As shown in Table , the SARS-COV-2 virus structural proteins (E, M, and N) and non-structural proteins (ORF3a, ORF6, ORF7a, ORF7b, ORF8, ORF10, and ORF1ab) contain the Plasmodium antigen's EBA-175 VI domain (PF11556). The EBA-175 VI domain encodes the red blood cell binding antigen 175, and this family represents region VI. EBA-175 interacts with glycophorin GPA, assisting in forming tight junctions, a necessary step for invasion. VI is a cysteine-rich domain that is required for EBA-175 trafficking. EBA-175 is an alpha helix-containing homodimer. N, ORF3a, and ORF8 all can form dimers. N's EBA-175 VI domain, on the other hand, is concise and does not contain cysteine. As a result, the EBA-175 VI domains of N, E, M, ORF6, ORF7a, ORF7b, and ORF10 are incapable of exhibiting complete GPA binding activity. ORF3a and ORF8 have EBA-175 VI domains that overlap with TryThrA_C domains, respectively. Thus, ORF3a and ORF8 may bind to the red blood cell membrane's glycophorin GPA via the Plasmodium antigen (EBA-175 VI) rich in the amino acid threonine.