Abstract
By applying analysis of the principal components of amino acid physical properties we predicted cathepsin cleavage sites, MHC binding affinity, and probability of B-cell epitope binding of peptides in tetanus toxin and in ten diverse additional proteins. Cross-correlation of these metrics, for peptides of all possible amino acid index positions, each evaluated in the context of a ±25 amino acid flanking region, indicated that there is a strongly repetitive pattern of short peptides of approximately thirty amino acids each bounded by cathepsin cleavage sites and each comprising B-cell linear epitopes, MHC-I and MHC-II binding peptides. Such "immunologic kernel" peptides comprise all signals necessary for adaptive immunologic cognition, response and recall. The patterns described indicate a higher order spatial integration that forms a symbolic logic coordinating the adaptive immune system.
MeSH terms
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B-Lymphocytes / immunology
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B-Lymphocytes / metabolism
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Cathepsins / chemistry
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Cathepsins / metabolism
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Cluster Analysis
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Epitopes / chemistry
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Epitopes / immunology
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Epitopes / metabolism
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Epitopes, B-Lymphocyte
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Histocompatibility Antigens Class I / immunology
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Histocompatibility Antigens Class I / metabolism
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Histocompatibility Antigens Class II / immunology
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Histocompatibility Antigens Class II / metabolism
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Humans
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Models, Immunological
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Peptides / chemistry
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Peptides / immunology
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Peptides / metabolism
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Protein Binding / immunology
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Proteins / chemistry*
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Proteins / immunology*
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Proteins / metabolism
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Proteolysis
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Tetanus Toxin / chemistry
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Tetanus Toxin / immunology
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Tetanus Toxin / metabolism
Substances
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Epitopes
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Epitopes, B-Lymphocyte
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Histocompatibility Antigens Class I
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Histocompatibility Antigens Class II
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Peptides
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Proteins
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Tetanus Toxin
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Cathepsins
Grants and funding
The authors have no support or funding to report.