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Febrile temperatures increase in vitro antibody affinity for malarial and dengue antigens

机译:发热温度提高了体外对疟疾和登革热抗原的抗体亲和力

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摘要

Fever is a regulated increase of the body temperature resulting from both infectious and non-infectious causes. Fever is known to play a role in modulating immune responses to infection, but the potential of febrile temperatures in regulating antigen binding affinity to antibodies has not been explored. Here we investigated this process under in vitro conditions using Isothermal titration calorimetry and ELISA. We used selected malarial and dengue antigens against specific monoclonal antibodies, and observed a marked increase in the affinity of these antibody-antigen complexes at 40°C, compared to physiological (37°C) or pathophysiological temperatures (42°C). Induced thermal equilibration of the protein partners at these temperatures in vitro, prior to measurements, further increased their binding affinity. These results suggest another positive and adaptive role for fever in vivo, and highlight the favourable role of thermal priming in enhancing protein-protein affinity for samples with limited availability.
机译:发烧是由传染性和非传染性两种原因导致的体温升高。已知发烧在调节对感染的免疫反应中起作用,但是尚未探索高热温度在调节抗原对抗体的结合亲和力方面的潜力。在这里,我们使用等温滴定量热法和ELISA在体外条件下研究了这一过程。我们使用了针对特定单克隆抗体的精选疟疾和登革热抗原,与生理温度(37°C)或病理生理温度(42°C)相比,在40°C下观察到这些抗体-抗原复合物的亲和力显着增加。在测量之前,在体外这些温度下,蛋白质伴侣的诱导热平衡进一步提高了它们的结合亲和力。这些结果表明了体内发烧的另一种积极和适应性作用,并突出了热启动对增强有限样品的蛋白质亲和力的有利作用。

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