تعیین اپی توپ های ناپیوسته زنجیره سبک ایمونوگلوبولین انسان توسط ایمونولوژی محاسبه ای

Background: Immunoglobulins are a group of proteins that have important role in defense against microorganisms. Immunoglobulins consist of heavy and light chains. In human, immunoglobulin light chain comprises of two isotypes: Kappa (K) and lambda (λ) based on amino acid differences in carboxylic end of their constant region. Marked changes in the K to λ ratio can happen in monoclonal expansion of neoblastic B cells or HIV infection in neonatal periods. Highly sensitive and specific anti-light chain MAbs have clinical importance in the diagnosis and immunotherapy of patients with B-cell immunoproliferative diseases. Thus, precise determination of specific epitopes in light chains is very important. Computational immunology uses the computational data for more accurate diagnosis of diseases. This study describes determination of conformational epitopes in constant region of human immunoglobulin light chain by computational immunology. Methods: The amino acid residue and third structure of reference human immunoglobulin G light chain was found in PDB database. The second immunoglobulin G structure was defined by Phyre 2 software. Conformational epitopes of the immunoglobulin light chain were specified by CEP software. Results: In this study five conformational epitopes located on constant domain of human immunoglobulin light chain were determined by CEP software. These conformational epitopes were located in 100-214 amino acid sequences of light chains. Conclusion: In this study a number of conformational epitopes located on constant domain of human immunoglobulin light chain were determined. These epitopes are valuable tools for generating specific monoclonal anti-immunoglobulin light chain antibodies and might have possible implication in production of specific diagnostic kits for human immunoglobulin light chain, monitoring of monoclonal light chain diseases, treatment of related B cell tumors, epitope mapping of immunoglobulin light chain and evolutionary studies.