in silico prediction of continuous epitopes on human immunoglobulin light chains

Background & objective: immunoglobulins (igs) have a vital role in body protection against germs. igs contain heavy and light chains. ig light chains consist of two isotypes: kappa and lambda. remarkable alterations in kappa to lambda proportion could occur in monoclonal growth of malignant b cells. antihuman light chain monoclonal antibodies (mabs) have medical implication in diagnosis and immunotherapy of bcell proliferative disorders. in current study, prediction of continuous epitopes in constant part of human ig light chain by immunoinformatics is explained.materials & methods: amino acid sequence and third structure of reference human igg light chain was obtained in pdb database. second igg structure was identified by phyre 2 software. continuous epitopes of ig light chains were delineated by bepipred and ellipro software programs.results: four continuous epitopes situated to constant domain of human ig light chain were predicted by bepipred software. these continuous epitopes were located at amino acid sequences 110130, 150160, 160175 and 180205 of ig light chain. the prominent epitope was sited at amino acids 160175. also, one continuous epitope situated in 198203 amino acid sequences was predicted by ellipro software.conclusion: in present study several continuous epitopes sited to constant part of human ig light chain were determined. these epitopes are valuable for making specific monoclonal anti ig light chain antibodies and could have plausible implication in generation of specific diagnostic kits for human ig light chain, monitoring the monoclonal light chain diseases, treatment of associated b cell malignancies and epitope mapping of ig light chain.

In Silico Prediction of Continuous Epitopes on Human immunoglobulin Light Chains

Background Objective: Immunoglobulins (Igs) have a vital role in body protection against germs. Igs contain heavy and light chains. Ig light chains consist of two isotypes: Kappa and lambda. Remarkable alterations in kappa to lambda proportion could occur in monoclonal growth of malignant B cells. Antihuman light chain monoclonal antibodies (MAbs) have medical implication in diagnosis and immunotherapy of Bcell proliferative disorders. In current study, prediction of continuous epitopes in constant part of human Ig light chain by immunoinformatics is explained.Materials Methods: Amino acid sequence and third structure of reference human IgG light chain was obtained in PDB database. Second IgG structure was identified by Phyre 2 software. Continuous epitopes of Ig light chains were delineated by Bepipred and Ellipro software programs.Results: Four continuous epitopes situated to constant domain of human Ig light chain were predicted by Bepipred software. These continuous epitopes were located at amino acid sequences 110130, 150160, 160175 and 180205 of Ig light chain. The prominent epitope was sited at amino acids 160175. Also, one continuous epitope situated in 198203 amino acid sequences was predicted by Ellipro software.Conclusion: In present study several continuous epitopes sited to constant part of human Ig light chain were determined. These epitopes are valuable for making specific monoclonal anti Ig light chain antibodies and could have plausible implication in generation of specific diagnostic kits for human Ig light chain, monitoring the monoclonal light chain diseases, treatment of associated B cell malignancies and epitope mapping of Ig light chain.