Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2019 Aug 14;10:1905. doi: 10.3389/fimmu.2019.01905

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2019 Yasamut, Thongkum, Moonmuang, Sakkhachornphop, Chaiwarith, Praparattanapan, Wipasa, Chawansuntati, Supparatpinyo, Lai and Tayapiwatana.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

Characterization of anti-IFN-γ autoAbs in AOID patients by competitive-binding ELISA. The domains recognized by anti-IFN-γ autoAbs in patient sera were evaluated by competitive-binding ELISA. The binding of each mouse neutralizing anti-IFN-γ mAb (B27, B133.5, and MD-1) was competed with the anti-IFN-γ autoAbs in each patient serum. The reduction of the optical density demonstrates that there was competition. (A) The optical density of the B27 mAb. (B) The optical density of the B133.5 mAb. (C) The optical density of the MD-1 mAb. (D) Percentage of inhibition was calculated and showed the relative level of anti-IFN-γ autoAbs recognizing the mAb-binding epitope in patient sera. Experiments were performed in triplicate. Error bars represent the mean ± SEM. C, non-competitive condition; N, normal serum; A, AOID patient serum.