Please use this identifier to cite or link to this item:
|Title:||Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy|
|Authors:||Alonso, S. |
|Source:||Alonso, S., Pethe, K., Russell, D.G., Purdy, G.E. (2007-04-03). Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy. Proceedings of the National Academy of Sciences of the United States of America 104 (14) : 6031-6036. ScholarBank@NUS Repository. https://doi.org/10.1073/pnas.0700036104|
|Abstract:||Mycobacterium tuberculosis parasitizes resting macrophages yet is killed by activated macrophages through both oxidative and nonoxidative mechanisms. Nonoxidative mechanisms are linked to the maturation of the bacteria-containing phagosome into an acidified, hydrolytically active compartment. We describe here a mechanism for killing Mycobacteria in the lysosomal compartment through the activity of peptides generated by the hydrolysis of ubiquitin. The induction of autophagy in infected macrophages enhanced the delivery of ubiquitin conjugates to the lysosome and increased the bactericidal capacity of the lysosomal soluble fraction. The accumulation of ubiquitinated proteins in the autophagolysosome provides one possible mechanism behind the antimicrobial activities observed for a range of pathogens in autophagous host cells. © 2007 by The National Academy of Sciences of the USA.|
|Source Title:||Proceedings of the National Academy of Sciences of the United States of America|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jan 17, 2018
WEB OF SCIENCETM
checked on Dec 13, 2017
checked on Jan 15, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.