Histone methyltransferase SUV39H1 participates in host defense by methylating mycobacterial histone-like protein HupB
| Autor: | Imtiyaz Yaseen, Sanjeev Khosla, Mitali Choudhury, Manjula Sritharan |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Methyltransferase THP-1 Cells Host–pathogen interaction 030106 microbiology Biology Methylation General Biochemistry Genetics and Molecular Biology Microbiology Histones 03 medical and health sciences Mice Bacterial Proteins Histone methylation Animals Humans Tuberculosis News & Views Epigenetics Cell adhesion Molecular Biology Mice Inbred BALB C General Immunology and Microbiology General Neuroscience Methyltransferases Mycobacterium bovis Chromatin Repressor Proteins 030104 developmental biology Histone Histone methyltransferase biology.protein Macrophages Peritoneal |
| Zdroj: | The EMBO journal. 37(2) |
| ISSN: | 1460-2075 |
| Popis: | Host cell defense against an invading pathogen depends upon various multifactorial mechanisms, several of which remain undiscovered. Here, we report a novel defense mechanism against mycobacterial infection that utilizes the histone methyltransferase, SUV39H1. Normally, a part of the host chromatin, SUV39H1, was also found to be associated with the mycobacterial bacilli during infection. Its binding to bacilli was accompanied by trimethylation of the mycobacterial histone‐like protein, HupB, which in turn reduced the cell adhesion capability of the bacilli. Importantly, SUV39H1‐mediated methylation of HupB reduced the mycobacterial survival inside the host cell. This was also true in mice infection experiments. In addition, the ability of mycobacteria to form biofilms, a survival strategy of the bacteria dependent upon cell–cell adhesion, was dramatically reduced in the presence of SUV39H1. Thus, this novel defense mechanism against mycobacteria represents a surrogate function of the epigenetic modulator, SUV39H1, and operates by interfering with their cell–cell adhesion ability. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text