@article {1443,
	title = {Mycobacterial lipid logic.},
	journal = {Cell Host Microbe},
	volume = {15},
	year = {2014},
	month = {2014 Jan 15},
	pages = {1-2},
	abstract = {<p>During infection of the lung epithelium, Mycobacterium tuberculosis must infect and survive within macrophages long enough to be transported into deeper lung tissues. Cambier et~al. (2013) show that pathogenic mycobacteria use the coordinated action of two cell wall glycolipids to regulate macrophage recruitment to initial infection sites.</p>},
	keywords = {Animals, Female, Immune Evasion, Macrophages, Membrane Lipids, Mycobacterium},
	issn = {1934-6069},
	doi = {10.1016/j.chom.2013.12.005},
	author = {Siegrist, M Sloan and Bertozzi, Carolyn R}
}
@article {1447,
	title = {Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition.},
	journal = {Proc Natl Acad Sci U S A},
	volume = {106},
	year = {2009},
	month = {2009 Nov 3},
	pages = {18792-7},
	abstract = {<p>The Esx secretion pathway is conserved across Gram-positive bacteria. Esx-1, the best-characterized system, is required for virulence of Mycobacterium tuberculosis, although its precise function during infection remains unclear. Esx-3, a paralogous system present in all mycobacterial species, is required for growth in vitro. Here, we demonstrate that mycobacteria lacking Esx-3 are defective in acquiring iron. To compete for the limited iron available in the host and the environment, these organisms use mycobactin, high-affinity iron-binding molecules. In the absence of Esx-3, mycobacteria synthesize mycobactin but are unable to use the bound iron and are impaired severely for growth during macrophage infection. Mycobacteria thus require a specialized secretion system for acquiring iron from siderophores.</p>},
	keywords = {Animals, Bacterial Proteins, Genome, Bacterial, Iron, Macrophages, Mice, Mutation, Mycobacterium, Mycobacterium Infections, Oxazoles, Protein Binding, Secretory Pathway, Siderophores, Transcription, Genetic, Up-Regulation},
	issn = {1091-6490},
	doi = {10.1073/pnas.0900589106},
	author = {Siegrist, M Sloan and Unnikrishnan, Meera and McConnell, Matthew J and Borowsky, Mark and Cheng, Tan-Yun and Siddiqi, Noman and Fortune, Sarah M and Moody, D Branch and Rubin, Eric J}
}
@article {712,
	title = {Association of caveolin with Chlamydia trachomatis inclusions at early and late stages of infection.},
	journal = {Exp Cell Res},
	volume = {266},
	year = {2001},
	month = {2001 Jun 10},
	pages = {229-38},
	abstract = {The mechanism by which the intracellular bacterial pathogen Chlamydia trachomatis enters eukaryotic cells is poorly understood. There are conflicting reports of entry occurring by clathrin-dependent and clathrin-independent processes. We report here that C. trachomatis serovar K enters HEp-2 and HeLa 229 epithelial cells and J-774A.1 mouse macrophage/monocyte cells via caveolin-containing sphingolipid and cholesterol-enriched raft microdomains in the host cell plasma membranes. First, filipin and nystatin, drugs that specifically disrupt raft function by cholesterol chelation, each impaired entry of C. trachomatis serovar K. In control experiments, filipin did not impair entry of the same organism by an antibody-mediated opsonic process, nor did it impair entry of BSA-coated microspheres. Second, the chlamydia-containing endocytic vesicles specifically reacted with antisera against the caveolae marker protein caveolin. These vesicles are known to become the inclusions in which parasite replication occurs. They avoid fusion with lysosomes and instead traffic to the Golgi region, where they intercept Golgi-derived vesicles that recycle sphingolipids and cholesterol to the plasma membrane. We also report that late-stage C. trachomatis inclusions continue to display high levels of caveolin, which they likely acquire from the exocytic Golgi vesicles. We suggest that the atypical raft-mediated entry process may have important consequences for the host-pathogen interaction well after entry has occurred. These consequences include enabling the chlamydial vesicle to avoid acidification and fusion with lysosomes, to traffic to the Golgi region, and to intercept sphingolipid-containing vesicles from the Golgi.},
	keywords = {Animals, Caveolin 1, Caveolins, Cell Line, Chlamydia trachomatis, Epithelium, Filipin, HeLa Cells, Humans, Inclusion Bodies, Macrophages, Membrane Microdomains, Mice, Nystatin, Phagosomes},
	issn = {0014-4827},
	doi = {10.1006/excr.2001.5202},
	author = {Norkin, L C and Wolfrom, S A and Stuart, E S}
}
