The slight sequence similarity suggests that ORF8 and ORF7a have the same immunoglobulin-like fold, confirmed by structural determination . The SARS-CoV Ig-like virus protein ORF7a interacts with immune cells because of its interaction with the integrin LFA-1 . SARS-CoV2 ORF7a has the critical structural required to bind LFA-1 Cluster and has the associated leukocyte integrin Mac-1 (also known to be expressed by macrophages). The accumulation of ORF7a protein in cells limits the transport of LFA-1/Mac1 integrins to the cell membrane and reduces LFA-1/Mac-1 dependent cell signal transduction, which is an essential cascade of white blood cell function. These include the type II integral membrane protein BST2/tetherin, which is found to prevent virus release and is targeted by the SARS-CoV-2 ORF7a protein to escape immunity .