Probing the mycobacterial trehalome with bioorthogonal chemistry

Benjamin M. Swarts; Cynthia M. Holsclaw; John C. Jewett; Marina Alber; Douglas M. Fox; M. Sloan Siegrist; Julie A. Leary; Rainer Kalscheuer; Carolyn R. Bertozzi

doi:10.1021/ja3062419

Probing the mycobacterial trehalome with bioorthogonal chemistry

Benjamin M. Swarts
, Cynthia M. Holsclaw
, John C. Jewett
, Marina Alber
, Douglas M. Fox
, M. Sloan Siegrist
, Julie A. Leary
, Rainer Kalscheuer
, Carolyn R. Bertozzi

Research output: Contribution to journal › Article › peer-review

159 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	16123-16126
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	134
Issue number	39
DOIs	https://doi.org/10.1021/ja3062419
State	Published - Oct 3 2012

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja3062419

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title = "Probing the mycobacterial trehalome with bioorthogonal chemistry",

abstract = "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.",

author = "Swarts, \{Benjamin M.\} and Holsclaw, \{Cynthia M.\} and Jewett, \{John C.\} and Marina Alber and Fox, \{Douglas M.\} and Siegrist, \{M. Sloan\} and Leary, \{Julie A.\} and Rainer Kalscheuer and Bertozzi, \{Carolyn R.\}",

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AU - Swarts, Benjamin M.

AU - Holsclaw, Cynthia M.

AU - Jewett, John C.

AU - Alber, Marina

AU - Fox, Douglas M.

AU - Siegrist, M. Sloan

AU - Leary, Julie A.

AU - Kalscheuer, Rainer

AU - Bertozzi, Carolyn R.

PY - 2012/10/3

Y1 - 2012/10/3

N2 - 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.

AB - 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.

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JO - Journal of the American Chemical Society

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Probing the mycobacterial trehalome with bioorthogonal chemistry

Abstract

ASJC Scopus subject areas

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