Prediction of accessibility of amino acids in human immunoglobulin G light chains

Fatemeh Hajighasemi | Soheila Rohani | Fatemeh Sefid

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URL :   http://research.shahed.ac.ir/WSR/WebPages/Report/PaperView.aspx?PaperID=85504
Date :  2018/01/31
Publish in :    دهمين کنگره بين المللي ازمايشگاه و بالين

Link :  http://isacl-congress.ir
Keywords : Human IgG, immunoinformatic, accessibility

Abstract :

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Objective: Immunoglobulin G (IgG) has very important role in defense against microorganisms. The quantity of serum IgG is linked to severity of some diseases specially infections. Thus IgG has high diagnostic value. For careful measurement of IgG, diagnostic tools such as IgG- epitope specific monoclonal antibodies (MAbs) are required. Immunogenic epitopes are valuable targets for producing very efficient MAbs. More accessible amino acids in an epitope make it more immunogenic. Immunoinformatic is an immunology branch helpful for better determination of immunogenic epitopes through definition of their physiochemical properties such as amino acids accessibility. The aim of this study is prediction of accessibility of amino acids in human immunoglobulin G light chains by immunoinformatic. Methods: The amino acid sequence and third structure of reference human IgG was found in PDB database. The second IgG structure was determined by Phyre 2 software. IgG light chains amino acids accessibility was defined by IEDB software. Results: The most accessible amino acids were located in 125 - 175 and in 181 – 191 amino acid sequence (in constant domain (CL)) of light chains as was determined by IEDB software. Conclusion: According to the results of this study the amino acid sequences located in 125 - 175 or 181 – 191 positions of light chains are the most accessible amino acids and hence very useful tools for recognition of more immunogenic epitopes to producing highly sensitive and specific anti IgG MAbs. Key words: Human IgG, immunoinformatic, accessibility

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