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.