التفاصيل البيبلوغرافية
| العنوان: |
Pseudorabies virus UL38 attenuates the cGAS-STING signaling pathway by recruiting Tollip to promote STING for autophagy degradation. |
| المؤلفون: |
Yan, Zhenfang, Xie, Jingying, Hou, Zhengyang, Zhang, Yaxin, Yue, Jiayu, Zhang, Xiangbo, Chen, Lei, Yang, Yanmei, Li, Xiangrong, Li, Huixia, Feng, Ruofei |
| المصدر: |
Virology Journal; 5/8/2024, Vol. 21, p1-12, 12p |
| مصطلحات موضوعية: |
AUJESZKY'S disease virus, CELLULAR signal transduction, AUTOPHAGY, NATURAL immunity, PATHOGENIC microorganisms |
| مستخلص: |
Natural immunity is the first defense line of the host immune system, which plays a significant role in combating foreign pathogenic microorganisms. The IFN-β (interferon-beta) signaling pathway, being a typical example of innate immunity, plays a vital function. This study aimed to elucidate the function of pseudorabies virus (PRV) UL38 protein (unique long region 38) in suppressing the activation of the IFN-β signaling pathway. The findings from our study indicate that the PRV UL38 protein effectively hampers the activation of IFN-β by poly (dA: dT) (poly(deoxyadenylic-deoxythymidylic)) and 2'3'-cGAMP (2'-3'-cyclic GMP-AMP). Furthermore, UL38 exhibits spatial co-localization with STING (stimulator of interferon genes) and effectively hinders STING dimerization. Subsequently, STING was downgraded to suppress the production of IFN-β and ISGs (interferon stimulated genes). Immunoprecipitation analysis revealed that the interaction between UL38 and STING, which subsequently initiated the degradation of STING via selective autophagy mediated by TOLLIP (toll interacting protein). To summarize, this research elucidates the function of UL38 in counteracting the cGAS (cGAMP synthase)-STING-induced IFN-β pathway. The PRV UL38 protein may attenuate the activation of IFN-β as a means of regulating the virus's persistence in the host. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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