@article {1446,
	title = {Probing the mycobacterial trehalome with bioorthogonal chemistry.},
	journal = {J Am Chem Soc},
	volume = {134},
	year = {2012},
	month = {2012 Oct 3},
	pages = {16123-6},
	abstract = {<p>Mycobacteria, including the pathogen Mycobacterium tuberculosis, use the non-mammalian disaccharide trehalose as a precursor for essential cell-wall glycolipids and other metabolites. Here we describe a strategy for exploiting trehalose metabolic pathways to label glycolipids in mycobacteria with azide-modified trehalose (TreAz) analogues. Subsequent bioorthogonal ligation with alkyne-functionalized probes enabled detection and visualization of cell-surface glycolipids. Characterization of the metabolic fates of four TreAz analogues revealed unique labeling routes that can be harnessed for pathway-targeted investigation of the mycobacterial trehalome.</p>},
	keywords = {Alkynes, Azides, Fluorescent Dyes, Glycolipids, Mycobacterium, Trehalose},
	issn = {1520-5126},
	doi = {10.1021/ja3062419},
	author = {Swarts, Benjamin M and Holsclaw, Cynthia M and Jewett, John C and Alber, Marina and Fox, Douglas M and Siegrist, M Sloan and Leary, Julie A and Kalscheuer, Rainer and Bertozzi, Carolyn R}
}
@article {857,
	title = {Cell surface display of the chlamydial glycolipid exoantigen (GLXA) demonstrated by antibody-dependent complement-mediated cytotoxicity.},
	journal = {Curr Microbiol},
	volume = {49},
	year = {2004},
	month = {2004 Jul},
	pages = {13-21},
	abstract = {The chlamydial species are Gram-negative bacterial pathogens critical to human health. Their developmental cycle is associated with the formation and release of the broadly conserved glycolipid exoantigen (GLXA), which has been implicated in the chlamydial elementary body-host cell interaction. This study examines the potential surface display of this glycolipid by chlamydiae-infected cells and the ability of the GLXA they secrete to associate with the plasma membranes of uninfected cells, a prerequisite for exerting influence on them. The sequential incubation of anti-GLXA antibody and complement with Chlamydia trachomatis serovar K or C. pneumoniae AR-39-infected HeLa 229 or macrophage cells resulted in significant cellular cytotoxicity, which preceded the formation of mature elementary bodies. For uninfected cells, co-incubation of GLXA, purified from supernatants of either C. trachomatis or C. pneumoniae-infected HeLa 229 cells, followed by the successive addition of mouse anti-GLXA antibody and complement, yielded similar levels of cellular cytotoxicity. Thus, GLXA indeed is displayed on the surface of infected cells and, therefore, if antibody of appropriate specificity were present, this GLXA could serve to target these infected cells for elimination. Furthermore, released GLXA can associate with uninfected cells and therefore would be positioned to influence their behavior, especially in the context of infection.},
	keywords = {Antibody Specificity, Chlamydia, Complement System Proteins, Glycolipids, HeLa Cells, Humans, Polysaccharides, Bacterial},
	issn = {0343-8651},
	doi = {10.1007/s00284-003-4181-7},
	author = {Webley, Wilmore C and Vora, Gary J and Stuart, Elizabeth S}
}
