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1.
Sci Rep ; 11(1): 17199, 2021 08 25.
Article in English | MEDLINE | ID: mdl-34433832

ABSTRACT

An extremely high contagiousness of SARS CoV-2 indicates that the virus developed the ability to deceive the innate immune system. The virus could have included in its outer protein domains some motifs that are structurally similar to those that the potential victim's immune system has learned to ignore. The similarity of the primary structures of the viral and human proteins can provoke an autoimmune process. Using an open-access protein database Uniprot, we have compared the SARS CoV-2 proteome with those of other organisms. In the SARS CoV-2 spike (S) protein molecule, we have localized more than two dozen hepta- and octamers homologous to human proteins. They are scattered along the entire length of the S protein molecule, while some of them fuse into sequences of considerable length. Except for one, all these n-mers project from the virus particle and therefore can be involved in providing mimicry and misleading the immune system. All hepta- and octamers of the envelope (E) protein, homologous to human proteins, are located in the viral transmembrane domain and form a 28-mer protein E14-41 VNSVLLFLAFVVFLLVTLAILTALRLCA. The involvement of the protein E in provoking an autoimmune response (after the destruction of the virus particle) seems to be highly likely. Some SARS CoV-2 nonstructural proteins may also be involved in this process, namely ORF3a, ORF7a, ORF7b, ORF8, and ORF9b. It is possible that ORF7b is involved in the dysfunction of olfactory receptors, and the S protein in the dysfunction of taste perception.


Subject(s)
Proteomics , SARS-CoV-2/metabolism , Sequence Homology, Amino Acid , Viral Proteins/chemistry , Viral Proteins/metabolism , Cell Line , Humans , SARS-CoV-2/physiology , Spike Glycoprotein, Coronavirus/chemistry , Spike Glycoprotein, Coronavirus/metabolism
2.
Mol Biol Rep ; 45(2): 143-150, 2018 Apr.
Article in English | MEDLINE | ID: mdl-29340900

ABSTRACT

Xenin is a regulatory peptide first isolated from the human gastric mucosa. Using an open-access protein database MEDLINE (33 million molecules; 11 billion amino acid residues) and our original computer program, we conducted a search for the xenin motifs in the primary structure of proteins across almost the entire taxonomic range of evolution. Motifs with 40% homology to human xenin are already present in prokaryotes. Homology reaches 84-96% in single-cell algae and plants, becoming complete since bony fishes. We suppose that this regulatory peptide is more ancient and significant than is usually thought.


Subject(s)
Neurotensin/genetics , Amino Acid Motifs/genetics , Amino Acid Sequence/genetics , Animals , Databases, Protein , Evolution, Molecular , Gastric Mucosa , Humans , Insulin/genetics , Insulin/metabolism , Neurotensin/metabolism , Peptides/metabolism , Software
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