Abstract
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.