) inflammatory response.66 Nonstructural protein, no difference. Compared with SARS-CoV, ORF8 has a 20% homology, which is the lowest homologous protein but can mediate the downregulation of host cell MHC-II.67