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Analysis Interaction of Immunoglobulin G and Immunoglobulin A Against PstS1 as a Basis Specimen Selection for M. tuberculosis Rapid Test Diagnostic Agent

1Faculty of Medicine, Universitas Brawijaya, Indonesia

2Departement of Biochemistry and Molecular Biology, Faculty of Medicine, Universitas Brawijaya, Indonesia

3Departement of Clinical Pathology, Faculty of Medicine, Universitas Brawijaya, Indonesia

Received: 17 Jul 2023; Revised: 5 Dec 2023; Accepted: 8 Dec 2023; Available online: 31 Dec 2023; Published: 31 Dec 2023.
Open Access Copyright (c) 2023 Journal of Biomedicine and Translational Research
Creative Commons License This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.

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Background: The recombinant Ag38 protein developed from a local strain of Mycobacterium tuberculosis has great potential to be used as a sero-diagnosis agent using the antigen rapid test because it has several epitopes that bind to antibodies. However, it is not yet known which antibody Ag38-recombinant binds maximally between IgA and IgG.

Objective: The aim of this study is to compare the interaction between IgG and IgA on Ag-38 rec in silico as a basis for the selection of sero-diagnosis agents in the TB rapid test.

Methods: The results show that the protein PstS1 has a higher binding sensitivity to IgG based on one of the docking models which shows a docking score of -229.70, a confident score of 0.8312 and RMSD 1.060 A. The ramachandran plot also shows that testing on this model has a protein structure that is good, with disallowed regions [X,X] values of 0.5% (less than 0.8%). The results of this analysis show that the most favored regions are 90.5% with a G-factor of -0.27. The quality of the structure of the 3D mooring model can be said to be good because it fulfills the ideal structure requirements.

Conclusion: Ag38-rec antigen M. tuberculosis H37Rv binds to IgG more strongly than IgA.

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Keywords: M. tuberculosis; Ag38-rec; PstS1; Immunoglobulin G; Immunoglobulin A
Funding: LPDP

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