<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Fiolek, Taylor J</style></author><author><style face="normal" font="default" size="100%">Banahene, Nicholas</style></author><author><style face="normal" font="default" size="100%">Kavunja, Herbert W</style></author><author><style face="normal" font="default" size="100%">Holmes, Nathan J</style></author><author><style face="normal" font="default" size="100%">Rylski, Adrian K</style></author><author><style face="normal" font="default" size="100%">Pohane, Amol Arunrao</style></author><author><style face="normal" font="default" size="100%">Siegrist, M Sloan</style></author><author><style face="normal" font="default" size="100%">Swarts, Benjamin M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Engineering the Mycomembrane of Live Mycobacteria with an Expanded Set of Trehalose Monomycolate Analogues.</style></title><secondary-title><style face="normal" font="default" size="100%">Chembiochem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Chembiochem</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Acyltransferases</style></keyword><keyword><style  face="normal" font="default" size="100%">Alkynes</style></keyword><keyword><style  face="normal" font="default" size="100%">Azides</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacillus subtilis</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Engineering</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Click Chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Cord Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Corynebacterium</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli</style></keyword><keyword><style  face="normal" font="default" size="100%">Fluorescent Dyes</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Structure</style></keyword><keyword><style  face="normal" font="default" size="100%">Mycobacterium smegmatis</style></keyword><keyword><style  face="normal" font="default" size="100%">Mycobacterium tuberculosis</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2019 05 15</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">1282-1291</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Mycobacteria and related organisms in the Corynebacterineae suborder are characterized by a distinctive outer membrane referred to as the mycomembrane. Biosynthesis of the mycomembrane occurs through an essential process called mycoloylation, which involves antigen 85 (Ag85)-catalyzed transfer of mycolic acids from the mycoloyl donor trehalose monomycolate (TMM) to acceptor carbohydrates and, in some organisms, proteins. We recently described an alkyne-modified TMM analogue (O-AlkTMM-C7) which, in conjunction with click chemistry, acted as a chemical reporter for mycoloylation in intact cells and allowed metabolic labeling of mycoloylated components of the mycomembrane. Here, we describe the synthesis and evaluation of a toolbox of TMM-based reporters bearing alkyne, azide, trans-cyclooctene, and fluorescent tags. These compounds gave further insight into the substrate tolerance of mycoloyltransferases (e.g., Ag85s) in a cellular context and they provide significantly expanded experimental versatility by allowing one- or two-step cell labeling, live cell labeling, and rapid cell labeling via tetrazine ligation. Such capabilities will facilitate research on mycomembrane composition, biosynthesis, and dynamics. Moreover, because TMM is exclusively metabolized by Corynebacterineae, the described probes may be valuable for the specific detection and cell-surface engineering of Mycobacterium tuberculosis and related pathogens. We also performed experiments to establish the dependence of probe incorporation on mycoloyltransferase activity, results from which suggested that cellular labeling is a function not only of metabolic incorporation (and likely removal) pathway(s), but also accessibility across the envelope. Thus, whole-cell labeling experiments with TMM reporters should be carefully designed and interpreted when envelope permeability may be compromised. On the other hand, this property of TMM reporters can potentially be exploited as a convenient way to probe changes in envelope integrity and permeability, facilitating drug development studies.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ishikawa, Eri</style></author><author><style face="normal" font="default" size="100%">Ishikawa, Tetsuaki</style></author><author><style face="normal" font="default" size="100%">Morita, Yasu S</style></author><author><style face="normal" font="default" size="100%">Toyonaga, Kenji</style></author><author><style face="normal" font="default" size="100%">Yamada, Hisakata</style></author><author><style face="normal" font="default" size="100%">Takeuchi, Osamu</style></author><author><style face="normal" font="default" size="100%">Kinoshita, Taroh</style></author><author><style face="normal" font="default" size="100%">Akira, Shizuo</style></author><author><style face="normal" font="default" size="100%">Yoshikai, Yasunobu</style></author><author><style face="normal" font="default" size="100%">Yamasaki, Sho</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Direct recognition of the mycobacterial glycolipid, trehalose dimycolate, by C-type lectin Mincle.</style></title><secondary-title><style face="normal" font="default" size="100%">J Exp Med</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Exp. Med.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cord Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Granuloma</style></keyword><keyword><style  face="normal" font="default" size="100%">Lectins, C-Type</style></keyword><keyword><style  face="normal" font="default" size="100%">Ligands</style></keyword><keyword><style  face="normal" font="default" size="100%">Lung Diseases</style></keyword><keyword><style  face="normal" font="default" size="100%">Macrophage Activation</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Inbred C57BL</style></keyword><keyword><style  face="normal" font="default" size="100%">Myeloid Differentiation Factor 88</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, IgG</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Dec 21</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">206</style></volume><pages><style face="normal" font="default" size="100%">2879-88</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Tuberculosis remains a fatal disease caused by Mycobacterium tuberculosis, which contains various unique components that affect the host immune system. Trehalose-6,6'-dimycolate (TDM; also called cord factor) is a mycobacterial cell wall glycolipid that is the most studied immunostimulatory component of M. tuberculosis. Despite five decades of research on TDM, its host receptor has not been clearly identified. Here, we demonstrate that macrophage inducible C-type lectin (Mincle) is an essential receptor for TDM. Heat-killed mycobacteria activated Mincle-expressing cells, but the activity was lost upon delipidation of the bacteria; analysis of the lipid extracts identified TDM as a Mincle ligand. TDM activated macrophages to produce inflammatory cytokines and nitric oxide, which are completely suppressed in Mincle-deficient macrophages. In vivo TDM administration induced a robust elevation of inflammatory cytokines in sera and characteristic lung inflammation, such as granuloma formation. However, no TDM-induced lung granuloma was formed in Mincle-deficient mice. Whole mycobacteria were able to activate macrophages even in MyD88-deficient background, but the activation was significantly diminished in Mincle/MyD88 double-deficient macrophages. These results demonstrate that Mincle is an essential receptor for the mycobacterial glycolipid, TDM.</style></abstract><issue><style face="normal" font="default" size="100%">13</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/20008526?dopt=Abstract</style></custom1></record></records></xml>