Structural insight into the inactivation of Mycobacterium tuberculosis non-classical transpeptidase LdtMt2 by biapenem and tebipenem
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Cho H, Uehara T, Bernhardt TG. β-lactam antibiotics induce a lethal malfunctioning of the bacterial cell wall synthesis machinery. Cell. 2014;159(6):1300–11.
WHO. Global Tuberculosis Report. Geneva: World Health Organization; 2015.
Hugonnet JE, Blanchard JS. Irreversible inhibition of the Mycobacterium tuberculosis β-lactamase by clavulanate. Biochemistry. 2007;46(43):11998–2004.
Wivagg CN, Bhattacharyya RP, Hung DT. Mechanisms of β-lactam killing and resistance in the context of Mycobacterium tuberculosis. J Antibiotics. 2014;67(9):645–54.
Mainardi JL, Fourgeaud M, Hugonnet JE, Dubost L, Brouard JP, Ouazzani J, Rice LB, Gutmann L, Arthur M. A novel peptidoglycan cross-linking enzyme for a β-lactam-resistant transpeptidation pathway. J Biol Chem. 2005;280(46):38146–52.
Wietzerbin J, Das BC, Petit JF, Lederer E, Leyh-Bouille M, Ghuysen JM. Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria. Biochemistry. 1974;13(17):3471–6.
Lavollay M, Arthur M, Fourgeaud M, Dubost L, Marie A, Veziris N, Blanot D, Gutmann L, Mainardi JL. The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation. J Bacteriol. 2008;190(12):4360–6.
Gupta R, Lavollay M, Mainardi JL, Arthur M, Bishai WR, Lamichhane G. The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin. Nat Med. 2010;16(4):466–9.
Kumar P, Arora K, Lloyd JR, Lee IY, Nair V, Fischer E, Boshoff HI, Barry 3rd CE. Meropenem inhibits D, D-carboxypeptidase activity in Mycobacterium tuberculosis. Mol Microbiol. 2012;86(2):367–81.
Hugonnet JE, Tremblay LW, Boshoff HI, Barry 3rd CE, Blanchard JS. Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis. Science (New York NY). 2009;323(5918):1215–8.
Erdemli SB, Gupta R, Bishai WR, Lamichhane G, Amzel LM, Bianchet MA. Targeting the cell wall of Mycobacterium tuberculosis: structure and mechanism of L, D-transpeptidase 2. Structure. 2012;20(12):2103–15.
Dhar N, Dubee V, Ballell L, Cuinet G, Hugonnet JE, Signorino-Gelo F, Barros D, Arthur M, McKinney JD. Rapid Cytolysis of Mycobacterium tuberculosis by Faropenem, an Orally Bioavailable β-Lactam Antibiotic. Antimicrob Agents Chemother. 2015;59(2):1308–19.
Brammer Basta LA, Ghosh A, Pan Y, Jakoncic J, Lloyd EP, Townsend CA, Lamichhane G, Bianchet MA. Loss of a Functionally and Structurally Distinct L, D-Transpeptidase, LdtMt5, Compromises Cell Wall Integrity in Mycobacterium tuberculosis. J Biol Chem. 2015;290(42):25670–85.
Kieser KJ, Baranowski C, Chao MC, Long JE, Sassetti CM, Waldor MK, Sacchettini JC, Ioerger TR, Rubin EJ. Peptidoglycan synthesis in Mycobacterium tuberculosis is organized into networks with varying drug susceptibility. Proc Natl Acad Sci U S A. 2015;112(42):13087–92.
Schoonmaker MK, Bishai WR, Lamichhane G. Nonclassical transpeptidases of Mycobacterium tuberculosis alter cell size, morphology, the cytosolic matrix, protein localization, virulence, and resistance to β-lactams. J Bacteriol. 2014;196(7):1394–402.
Both D, Steiner EM, Stadler D, Lindqvist Y, Schnell R, Schneider G. Structure of LdtMt2, an L, D-transpeptidase from Mycobacterium tuberculosis. Acta Crystallogr Sect D: Biol Crystallogr. 2013;69(Pt 3):432–41.
Kim HS, Kim J, Im HN, Yoon JY, An DR, Yoon HJ, Kim JY, Min HK, Kim SJ, Lee JY, et al. Structural basis for the inhibition of Mycobacterium tuberculosis L, D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains. Acta Crystallogr Sect D: Biol Crystallogr. 2013;69(Pt 3):420–31.
