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The self/nonself issue: A confrontation between proteomes.

¹Department of Biochemistry and Molecular Biology; University of Bari; Bari, Italy.

|April 14, 2011

Summary

This summary is machine-generated.

Low sequence similarity to the host proteome defines immunological "nonself" antigens. This finding applies to cancer, autoimmunity, infectious diseases, and allergies, offering new insights into immune system function.

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Area of Science:

Immunology
Proteomics
Pathology

Background:

Distinguishing self from nonself is a fundamental immunological challenge.
Unresolved questions persist in antibody repertoire generation, tolerance, autoimmunity, and immune selection.
Antigen peptide recognition and immunogenicity are modulated by sequence similarity to the host proteome.

Purpose of the Study:

To investigate the role of proteomic similarity in defining immunological 'nonself' antigens.
To systematically define the proteomic similarity of experimentally validated B-cell epitopes using a low-similarity criterion.

Main Methods:

Utilized available proteome assemblies of viruses, bacteria, and higher vertebrates.
Applied a low-similarity criterion to assess proteomic similarity of B-cell epitopes.
Analyzed experimentally validated B-cell epitopes across various disease contexts.

Main Results:

A low similarity to the host proteome is a common property of immunological 'nonself' antigens.
This low similarity is documented in cancer, autoimmunity, infectious diseases, and allergy.
The findings support the hypothesis that sequence similarity modulates antigen recognition and immunogenicity.

Conclusions:

Low proteomic similarity is a key characteristic defining 'nonself' antigens.
This principle unifies the understanding of immune responses in diverse conditions like cancer, autoimmunity, and infections.
The study provides a novel framework for understanding immune system regulation and disease pathogenesis.