The sequence alignment of SARS-CoV-2 ORF7a and SARS-CoV ORF7a shows that SARS-CoV-2 ORF7a has a conserved Ig-like β sandwich fold with seven β chains. Most of the sequence variation is distributed in the extracellular domain (8-residue variation), so the potential protein function is diversified. Interestingly, this part represents the internal disordered C-terminal region of the SARS-CoV ORF7a protein, which the 3D structure of the ORF7a protein of SARS implied . Western blot analysis with a specific anti-ORF7a antibody indicates that SARS-CoV ORF7a is a new structural protein in viral particles 131 . The deletion of nucleotides at specific sites leads to the fusion of ORF7a and ORF7b 132 . The rare Greek SARS-CoV-2 variant contains a premature stop codon in ORF7a, causing the protein to be truncated. Premature termination will abolish the 28 amino acids at the C-terminus of the ORF7a protein . This mutation may represent the continued adaptation of the virus to human cells 133 . The C-terminal truncation of ORF7a will undoubtedly produce sub-proteins with LBP activity. The extracellular domain mutation makes us worried that there may be short ORF7a that enhances LBP-like activity.