T(oo)bAd

@article{Brodin2019ToobAd,
  title={T(oo)bAd},
  author={Priscille Brodin and Eik Hoffmann},
  journal={Nature Chemical Biology},
  year={2019},
  volume={15},
  pages={849 - 850}
}
An unusual terpene nucleoside, 1-TbAd, made by pathogenic mycobacteria acts as an antacid to block mycobacterial degradation in host cell vacuoles. The antacid activity acts to reduce acidity by neutralizing the pH of these degradative cell organelles. 

References

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Mycobacterium tuberculosis releases an antacid that remodels phagosomes
TLDR
The biological function of the terpene nucleoside 1-TbAd is elucidated, which is made abundantly by virulent but not avirulent Mycobacterium tuberculosis strains, and it is demonstrated that 1-tuberculosinyladenosine regulates the pH and function of host macrophage endolysosomes.
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TLDR
Immunoelectron microscopy of infected macrophages and immunoblotting of isolated phagosomes showed that Mycobacterium vacuoles acquire the lysosomal membrane protein LAMP-1, but not the vesicular proton-adenosine triphosphatase (ATPase) responsible for phagosomal acidification.
High Content Phenotypic Cell-Based Visual Screen Identifies Mycobacterium tuberculosis Acyltrehalose-Containing Glycolipids Involved in Phagosome Remodeling
TLDR
A high throughput phenotypic cell-based assay enabling individual sub-cellular analysis of over 11,000 Mycobacterium tuberculosis mutants suggests that glycolipids indeed play a critical role in the early intracellular fate of the tubercle bacillus.
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TLDR
It is demonstrated that restriction of phagosome acidification is a prerequisite for mycobacterial phagosomal rupture and cytosolic contact, and an important conceptual advance for knowledge on host processes targeted by Mtb evasion strategies.
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TLDR
It is shown that the secreted Mtb protein tyrosine phosphatase (PtpA) binds to subunit H of the macrophage vacuolar-H+-ATPase (V- ATPase) machinery, a multisubunit protein complex in the phagosome membrane that drives luminal acidification.
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TLDR
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