Keywords: Dormancy, Mycobacteria, Resuscitation, Structure, Hydrolase, Peptidoglycan, Article, Bacterial Cell Wall, Bacterial Growth, Bacterial Phenomena And Functions, Bacterial Resuscitation, Bacterial Survival, Cell Growth, Chemical Composition, Chemical Structure, Gram Negative Bacterium, Gram Positive Bacterium, Molecular Interaction, Nonhuman, Protein Structure, Cell Wall Chemistry
, Mycobacterium Tuberculosis Chemistry Cytology Growth, Development Physiology,
Affiliations: *** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, Naples, Italy.. alessia.ruggiero@unina.it.
References: Galperin, M.Y., Mekhedov, S.L., Puigbo, P., Smirnov, S., Wolf, Y.I., Rigden, D.J., Genomic determinants of sporulation in Bacilli and Clostridia: Towards the minimal set of sporulation-specific genes (2012) Environ. Microbiol., 14 (11), pp. 2870-289
Menozzi, F.D., Reddy, V.M., Cayet, D., Raze, D., Debrie, A.S., Dehouck, M.P., Cecchelli, R., Locht, C., Mycobacterium tuberculosis heparin-binding haemagglutinin adhesin (HBHA) triggers receptormediated transcytosis without altering the integrity of tight junctions (2006) Microbes Infect, 8, pp. 1-9
Esposito, C., Marasco, D., Delogu, G., Pedone, E., Berisio, R., Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation (2011) Biochem. Biophys. Res. Commun., 410 (2), pp. 339-344
Esposito, C., Carullo, P., Pedone, E., Graziano, G., Vecchio, P.D., Berisio, R., Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: Implications for bacterial agglutination (2010) FEBS Lett. 2010, 584 (6), pp. 1091-1096
Esposito, C., Pethoukov, M.V., Svergun, D.I., Ruggiero, A., Pedone, C., Pedone, E., Berisio, R., Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis (2008) J. Bacteriol., 190 (13), pp. 4749-4753
Barry, C.E., Boshoff, H.I., Dartois, V., Dick, T., Ehrt, S., Flynn, J., Schnappinger, D., Young, D., The spectrum of latent tuberculosis: Rethinking the biology and intervention strategies (2009) Nat. Rev. Microbiol., 7 (12), pp. 845-855
Koul, A., Arnoult, E., Lounis, N., Guillemont, J., Andries, K., The challenge of new drug discovery for tuberculosis (2011) Nature, 469 (7331), pp. 483-490
Kaufmann, S.H., McMichael, A.J., Annulling a dangerous liaison: Vaccination strategies against AIDS and tuberculosis (2005) Nat. Med., 11 (4), pp. S33-S44
Johnson, J.W., Fisher, J.F., Mobashery, S., Bacterial cell-wall recycling (2013) Ann. N. Y. Acad. Sci., 1277, pp. 54-75
Romano, M., Van De Weerd, R., Brouwer, F.C., Roviello, G.N., Lacroix, R., Sparrius, M., Van Den Brink-Van Stempvoort, G., Berisio, R., Structure and function of RNase AS, a polyadenylatespecific exoribonuclease affecting mycobacterial virulence in vivo (2014) Structure, 22 (5), pp. 719-730
Moulder, J.W., Why is Chlamydia sensitive to penicillin in the absence of peptidoglycan (1993) Infect. Agents Dis., 2 (2), pp. 87-99
Braun, V., Covalent lipoprotein from the outer membrane of Escherichia coli (1975) Biochim. Biophys. Acta, 415 (3), pp. 335-377
Shockman, G.D., Barrett, J.F., Structure, function, and assembly of cell walls of gram-positive bacteria (1983) Annu. Rev. Microbiol., 37, pp. 501-527
Graham, L.L., Harris, R., Villiger, W., Beveridge, T.J., Freezesubstitution of gram-negative eubacteria: General cell morphology and envelope profiles (1991) J. Bacteriol., 173 (5), pp. 1623-1633
Favrot, L., Ronning, D.R., Targeting the mycobacterial envelope for tuberculosis drug development (2012) Expert Rev. Anti Infect. Ther., 10 (9), pp. 1023-1036
Li, K., Schurig-Briccio, L.A., Feng, X., Upadhyay, A., Pujari, V., Lechartier, B., Fontes, F.L., Zhu, W., Multitarget drug discovery for tuberculosis and other infectious diseases (2014) J. Med. Chem., 57 (7), pp. 3126-3139
Ioerger, T.R., O'Malley, T., Liao, R., Guinn, K.M., Hickey, M.J., Mohaideen, N., Murphy, K.C., Rubin, E.J., Identification of new drug targets and resistance mechanisms in Mycobacterium tuberculosis (2013) PLoS One, 8 (9), p. e75245
