<?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%">García-Heredia, Alam</style></author><author><style face="normal" font="default" size="100%">Kado, Takehiro</style></author><author><style face="normal" font="default" size="100%">Sein, Caralyn E</style></author><author><style face="normal" font="default" size="100%">Puffal, Julia</style></author><author><style face="normal" font="default" size="100%">Osman, Sarah H</style></author><author><style face="normal" font="default" size="100%">Judd, Julius</style></author><author><style face="normal" font="default" size="100%">Gray, Todd A</style></author><author><style face="normal" font="default" size="100%">Morita, Yasu S</style></author><author><style face="normal" font="default" size="100%">Siegrist, M Sloan</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Membrane-partitioned cell wall synthesis in mycobacteria.</style></title><secondary-title><style face="normal" font="default" size="100%">Elife</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Elife</style></alt-title></titles><dates><year><style  face="normal" font="default" size="100%">2021</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2021 Feb 05</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">10</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Many antibiotics target the assembly of cell wall peptidoglycan, an essential, heteropolymeric mesh that encases most bacteria. In rod-shaped bacteria, cell wall elongation is spatially precise yet relies on limited pools of lipid-linked precursors that generate and are attracted to membrane disorder. By tracking enzymes, substrates, and products of peptidoglycan biosynthesis in , we show that precursors are made in plasma membrane domains that are laterally and biochemically distinct from sites of cell wall assembly. Membrane partitioning likely contributes to robust, orderly peptidoglycan synthesis, suggesting that these domains help template peptidoglycan synthesis. The cell wall-organizing protein DivIVA and the cell wall itself promote domain homeostasis. These data support a model in which the peptidoglycan polymer feeds back on its membrane template to maintain an environment conducive to directional synthesis. Our findings are applicable to rod-shaped bacteria that are phylogenetically distant from , indicating that horizontal compartmentalization of precursors may be a general feature of bacillary cell wall biogenesis.&lt;/p&gt;
</style></abstract></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%">Koyasseril-Yehiya, Thameez M</style></author><author><style face="normal" font="default" size="100%">García-Heredia, Alam</style></author><author><style face="normal" font="default" size="100%">Anson, Francesca</style></author><author><style face="normal" font="default" size="100%">Rangadurai, Poornima</style></author><author><style face="normal" font="default" size="100%">Siegrist, M Sloan</style></author><author><style face="normal" font="default" size="100%">Thayumanavan, S</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Supramolecular antibiotics: a strategy for conversion of broad-spectrum to narrow-spectrum antibiotics for .</style></title><secondary-title><style face="normal" font="default" size="100%">Nanoscale</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Nanoscale</style></alt-title></titles><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2020 Oct 22</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">20693-20698</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The propensity of broad-spectrum antibiotics to indiscriminately kill both pathogenic and beneficial bacteria has a profound impact on the spread of resistance across multiple bacterial species. Alternative approaches that narrow antibacterial specificity towards desired pathogenic bacterial population are of great interest. Here, we report an enzyme-responsive antibiotic-loaded nanoassembly strategy for narrow delivery of otherwise broad-spectrum antibiotics. We specifically target Staphylococcus aureus (S. aureus), an important blood pathogen that secretes PC1 &amp;beta;-lactamases. Our nanoassemblies selectively eradicate S. aureus grown in vitro with other bacteria, highlighting its potential capability in targeting the desired pathogenic bacterial population.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">40</style></issue></record></records></xml>