In this present study, we used the domain search method to find that many proteins of the SARS-COV-2 virus have MHC-like structures. It indicates that SARS-COV-2 interferes with antigen presentation and attacks immune cells through the MHC-like systems. The SARS-COV-2 virus protein with MHC-like forms could interfere with the antigen presentation response by binding to the MHC receptor of immune cells. The SARS-COV-2 virus employees the MHC-like structures of the S protein as bait. After the SARS-COV-2 S protein binds to CD4 + T, CD8 + T, and NK cells, the oxygen-free radicals(ROS) generated by the E protein destroys these immune cells, resulting in a decrease in the number of lymphocytes. Through the analysis of the MHC-like enhanced regions of existing popular variants, we found that: 127-194 and 144-162 areas of S viral proteins in Table . Table shows the structural proteins (S, E, N, M) and non-structural proteins (ORF3a, ORF6, ORF7a, ORF7b, ORF8, ORF10, ORF1ab) of SARS-COV-2 all have Ig-like domains. Ig-like (IPR032165) is a domain composed of approximately 100 residues. Smaller domains (74-90 residues) are observed in several Ig-related molecules (CD2, CD4). The Ig-like motifs of ORF10, E , some subprotein of ORF1ab are the short. ORF7a Ig-like A, ORF8 Ig-like A, ORF3a Ig-like C, N Ig-like B and C, M Ig-like A and C, S Ig-like B and H, 3'-to-5' exonuclease C, 3'-to-5' exonuclease C, helicase B motifs are longer. The Ig-like structures may help the receptor of CD4 + T, CD8 + T, and NK cell recognize the MHC-like area of the viral proteins.