Ishizaki, Y., Hayashi, C., Inoue, K., Igarashi, M., Takahashi, Y., Pujari, V., Crick, D.C., Nomoto, A., Inhibition of the First Step in Synthesis of the Mycobacterial Cell Wall Core, Catalyzed by the GlcNAc-1-phosphate Transferase WecA, by the Novel Caprazamycin Derivative CPZEN-45 (2013) J. Biol. Chem., 288 (42), pp. 30309-30319
Park, J.T., The convergence of murein recycling research with betalactamase research (1996) Microb. Drug Resist., 2 (1), pp. 105-112
Weidel, W., Pelzer, H., Bagshaped macromolecules-A new outlook on bacterial cell walls (1964) Adv. Enzymol. Relat. Areas Mol. Biol., 26, pp. 193-232
Ward, J.B., The chain length of the glycans in bacterial cell walls (1973) Biochem. J., 133 (2), pp. 395-398
Dmitriev, B.A., Toukach, F.V., Holst, O., Rietschel, E.T., Ehlers, S., Tertiary structure of Staphylococcus aureus cell wall murein (2004) J. Bacteriol., 186 (21), pp. 7141-7148
Shah, I.M., Laaberki, M.H., Popham, D.L., Dworkin, J., A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments (2008) Cell, 135 (3), pp. 486-496
Lavollay, M., Arthur, M., Fourgeaud, M., Dubost, L., Marie, A., Veziris, N., Blanot, D., Mainardi, J.L., The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L, Dtranspeptidation (2008) J. Bacteriol., 190 (12), pp. 4360-4366
Dubee, V., Triboulet, S., Mainardi, J.L., Etheve-Quelquejeu, M., Gutmann, L., Marie, A., Dubost, L., Arthur, M., Inactivation of Mycobacterium tuberculosis l, d-transpeptidase LdtMt(1) by carbapenems and cephalosporins (2012) Antimicrob. Agents Chemother., 56 (8), pp. 4189-4195
Gupta, R., Lavollay, M., Mainardi, J.L., Arthur, M., Bishai, W.R., Lamichhane, G., The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin (2010) Nat. Med., 16 (4), pp. 466-469
Lecoq, L., Bougault, C., Hugonnet, J.E., Veckerle, C., Pessey, O., Arthur, M., Simorre, J.P., Dynamics induced by beta-lactam antibiotics in the active site of Bacillus subtilis L, D-transpeptidase (2012) Structure, 20 (5), pp. 850-861
Mesnage, S., Chau, F., Dubost, L., Arthur, M., Role of Nacetylglucosaminidase and N-acetylmuramidase activities in Enterococcus faecalis peptidoglycan metabolism (2008) J. Biol. Chem., 283 (28), pp. 19845-19853
Prigozhin, D.M., Mavrici, D., Huizar, J.P., Vansell, H.J., Alber, T., Structural and biochemical analyses of Mycobacterium tuberculosis N-acetylmuramyl-L-alanine amidase 3717 point to a role in peptidoglycan fragment recycling (2013) J. Biol. Chem., 288 (44), pp. 31549-31555
Rocaboy, M., Herman, R., Sauvage, E., Remaut, H., Moonens, K., Terrak, M., Charlier, P., Kerff, F., The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain (2013) Mol. Microbiol., 90 (2), pp. 267-277
Chaloupka, J., Kreckova, P., Rihova, L., The mucopeptide turnover in the cell walls of growing cultures of Bacillus megaterium KM (1962) Experientia, 18, pp. 362-363
Rogers, H.J., The structure and biosynthesis of the components of the cell walls of gram-positive bacteria (1967) Folia Microbiol. (Praha), 12 (3), pp. 191-200
Mauck, J., Chan, L., Glaser, L., Turnover of the cell wall of Grampositive bacteria (1971) J. Biol. Chem., 246 (6), pp. 1820-1827
Boothby, D., Daneo-Moore, L., Higgins, M.L., Coyette, J., Shockman, G.D., Turnover of bacterial cell wall peptidoglycans (1973) J. Biol. Chem., 248 (6), pp. 2161-2169
Doyle, R.J., Chaloupka, J., Vinter, V., Turnover of cell walls in microorganisms (1988) Microbiol. Rev., 52 (4), pp. 554-567
Merad, T., Archibald, A.R., Hancock, I.C., Harwood, C.R., Hobot, J.A., Cell wall assembly in Bacillus subtilis: Visualization of old and new wall material by electron microscopic examination of samples stained selectively for teichoic acid and teichuronic acid (1989) J. Gen. Microbiol., 135 (6), pp. 645-655
Pooley, H.M., Turnover and spreading of old wall during surface growth of Bacillus subtilis (1976) J. Bacteriol., 125 (3), pp. 1127-1138
Graham, L.L., Beveridge, T.J., Structural differentiation of the Bacillus subtilis 168 cell wall (1994) J. Bacteriol., 176 (5), pp. 1413-1421
Dajkovic, A., