Conclusion
SARS-CoV-2 eight amino acid length peptides matched the human proteome and found six identical peptides. The peptide sequence with the highest probability of cross-reactivity was selected and analyzed. Selected peptide docked MHC-I and MHC-II receptors, these docking results show DEDDSEPV sequence can cause cross-reactivity to human myosin-16. Myosin-16 is a motor protein and is highly expressed in the central nervous system. Myosin-16 protein is also highly expressed in endocrine tissues (especially the pituitary gland), liver, and gallbladder. In our study, we proved by using in-silico methods that the DEDDSEPV peptide sequence can cause cross-reactivity. Auto-antibodies that may develop against myosin-16 may explain the neurological symptoms and diseases that may develop due to COVID-19. This could explain the pathophysiologic symptoms and diseases that may develop due to COVID-19 of the endocrine system, which affects the entire physiology of the human body, such as the immune system. Liver function tests are high in critical and severe COVID-19 patients. Since myosin-16 is expressed at a high level in the liver tissue, it can explain the irregularity in liver function tests. Our study is the first in the literature to try to define the molecular mimicry between SARS-CoV-2 and the human proteome using immunoinformatic techniques. We think that in the future it will illuminate the similarity between other organisms and the human proteome using the methodology in our study. It may contribute to elucidating the pathophysiology of autoimmune diseases by elucidating the similarity between other organisms and the human proteome. When molecular mimicries are illuminated and which organism triggers which autoimmunity, removal of the triggering organism or reduction of its antigenic load can open a new era in the treatment of autoimmune diseases.