Antibody-mediated biorecognition of myelin oligodendrocyte glycoprotein: computational evidence of demyelination-related epitopes View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Jéssica Cristiane Magalhães Ierich, Doralina Guimarães Brum, Ariana de Souza Moraes, Akemi Martins Higa, Pâmela Soto Garcia, Celina Massumi Miyazaki, Marystela Ferreira, Luís Antonio Peroni, Guedmiller Souza de Oliveira, Eduardo de Faria Franca, Luiz Carlos Gomide Freitas, Fabio Lima Leite

ABSTRACT

Antigen-antibody interaction is crucial in autoimmune disease pathogenesis, as multiple sclerosis and neuromyelitis optica. Given that, autoantibodies are essential biomolecules, of which the myelin oligodendrocyte glycoprotein (MOG) can figure as a target. Here we combined Molecular Dynamics (MD), Steered Molecular Dynamics (SMD), and Atomic Force Microscope (AFM) to detail MOG recognition by its specific antibody. The complex model consisted of the MOG external domain interacting with an experimental anti-MOG antibody from the Protein Data Bank (1PKQ). Computational data demonstrated thirteen MOG residues with a robust contribution to the antigen-antibody interaction. Comprising five of the thirteen anchor residues (ASP102, HIS103, SER104, TYR105, and GLN106), the well-known MOG92-106 peptide in complex with the anti-MOG was analysed by AFM and SMD. These analyses evidenced similar force values of 780 pN and 765 pN for computational and experimental MOG92-106 and anti-MOG detachment, respectively. MOG92-106 was responsible for 75% of the total force measured between MOG external domain and anti-MOG, holding the interaction with the antibody. The antigen-antibody binding was confirmed by Surface Plasmon Resonance (SPR) measurements. Combined approaches presented here can conveniently be adjusted to detail novel molecules in diseases research. This can optimize pre-clinical steps, guiding experiments, reducing costs, and animal model usage. More... »

PAGES

2033

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-018-36578-8

DOI

http://dx.doi.org/10.1038/s41598-018-36578-8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112134550

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30765742


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