These data largely extend our previous conclusion on the specific effect of CRYAB on the folding and trafficking of ATP7B-H1069Q [10], as well as the evidence obtained by others on the properties of CRYAB Pept 73–92, namely: chaperone-like activity (anti-aggregation in vitro) [21]; anti-apoptotic effect in human lens epithelial cells, in mouse organ-cultured lenses and in human fetal RPE cells [22,23]; therapeutic effects in experimental autoimmune encephalomyelitis in mice and in cataract development in selenite-treated rats [22,24]. Here, ATP7B is linked to experimental autoimmune encephalomyelitis.