Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy

被引：264

作者：

Alonso, Sylvie ^{[1
]}

Pethe, Kevin ^{[1
]}

Russell, David G. ^{[1
]}

Purdy, Georgiana E. ^{[1
]}

机构：

[1] Cornell Univ, Coll Vet Med, Dept Microbiol & Immunol, Ithaca, NY 14853 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2007年 / 104卷 / 14期

关键词：

macrophage; phagosome; tuberculosis; lysosome;

D O I：

10.1073/pnas.0700036104

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 [理学]; 0710 [生物学]; 09 [农学];

摘要：

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.

引用

页码：6031 / 6036

页数：6

共 41 条

[1]

Autophagy is an immediate macrophage response to Legionella pneumophila [J].