The ORF8 homodimer disulphide highly interdigitated interface is made up of complementary A-B amino acid surfaces implicating salt bridges ( 119 D-115 R and 115 R-92 E), hydrogen bonds ( 120 F-53 K, 53 K-24 S, 18 Q-22 L, 52 R-121 I) and many other hydrophobic interactions . The predominant natural mutants of ORF8 include the L 84 S mutation, but S L and V 62 L mutations are also abundant . The L 84 S mutation reduced some of the dimer interacting amino acids, including those implicated in salt bridges (i.e., 119 D, 115 R), hydrogen bonds ( 120 F, K, R, 121 I), and other interface interactions ( 98 R, 104 I, 117 V) .