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Related Concept Videos

Histone Modification02:32

Histone Modification

13.2K
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...
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Chromatin Modification in iPS Cells01:32

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Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
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Epigenetic Regulation01:37

Epigenetic Regulation

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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...
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Phase II Reactions: Methylation Reactions01:17

Phase II Reactions: Methylation Reactions

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Methylation is a phase II biotransformation process involving the attachment of a methyl group to a substrate. Enzymes known as methyltransferases orchestrate this reaction.
The mechanism of methylation unfolds in two stages. The first stage sees a methyltransferase enzyme facilitating the transfer of a methyl group from S-adenosylmethionine (SAM) to the substrate, forming S-adenosylhomocysteine (SAH). The second stage involves further metabolism of SAH into homocysteine, which can be recycled...
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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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...
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Quantifying the Cytotoxicity of Staphylococcus aureus Against Human Polymorphonuclear Leukocytes
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Staphylococcus aureus α-hemolysin induces DNA methylation changes in human Th1 cells.

Iwona Karwaciak1, Joanna Pastwińska1, Anna Sałkowska1

  • 1Laboratory of Epigenetics, Institute of Medical Biology, Polish Academy of Sciences, Lodowa 106, Lodz, 93-232, Poland.

Immunologic Research
|June 11, 2025
PubMed
Summary

Staphylococcus aureus alpha-hemolysin alters Th1 cell DNA methylation. This bacterial toxin impacts gene expression and epigenetic regulation in immune cells, potentially changing their function.

Keywords:
Staphylococcus aureusDNA methylationTh1α-Hemolysin

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Area of Science:

  • Immunology
  • Epigenetics
  • Microbial Pathogenesis

Background:

  • Staphylococcus aureus produces alpha-hemolysin, a key virulence factor.
  • Th1 lymphocytes are crucial immune cells responding to S. aureus.
  • The epigenetic impact of bacterial toxins on host immune cells is not well understood.

Purpose of the Study:

  • To investigate the effect of alpha-hemolysin on the DNA methylation patterns of Th1 lymphocytes.
  • To explore how alpha-hemolysin influences the expression of key epigenetic regulators in Th1 cells.

Main Methods:

  • Analysis of protein expression levels for HELLS, DNMT3A, and DNMT3L in Th1 cells.
  • Whole-genome bisulfite sequencing (WGBS) to assess global DNA methylation changes.
  • Exposure of Th1 lymphocytes to purified alpha-hemolysin.

Main Results:

  • Alpha-hemolysin significantly altered DNA methylation in Th1 cells, particularly in non-CpG regions.
  • The toxin upregulated the expression of HELLS and DNMT3A proteins.
  • Downregulation of DNMT3L protein expression was observed following alpha-hemolysin exposure.

Conclusions:

  • Bacterial virulence factors like alpha-hemolysin can act as epigenetic modulators of host immune cells.
  • Alpha-hemolysin induces significant changes in Th1 cell DNA methylation and gene expression.
  • These epigenetic alterations may influence Th1 cell activity, plasticity, and phenotype.