@article {2623,
	title = {Supramolecular antibiotics: a strategy for conversion of broad-spectrum to narrow-spectrum antibiotics for .},
	journal = {Nanoscale},
	volume = {12},
	year = {2020},
	month = {2020 Oct 22},
	pages = {20693-20698},
	abstract = {<p>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 \&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.</p>
},
	issn = {2040-3372},
	doi = {10.1039/d0nr04886k},
	author = {Koyasseril-Yehiya, Thameez M and Garc{\'\i}a-Heredia, Alam and Anson, Francesca and Rangadurai, Poornima and Siegrist, M Sloan and Thayumanavan, S}
}
@article {1440,
	title = {Subpolar addition of new cell wall is directed by DivIVA in mycobacteria.},
	journal = {Proc Natl Acad Sci U S A},
	volume = {111},
	year = {2014},
	month = {2014 Aug 5},
	pages = {E3243-51},
	abstract = {<p>Mycobacteria are surrounded by a complex multilayered envelope and elongate at the poles. The principles that organize the coordinated addition of chemically diverse cell wall layers during polar extension remain unclear. We show that enzymes mediating the terminal cytosolic steps of peptidoglycan, arabinogalactan, and mycolic acid synthesis colocalize at sites of cell growth or division. The tropomyosin-like protein, DivIVA, is targeted to the negative curvature of the pole, is enriched at the growing end, and determines cell shape from this site. In contrast, cell wall synthetic complexes are concentrated at a distinct subpolar location. When viewed at subdiffraction resolution, new peptidoglycan is deposited at this subpolar site, and inert cell wall covers the DivIVA-marked tip. The differentiation between polar tip and cell wall synthetic complexes is also apparent at the biochemical level. Enzymes that generate mycolate precursors interact with DivIVA, but the final condensation of mycolic acids occurs in a distinct protein complex at the site of nascent cell wall addition. We propose an ultrastructural model of mycobacterial polar growth where new cell wall is added in an annular zone below the cell tip. This model may be broadly applicable to other bacterial and fungal organisms that grow via polar extension.</p>},
	keywords = {Bacterial Proteins, Cell Cycle Proteins, Cell Membrane, Cell Polarity, Cell Wall, Models, Biological, Mycobacterium smegmatis, Mycolic Acids, Protein Binding},
	issn = {1091-6490},
	doi = {10.1073/pnas.1402158111},
	author = {Meniche, Xavier and Otten, Renee and Siegrist, M Sloan and Baer, Christina E and Murphy, Kenan C and Bertozzi, Carolyn R and Sassetti, Christopher M}
}
