Serum IgG2 levels predict long-term protection following pneumococcal vaccination in systemic lupus erythematosus (SLE)
VACCINE
Authors: Gerard, Anne-Laure; Goulenok, Tiphaine; Bahuaud, Mathilde; Francois, Chrystelle; Aucouturier, Pierre; Moins-Teisserenc, Helene; Batteux, Frederic; Papo, Thomas; Sacre, Karim
Abstract
Systemic lupus erythematosus (SLE) patients are at risk for pneumococcal infection. Twenty-one consecutive SLE patients (40[25-75] years) received the sequential PCV13/PPSV23 vaccine and factors associated with long-term protection were analyzed. Immune protection, defined by an antigen-specific IgG concentration >= 1.3 mu g/mL for at least 70% of 7 pneumococcal serotypes was assessed at baseline, 2, 6, 12 and 36 months defining long-term protection. Only 10 patients showed pneumococcal immune protection 36 months after vaccination. Eleven (52.4%) patients had no long-term protection with a seroconversion that never or only transiently occurred. SLE disease features, treatment received and immunological characteristics did not differ between protected and unprotected patients except for the pre-vaccination IgG2 serum levels. Serum IgG2 level >2.125 mu g/ml showed a sensitivity of 100% and a specificity of 90.9% for long-term protection. Sequential pneumococcal vaccination conferred poor immune protection in SLE. Baseline IgG2 serum level identified patients able to benefit from pneumococcal vaccination. (c) 2020 Elsevier Ltd. All rights reserved.
Mechanism of the effect of 2, 2 '-azobis (2-amidinopropane) dihydrochloride simulated lipid oxidation on the IgG/IgE binding ability of ovalbumin
FOOD CHEMISTRY
Authors: Zhang, Jing-jing; Tu, Zong-cai; Wang, Hui; Hu, Yue-ming; Du, Peng-cheng; Yang, Yi-peng
Abstract
In this work, the mechanism of the effect of lipid oxidation on the IgG/IgE binding ability of ovalbumin (OVA) was investigated via the peroxyl radicals produced by 2, 2'-azobis (2-amidinopropane) dihydrochloride to simulate lipid oxidation. Results showed that the structure of OVA unfolded partially with an increase in oxidation degree, leading to the exposure of the allergenic epitopes and increasing the IgG/IgE binding ability of OVA. Nine oxidation sites were found on the a-helix, and these sites may unwind the a-helix and expose the allergenic epitopes on the OVA surface, leading to antibody recognition and combination. Consequently, the IgG/IgE binding ability of OVA was increased. In conclusion, the allergenic capacity of OVA can be promoted by modifying peroxyl radical oxidation in processing egg products.