Please use this identifier to cite or link to this item:
https://doi.org/10.7554/eLife.37516
DC Field | Value | |
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dc.title | Maturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape | |
dc.contributor.author | Baranowski, C | |
dc.contributor.author | Welsh, M.A | |
dc.contributor.author | Sham, L.-T | |
dc.contributor.author | Eskandarian, H.A | |
dc.contributor.author | Lim, H.C | |
dc.contributor.author | Kieser, K.J | |
dc.contributor.author | Wagner, J.C | |
dc.contributor.author | McKinney, J.D | |
dc.contributor.author | Fantner, G.E | |
dc.contributor.author | Ioerger, T.R | |
dc.contributor.author | Walker, S | |
dc.contributor.author | Bernhardt, T.G | |
dc.contributor.author | Rubin, E.J | |
dc.contributor.author | Rego, E.H | |
dc.date.accessioned | 2020-10-20T03:30:37Z | |
dc.date.available | 2020-10-20T03:30:37Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Baranowski, C, Welsh, M.A, Sham, L.-T, Eskandarian, H.A, Lim, H.C, Kieser, K.J, Wagner, J.C, McKinney, J.D, Fantner, G.E, Ioerger, T.R, Walker, S, Bernhardt, T.G, Rubin, E.J, Rego, E.H (2018). Maturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape. eLife 7 : e37516. ScholarBank@NUS Repository. https://doi.org/10.7554/eLife.37516 | |
dc.identifier.issn | 2050084X | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/177836 | |
dc.description.abstract | In most well-studied rod-shaped bacteria, peptidoglycan is primarily crosslinked by penicillin-binding proteins (PBPs). However, in mycobacteria, crosslinks formed by L,D-transpeptidases (LDTs) are highly abundant. To elucidate the role of these unusual crosslinks, we characterized Mycobacterium smegmatis cells lacking all LDTs. We find that crosslinks generate by LDTs are required for rod shape maintenance specifically at sites of aging cell wall, a byproduct of polar elongation. Asymmetric polar growth leads to a non-uniform distribution of these two types of crosslinks in a single cell. Consequently, in the absence of LDT-mediated crosslinks, PBP-catalyzed crosslinks become more important. Because of this, Mycobacterium tuberculosis (Mtb) is more rapidly killed using a combination of drugs capable of PBP-and LDT-inhibition. Thus, knowledge about the spatial and genetic relationship between drug targets can be exploited to more effectively treat this pathogen. © Baranowski et al. | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.source | Unpaywall 20201031 | |
dc.subject | amoxicillin | |
dc.subject | amoxicillin plus clavulanic acid | |
dc.subject | beta lactam | |
dc.subject | binding protein | |
dc.subject | carbapenem | |
dc.subject | carboxypeptidase D | |
dc.subject | carboxypeptidase transpeptidase | |
dc.subject | hygromycin | |
dc.subject | meropenem | |
dc.subject | peptidoglycan | |
dc.subject | amino acid | |
dc.subject | aminoacyltransferase | |
dc.subject | amoxicillin | |
dc.subject | cross linking reagent | |
dc.subject | meropenem | |
dc.subject | penicillin binding protein | |
dc.subject | peptidoglycan | |
dc.subject | peptidoglycan transpeptidase | |
dc.subject | Agrobacterium tumefaciens | |
dc.subject | Article | |
dc.subject | atomic force microscopy | |
dc.subject | bacterial strain | |
dc.subject | bacterium culture | |
dc.subject | canonical analysis | |
dc.subject | cell division | |
dc.subject | controlled study | |
dc.subject | CRISPR Cas system | |
dc.subject | cross linking | |
dc.subject | daughter cell | |
dc.subject | Escherichia coli | |
dc.subject | fluorescence | |
dc.subject | fluorescence activated cell sorting | |
dc.subject | fractional anisotropy | |
dc.subject | genetic analysis | |
dc.subject | genetic linkage | |
dc.subject | genetic manipulation | |
dc.subject | MIC50 | |
dc.subject | microscopy | |
dc.subject | minimum inhibitory concentration | |
dc.subject | morphological trait | |
dc.subject | Mycobacterium smegmatis | |
dc.subject | nonhuman | |
dc.subject | organelle shape | |
dc.subject | osmolarity | |
dc.subject | polymerization | |
dc.subject | population | |
dc.subject | protein expression | |
dc.subject | real time polymerase chain reaction | |
dc.subject | sequence analysis | |
dc.subject | single cell analysis | |
dc.subject | sputum analysis | |
dc.subject | time-lapse microscopy | |
dc.subject | tuberculosis | |
dc.subject | Bacillus | |
dc.subject | biological model | |
dc.subject | cell wall | |
dc.subject | chemistry | |
dc.subject | drug effect | |
dc.subject | kinetics | |
dc.subject | metabolism | |
dc.subject | microbial viability | |
dc.subject | Mycobacterium smegmatis | |
dc.subject | Amino Acids | |
dc.subject | Aminoacyltransferases | |
dc.subject | Amoxicillin | |
dc.subject | Bacillus | |
dc.subject | Cell Wall | |
dc.subject | Cross-Linking Reagents | |
dc.subject | Escherichia coli | |
dc.subject | Fluorescence | |
dc.subject | Kinetics | |
dc.subject | Meropenem | |
dc.subject | Microbial Viability | |
dc.subject | Models, Biological | |
dc.subject | Mycobacterium smegmatis | |
dc.subject | Penicillin-Binding Proteins | |
dc.subject | Peptidoglycan | |
dc.type | Article | |
dc.contributor.department | MICROBIOLOGY AND IMMUNOLOGY | |
dc.description.doi | 10.7554/eLife.37516 | |
dc.description.sourcetitle | eLife | |
dc.description.volume | 7 | |
dc.description.page | e37516 | |
Appears in Collections: | Staff Publications Elements |
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