@article {380,
	title = {Three mitochondrial DNA polymerases are essential for kinetoplast DNA replication and survival of bloodstream form Trypanosoma brucei.},
	journal = {Eukaryot Cell},
	volume = {10},
	year = {2011},
	month = {2011 Jun},
	pages = {734-43},
	abstract = {Trypanosoma brucei, the causative agent of human African trypanosomiasis, has a complex life cycle that includes multiple life cycle stages and metabolic changes as the parasite switches between insect vector and mammalian host. The parasite{\textquoteright}s single mitochondrion contains a unique catenated mitochondrial DNA network called kinetoplast DNA (kDNA) that is composed of minicircles and maxicircles. Long-standing uncertainty about the requirement of kDNA in bloodstream form (BF) T. brucei has recently eroded, with reports of posttranscriptional editing and subsequent translation of kDNA-encoded transcripts as essential processes for BF parasites. These studies suggest that kDNA and its faithful replication are indispensable for this life cycle stage. Here we demonstrate that three kDNA replication proteins (mitochondrial DNA polymerases IB, IC, and ID) are required for BF parasite viability. Silencing of each polymerase was lethal, resulting in kDNA loss, persistence of prereplication DNA monomers, and collapse of the mitochondrial membrane potential. These data demonstrate that kDNA replication is indeed crucial for BF T. brucei. The contributions of mitochondrial DNA polymerases IB, IC, and ID to BF parasite viability suggest that these and other kDNA replication proteins warrant further investigation as a new class of targets for the development of antitrypanosomal drugs.},
	keywords = {Cell Survival, Cells, Cultured, DNA Replication, DNA, Kinetoplast, DNA-Directed DNA Polymerase, Humans, Membrane Potential, Mitochondrial, Mitochondria, Parasitemia, RNA Interference, Trypanosoma brucei brucei, Trypanosomiasis, African},
	issn = {1535-9786},
	doi = {10.1128/EC.05008-11},
	author = {Bruhn, David F and Sammartino, Mark P and Klingbeil, Michele M}
}
@article {716,
	title = {Caveolin-2 associates with intracellular chlamydial inclusions independently of caveolin-1.},
	journal = {BMC Infect Dis},
	volume = {4},
	year = {2004},
	month = {2004 Jul 22},
	pages = {23},
	abstract = {BACKGROUND: Lipid raft domains form in plasma membranes of eukaryotic cells by the tight packing of glycosphingolipids and cholesterol. Caveolae are invaginated structures that form in lipid raft domains when the protein caveolin-1 is expressed. The Chlamydiaceae are obligate intracellular bacterial pathogens that replicate entirely within inclusions that develop from the phagocytic vacuoles in which they enter. We recently found that host cell caveolin-1 is associated with the intracellular vacuoles and inclusions of some chlamydial strains and species, and that entry of those strains depends on intact lipid raft domains. Caveolin-2 is another member of the caveolin family of proteins that is present in caveolae, but of unknown function.

METHODS: We utilized a caveolin-1 negative/caveolin-2 positive FRT cell line and laser confocal immunofluorescence techniques to visualize the colocalization of caveolin-2 with the chlamydial inclusions.

RESULTS: We show here that in infected HeLa cells, caveolin-2, as well as caveolin-1, colocalizes with inclusions of C. pneumoniae (Cp), C. caviae (GPIC), and C. trachomatis serovars E, F and K. In addition, caveolin-2 also associates with C. trachomatis serovars A, B and C, although caveolin-1 did not colocalize with these organisms. Moreover, caveolin-2 appears to be specifically, or indirectly, associated with the pathogens at the inclusion membranes. Using caveolin-1 deficient FRT cells, we show that although caveolin-2 normally is not transported out of the Golgi in the absence of caveolin-1, it nevertheless colocalizes with chlamydial inclusions in these cells. However, our results also show that caveolin-2 did not colocalize with UV-irradiated Chlamydia in FRT cells, suggesting that in these caveolin-1 negative cells, pathogen viability and very likely pathogen gene expression are necessary for the acquisition of caveolin-2 from the Golgi.

CONCLUSION: Caveolin-2 associates with the chlamydial inclusion independently of caveolin-1. The function of caveolin-2, either in the uninfected cell or in the chlamydial developmental cycle, remains to be elucidated. Nevertheless, this second caveolin protein can now be added to the small number of host proteins that are associated with the inclusions of this obligate intracellular pathogen.},
	keywords = {Animals, Blotting, Western, Caveolin 1, Caveolin 2, Caveolins, Cells, Cultured, Chlamydia, Fluorescent Antibody Technique, Golgi Apparatus, Guinea Pigs, HeLa Cells, Humans, Mice, Microscopy, Confocal, Rats, Vacuoles, Virulence},
	issn = {1471-2334},
	doi = {10.1186/1471-2334-4-23},
	author = {Webley, Wilmore C and Norkin, Leonard C and Stuart, Elizabeth S}
}
@article {1729,
	title = {Effect of chloroquine on cultured fibroblasts: release of lysosomal hydrolases and inhibition of their uptake.},
	journal = {Biochem Biophys Res Commun},
	volume = {66},
	year = {1975},
	month = {1975 Oct 27},
	pages = {1338-43},
	keywords = {Biological Transport, Cells, Cultured, Cerebroside-Sulfatase, Chloroquine, Dextrans, Fibroblasts, Glucuronidase, Humans, Leukodystrophy, Metachromatic, Lysosomes, Pinocytosis, Skin, Sulfatases},
	issn = {0006-291X},
	author = {Wiesmann, U N and DiDonato, S and Herschkowitz, N N}
}
