文献类型： 外文期刊
作者： Peng, Huakang 1 ; Wang, Nan 1 ; Wang, Mengqi 1 ; Yang, Caifeng 1 ; Guo, Wenfang 1 ; Li, Gangqiang 1 ; Huang, Sumei 2 ; Wei, Di 2 ; Liu, Dehu 1 ;
作者机构： 1.Chinese Acad Agr Sci, Biotechnol Res Inst, Beijing 100081, Peoples R China
2.Guangxi Acad Agr Sci, Biotechnol Res Inst, Nanning 530007, Peoples R China
关键词： N-glycosylation sites; plasminogen activator; fibrin selectivity; DSPA alpha 1; rat; drug safety
期刊名称：LIFE-BASEL （ 影响因子：3.2； 五年影响因子：3.2 ）
ISSN：
年卷期： 2023 年 13 卷 4 期
页码：
收录情况： SCI
摘要： DSPAa1 is a potent rude thrombolytic protein with high medicative value. DSPAa1 has two natural N-glycan sites (N153Q-S154-S155, N398Q-K399-T400) that may lead to immune responses when administered in vivo. We aimed to study the effect of its N-glycosylation sites on DSPAa1 in vitro and in vivo by mutating these N-glycosylation sites. In this experiment, four single mutants and one double mutant were predicted and expressed in Pichia pastoris. When the N398Q-K399-T400 site was mutated, the fibrinolytic activity of the mutant was reduced by 75%. When the N153Q-S154-S155 sites were inactivated as described above, the plasminogen activating activity of its mutant was reduced by 40%, and fibrin selectivity was significantly reduced by 21-fold. The introduction of N-glycosylation on N184-G185-A186T and K368N-S369-S370 also considerably reduced the activity and fibrin selectivity of DSPAa1. The pH tolerance and thermotolerance of all mutants did not change significantly. In vivo experiments also confirmed that N-glycosylation mutations can reduce the safety of DSPAa1, lead to prolonged bleeding time, non-physiological reduction of coagulation factor (a2-AP, PAI) concentration, and increase the risk of irregular bleeding. This study ultimately demonstrated the effect of N-glycosylation mutations on the activity and safety of DSPAa1.
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