ORF8 monomers, contain an Ig-like fold stabilized by intramolecular disulphides ( 25 C-90 C, C-102 C) and a highly-dynamic fold loop (hypervariable loop) flanked by its 61 C-83 C disulphide and coding for a 73 YIDI motif including a glycosylation site ( 78 N). The hypervariable loop has been implicated in the many host protein interactions mentioned above, capable of adapting its hypervariable fold to any of those different ligands . However, to our knowledge, there are no crystallographic ORF8-protein complex structures reported to date.