Myosin 16 mimicries may explain post- COVID-19 related neurological consequences

Autoimmune diseases arise from an immune response against self-antigens, but their pathophysiology is not fully understood. One of the proposed mechanisms is molecular mimicry, where infectious agents share similar antigens with host proteins leading to cross-reactivity. Our study aimed to investigate the presence of molecular mimicry between SARS-CoV-2 and human proteome using bioinformatics techniques. To accomplish this, we constructed sequences of 8 consecutive amino acids for structural proteins of SARS-CoV-2, such as spike, nucleocapsid, membrane, and envelope proteins. Next, we evaluated the mimicry of these sequences with the human proteome and analyzed their antigenicity, allergenicity, toxicity, TAP affinity, and IFNγ and IL-10 induction.We also calculated the affinity of the amino acid sequence DEDDSEPV, which showed molecular mimicry, to HLA receptors and found that it had a good binding energy. Based on our in silico analysis, we found that DEDDSEPV amino acid sequence might trigger autoimmunity due to its similarity with myosin-16 protein. Our study provides evidence for the possibility of SARS-CoV-2 inducing autoimmunity via molecular mimicry. Our findings can have significant implications for understanding the pathophysiology of autoimmune diseases and may contribute to the development of potential therapeutic strategies.