相关实验视频

Updated: Jan 12, 2026

Detection of the Genome and Transcripts of a Persistent DNA Virus in Neuronal Tissues by Fluorescent In situ Hybridization Combined with Immunostaining

Detection of the Genome and Transcripts of a Persistent DNA Virus in Neuronal Tissues by Fluorescent In situ Hybridization Combined with Immunostaining

Published on: January 23, 2014

氨酸特异性基因组脱甲基酶复合体限制了爱斯坦-巴尔病毒的性活性化

Yifei Liao^1,2,3, Jinjie Yan^1,2,3, Isabella Y Kong⁴

¹Division of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA.

Nature microbiology

|November 1, 2025

概括

爱斯坦-巴尔病毒 (EBV) 延迟依赖于宿主因素,如LSD1.1. 抑制LSD1会重新激活EBV,使其成为EBV驱动癌症的潜在治疗标.

科学领域:

病毒学病毒学
表观遗传学在表观遗传学中,表观遗传学是指表观遗传学.
癌症生物学癌症生物学

背景情况:

爱斯坦-巴尔病毒 (EBV) 感染了超过95%的成年人,并与各种人类癌症有关.
在EBV的潜伏期内,病毒基因会沉默,阻碍诸如甘西克洛维尔之类的抗病毒治疗.
控制EBV延迟的宿主因素在很大程度上仍然没有特征.

研究的目的:

为了确定维持爱斯坦-巴尔病毒 (EBV) 潜伏期所必需的宿主因素.
探索针对这些宿主因子进行EBV再激活和治疗的治疗潜力.

主要方法:

在伯基特淋巴瘤B细胞中进行全基因组的CRISPR-Cas9查.
基因淘汰和药物抑制已识别的宿主因子.
对EBV再激活标志物和甘西克洛维尔敏感性的分析.
研究涉及基因素修饰和DNA循环的分子机制.

主要成果:

屏幕确定了氨酸特异性组织脱甲基酶1 (LSD1) 和其核心压缩剂 (CoREST,ZNF217) 作为EBV延迟的关键.
抑制LSD1或基因淘汰诱导了EBV的重新激活和对甘西克洛维尔敏感的细胞.
ZNF217将LSD1/CoREST调用到特定的DNA基因,去除H3K4甲基化标记以保持延迟.
突出显示H3K4甲基化是EBV光学开关的关键调节者.

结论:

LSD1,CoREST和ZNF217是维持EBV延迟的关键宿主因素.
向LSD1会重新激活EBV,并增强甘西克洛维尔对抗EBV相关的恶性瘤的疗效.
希斯H3K4甲基化代表了EBV重新激活的重要调节机制和治疗标.

更多相关视频

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

Isolation and Quantification of Epstein-Barr Virus from the P3HR1 Cell Line

Isolation and Quantification of Epstein-Barr Virus from the P3HR1 Cell Line

Published on: September 28, 2022

相关概念视频

Histone Modification

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...

Spreading of Chromatin Modifications

Spreading of Chromatin Modifications

The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...

Epigenetic Regulation

Epigenetic Regulation

Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
X-chromosome...