Jiang, Lijun; Lung, Hong Lok; Huang, Tao; Lan, Rongfeng; Zha, Shuai; Chan, Lai Sheung; Thor, Waygen; Tsoi, Tik-Hung; Chau, Ho-Fai; Borestrom, Cecilia; Cobb, Steven L.; Tsao, Sai Wah; Bian, Zhao-Xiang; Law, Ga-Lai; Wong, Wing-Tak; Tai, William Chi-Shing; Chau, Wai Yin; Du, Yujun; Tang, Lucas Hao Xi; Chiang, Alan Kwok Shing; Middeldorp, Jaap M.; Lo, Kwok-Wai; Mak, Nai Ki; Long, Nicholas J.; Wong, Ka-Leung published the artcile< Reactivation of epstein-barr virus by a dual-responsive fluorescent EBNA1-targeting agent with Zn2+-chelating function>, COA of Formula: C19H34O2, the main research area is epstein barr virus oncolysis cancer EBNA1 zinc probe ZRL5P4; EBNA1-targeting agent; EBV-specific lytic inducer; dual-responsive fluorescent EBV probe.
Epstein-Barr nuclear antigen 1 (EBNA1) plays a vital role in the maintenance of the viral genome and is the only viral protein expressed in nearly all forms of Epstein-Barr virus (EBV) latency and EBV-associated diseases, including numerous cancer types. To our knowledge, no specific agent against EBV genes or proteins has been established to target EBV lytic reactivation. Here we report an EBNA1- and Zn2+-responsive probe (ZRL5P4) which alone could reactivate the EBV lytic cycle through specific disruption of EBNA1. We have utilized the Zn2+ chelator to further interfere with the higher order of EBNA1 self-association The bioprobe ZRL5P4 can respond independently to its interactions with Zn2+ and EBNA1 with different fluorescence changes. It can selectively enter the nuclei of EBV-pos. cells and disrupt the oligomerization and oriP-enhanced transactivation of EBNA1. ZRL5P4 can also specifically enhance Dicer1 and PML expression, mol. events which had been reported to occur after the depletion of EBNA1 expression. Importantly, we found that treatment with ZRL5P4 alone could reactivate EBV lytic induction by expressing the early and late EBV lytic genes/proteins. Lytic induction is likely mediated by disruption of EBNA1 oligomerization and the subsequent change of Dicer1 expression. Our probe ZRL5P4 is an EBV protein-specific agent that potently reactivates EBV from latency, leading to the shrinkage of EBV-pos. tumors, and our study also suggests the association of EBNA1 oligomerization with the maintenance of EBV latency.
Proceedings of the National Academy of Sciences of the United States of America published new progress about Antitumor agents. 112-63-0 belongs to class esters-buliding-blocks, and the molecular formula is C19H34O2, COA of Formula: C19H34O2.
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