@inbook{9a75f63c108a4f2e9f070155a090b1da,
title = "Metabolic Labeling of Live Mycobacteria with Trehalose-Based Probes",
abstract = "The mycobacterial cell envelope includes a unique outer membrane, also known as the mycomembrane, which is the major defense barrier that confers intrinsic drug tolerance to Mycobacterium tuberculosis (Mtb) and related bacteria. The mycomembrane is typified by long-chain mycolic acids that are esterified to various acceptors, including: (1) trehalose, forming trehalose mono- and di-mycolate; (2) arabinogalactan, forming arabinogalactan-linked mycolates; and (3) in some species, protein serine residues, forming O-mycoloylated proteins. Synthetic trehalose and trehalose monomycolate analogs have been shown to specifically and metabolically incorporate into mycomembrane components, facilitating their analysis in native contexts and opening new avenues for the specific detection and therapeutic targeting of mycobacterial pathogens in complex settings. This chapter highlights trehalose-based probes that have been developed to date, briefly discusses their applications, and describes protocols for their use in mycobacteria research.",
keywords = "Click chemistry, Fluorescence imaging, Glycolipids, Mycomembrane, O-mycoloylated proteins, Tetrazine ligation, Trehalose",
author = "Nicholas Banahene and Swarts, {Benjamin M.}",
note = "Publisher Copyright: {\textcopyright} 2021, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2021",
doi = "10.1007/978-1-0716-1460-0_18",
language = "English",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "385--398",
booktitle = "Methods in Molecular Biology",
}