Li WJ, Li DF, Hu YL, Zhang XE, Bi LJ, Wang DC. Crystal structure of L, D-transpeptidase LdtMt2 in complex with meropenem reveals the mechanism of carbapenem against Mycobacterium tuberculosis. Cell Res. 2013;23(5):728–31.
Kumar P, Kaushik A, Lloyd EP, Li SG, Mattoo R, Ammerman NC, Bell DT, Perryman AL, Zandi TA, Ekins S, et al. Non-classical transpeptidases yield insight into new antibacterials. Nat Chem Biol. 2017;13(1):54–61.
Steiner EM, Schneider G, Schnell R. Binding and processing of β-lactam antibiotics by the transpeptidase LdtMt2 from Mycobacterium tuberculosis. FEBS J. 2017.
Correale S, Ruggiero A, Capparelli R, Pedone E, Berisio R. Structures of free and inhibited forms of the L, D-transpeptidase LdtMt1 from Mycobacterium tuberculosis. Acta Crystallogr Sect D: Biol Crystallogr. 2013;69(Pt 9):1697–706.
Horita Y, Maeda S, Kazumi Y, Doi N. In vitro susceptibility of Mycobacterium tuberculosis isolates to an oral carbapenem alone or in combination with β-lactamase inhibitors. Antimicrob Agents Chemother. 2014;58(11):7010–4.
Kaushik A, Makkar N, Pandey P, Parrish N, Singh U, Lamichhane G. Carbapenems and Rifampin Exhibit Synergy against Mycobacterium tuberculosis and Mycobacterium abscessus. Antimicrob Agents Chemother. 2015;59(10):6561–7.
Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004;25(13):1605–12.
Gill SC, von Hippel PH. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem. 1989;182(2):319–26.
Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997;276:307–26.
McCoy AJ. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr Sect D: Biol Crystallogr. 2007;63(Pt 1):32–41.
Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, Echols N, Headd JJ, Hung LW, Kapral GJ, Grosse-Kunstleve RW, et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr Sect D: Biol Crystallogr. 2010;66(Pt 2):213–21.
Emsley P, Lohkamp B, Scott WG, Cowtan K. Features and development of Coot. Acta Crystallogr Sect D: Biol Crystallogr. 2010;66(Pt 4):486–501.
Schmidt MW, Baldrige KK, Boatz JA, Elbert ST, Gordon MS, Jensen JH, Koseki S, Matsunaga N, Nguyen KA, Su SJ, et al. General Atomic and molecular Electronic-Structure System. J Comput Chem. 1993;14:1347–63.
Dubee V, Arthur M, Fief H, Triboulet S, Mainardi JL, Gutmann L, Sollogoub M, Rice LB, Etheve-Quelquejeu M, Hugonnet JE. Kinetic analysis of Enterococcus faecium L, D-transpeptidase inactivation by carbapenems. Antimicrob Agents Chemother. 2012;56(6):3409–12.
Dubee V, Triboulet S, Mainardi JL, Etheve-Quelquejeu M, Gutmann L, Marie A, Dubost L, Hugonnet JE, Arthur M. Inactivation of Mycobacterium tuberculosis L, D-transpeptidase LdtMt1 by carbapenems and cephalosporins. Antimicrob Agents Chemother. 2012;56(8):4189–95.
Triboulet S, Dubee V, Lecoq L, Bougault C, Mainardi JL, Rice LB, Etheve-Quelquejeu M, Gutmann L, Marie A, Dubost L, et al. Kinetic features of L, D-transpeptidase inactivation critical for β-lactam antibacterial activity. PLoS One. 2013;8(7), e67831.
Eliot AC, Kirsch JF. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annu Rev Biochem. 2004;73:383–415.
Cooper AJ. Mechanisms of cysteine S-conjugate β-lyases. Adv Enzymol Relat Areas Mol Biol. 1998;72:199–238.
Drawz SM, Babic M, Bethel CR, Taracila M, Distler AM, Ori C, Caselli E, Prati F, Bonomo RA. Inhibition of the class C β-lactamase from Acinetobacter spp.: insights into effective inhibitor design. Biochemistry. 2010;49(2):329–40.
Endimiani A, Luzzaro F, Pini B, Amicosante G, Rossolini GM, Toniolo AQ. Pseudomonas aeruginosa bloodstream infections: risk factors and treatment outcome related to expression of the PER-1 extended-spectrum β-lactamase. BMC Infect Dis. 2006;6:52.