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388 results on '"Cai, Xiaoli"'

13. A ruthenium single atom nanozyme-based antibiotic for the treatment of otitis media caused by Staphylococcus aureus.

Author

Wang, Jie, Gong, Rui, Yang, Ming, Wu, Xi, Li, Ziwei, Huang, Haibing, Yan, Xiyun, Wang, Daji, Cai, Xiaoli, and Wang, Zixin

Subjects
OTITIS media, RUTHENIUM, STAPHYLOCOCCUS aureus, HORSERADISH peroxidase, OTITIS, ANTIBIOTICS
Abstract

Staphylococcus aureus (S. aureus) infection is a primary cause of otitis media (OM), the most common disease for which children are prescribed antibiotics. However, the abuse of antibiotics has led to a global increase in antimicrobial resistance (AMR). Nanozymes, as promising alternatives to traditional antibiotics, are being extensively utilized to combat AMR. Here, we synthesize a series of single-atom nanozymes (metal-C3N4 SANzymes) by loading four metals (Ag, Fe, Cu, Ru) with antibacterial properties onto a crystalline g-C3N4. These metal-C3N4 display a rob-like morphology and well-dispersed metal atoms. Among them, Ru-C3N4 demonstrates the optimal peroxidase-like activity (285.3 U mg-1), comparable to that of horseradish peroxidase (267.7 U mg-1). In vitro antibacterial assays reveal that Ru-C3N4 significantly inhibits S. aureus growth compared with other metal-C3N4 even at a low concentration (0.06 mg mL-1). Notably, Ru-C3N4 acts as a narrow-spectrum nanoantibiotic with relative specificity against Gram-positive bacteria. Biofilms formed by S. aureus are easily degraded by Ru-C3N4 due to its high peroxidase-like activity. In vivo, Ru-C3N4 effectively eliminates S. aureus and relieves ear inflammation in OM mouse models. However, untreated OM mice eventually develop hearing impairment. Due to its low metal load, Ru-C3N4 does not exhibit significant toxicity to blood, liver, or kidney. In conclusion, this study presents a novel SANzyme-based antibiotic that can effectively eliminate S. aureus and treat S. aureus-induced OM. [ABSTRACT FROM AUTHOR]

Published
2024
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42. Perturbing TET2 condensation promotes aberrant genome-wide DNA methylation and curtails leukaemia cell growth

Author

Guo, Lei, Hong, Tingting, Lee, Yi-Tsang, Hu, Xue, Pan, Guokai, Zhao, Rongjie, Yang, Yuhan, Yang, Jingwen, Cai, Xiaoli, Rivera, Logan, Liang, Jie, Wang, Rui, Dou, Yaling, Kodali, Srikanth, Li, Wenbo, Han, Leng, Di Stefano, Bruno, Zhou, Yubin, Li, Jia, and Huang, Yun

Abstract

The ten-eleven translocation (TET) family of dioxygenases maintain stable local DNA demethylation during cell division and lineage specification. As the major catalytic product of TET enzymes, 5-hydroxymethylcytosine is selectively enriched at specific genomic regions, such as enhancers, in a tissue-dependent manner. However, the mechanisms underlying this selectivity remain unresolved. Here we unveil a low-complexity insert domain within TET2 that facilitates its biomolecular condensation with epigenetic modulators, such as UTX and MLL4. This co-condensation fosters a permissive chromatin environment for precise DNA demethylation. Disrupting low-complexity insert-mediated condensation alters the genomic binding of TET2 to cause promiscuous DNA demethylation and genome reorganization. These changes influence the expression of key genes implicated in leukaemogenesis to curtail leukaemia cell proliferation. Collectively, this study establishes the pivotal role of TET2 condensation in orchestrating precise DNA demethylation and gene transcription to support tumour cell growth.

Published
2024
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