AI Article Synopsis
- Understanding autoimmunity to the body's own proteins is key for diagnosing and treating autoimmune diseases, prompting the development of the AAgAtlas portal which lists over 8,000 autoantigens linked to various human diseases.
- The portal allows users to explore the properties and characteristics of these autoantigens, highlighting their evolutionary conservation and common features like hydrophilic amino acids that are often found on protein surfaces.
- Findings indicate that the production of antibodies targeting these autoantigens is related to genetic variations and abnormal protein expression in diseases, aiding in the identification of potential biomarkers for autoimmune conditions.
Article Abstract
Understanding autoimmunity to endogenous proteins is crucial in diagnosing and treating autoimmune diseases. In this work, we developed a user-friendly AAgAtlas portal (http://biokb.ncpsb.org.cn/aagatlas_portal/index.php#), which can be used to search for 8045 non-redundant autoantigens (AAgs) and 47 post-translationally modified AAgs against 1073 human diseases that are prioritized by a credential score developed by multisource evidence. Using AAgAtlas, the immunogenic properties of human AAgs was systematically elucidated according to their genetic, biophysical, cytological, expression profile, and evolutionary characteristics. The results indicated that human AAgs are evolutionally conserved in protein sequence and enriched in three hydrophilic and polar amino acid residues (K, D, and E) that are located at the protein surface. AAgs are enriched in proteins that are involved in nucleic acid binding, transferase, and the cytoskeleton. Genome, transcriptome, and proteome analyses further indicated that AAb production is associated with gene variance and abnormal protein expression related to the pathological activities of different tumors. Collectively, our data outlines the hallmarks of human AAgs that facilitate the understanding of humoral autoimmunity and the identification of biomarkers of human diseases.
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| http://dx.doi.org/10.1021/acs.jproteome.2c00799 | DOI Listing |
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