Journal
JOURNAL OF BACTERIOLOGY
Volume 191, Issue 14, Pages 4546-4554Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.00245-09
Keywords
-
Categories
Funding
- Swiss National Science Foundation
- Lungenliga
- Olga Mayenfisch Stiftung
- Swiss Life Foundation
- Kanton Basel Stadt
Ask authors/readers for more resources
Pathogenic mycobacteria survive within macrophages through the inhibition of phagosome-lysosome fusion. A crucial factor for avoiding lysosomal degradation is the mycobacterial serine/threonine protein kinase G (PknG). PknG is released into the macrophage cytosol upon mycobacterial infection, suggesting that PknG might exert its activity by interfering with host signaling cascades, but the mode of action of PknG remains unknown. Here, we show that PknG undergoes autophosphorylation on threonine residues located at the N terminus. In contrast to all other mycobacterial kinases investigated thus far, autophosphorylation of PknG was not involved in the regulation of its kinase activity. However, autophosphorylation was crucial for the capacity of PknG to promote mycobacterial survival within macrophages. These results will contribute to a better understanding of the virulence mechanisms of pathogenic mycobacteria and may help to design improved inhibitors of PknG to be developed as antimycobacterial compounds.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available