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dc.contributor.authorUmpa Yasamuten_US
dc.contributor.authorWeeraya Thongkumen_US
dc.contributor.authorSutpirat Moonmuangen_US
dc.contributor.authorSupachai Sakkhachornphopen_US
dc.contributor.authorRomanee Chaiwarithen_US
dc.contributor.authorJutarat Praparattanapanen_US
dc.contributor.authorJiraprapa Wipasaen_US
dc.contributor.authorKriangkrai Chawansuntatien_US
dc.contributor.authorKhuanchai Supparatpinyoen_US
dc.contributor.authorEthan Laien_US
dc.contributor.authorChatchai Tayapiwatanaen_US
dc.description.abstract© 2019 Yasamut, Thongkum, Moonmuang, Sakkhachornphop, Chaiwarith, Praparattanapan, Wipasa, Chawansuntati, Supparatpinyo, Lai and Tayapiwatana. Adult-onset immunodeficiency (AOID) with anti-interferon-γ (IFN-γ) autoantibodies (autoAbs) is an emerging immunodeficiency syndrome in Asian countries. The presence of neutralizing anti-IFN-γ autoAbs are significantly associated with severe disseminated opportunistic infections. However, the characteristics of the neutralizing antibodies in patients are poorly defined. To better understand the properties of the anti-IFN-γ autoAbs in patients with opportunistic infections, a simplified competitive-binding ELISA was developed. The domains recognized by anti-IFN-γ autoAbs were assessed based on their competition with commercial neutralizing mouse anti-IFN-γ monoclonal antibodies (mAbs). First, the binding affinity and neutralizing capacity of these mAbs (clones B27, B133.5, and MD-1) were characterized. Kinetic analysis and epitope binning using bio-layer interferometry showed the comparable binding affinity of these mAbs to full-length IFN-γ and to the adjacent binding region. These mAbs did not recognize the synthetic 20-mer peptides and inhibited IFN-γ-mediated functions differently. In a competitive-binding ELISA, the anti-IFN-γ autoAbs in AOID serum blocked B27, B133.5, and MD-1 mAb binding. This evidence suggested that the autoAbs that competed with neutralizing mouse anti-IFN-γ mAbs recognized a discontinuous epitope of homodimeric IFN-γ as these mAbs. The patient autoAbs that recognized the B27 epitope exhibited strong neutralizing activity that was determined by the functional analysis. Our results demonstrated the heterogeneity of the autoAbs against IFN-γ in AOID patients and the different patterns among individuals. These data expand upon the fundamental knowledge of neutralizing anti-IFN-γ autoAbs in AOID patients.en_US
dc.subjectImmunology and Microbiologyen_US
dc.titleNeutralizing activity of anti-interferon-γ autoantibodies in adult-onset immunodeficiency is associated with their binding domainsen_US
article.title.sourcetitleFrontiers in Immunologyen_US
article.volume10en_US Mai Universityen_US Filtrationen_US
Appears in Collections:CMUL: Journal Articles

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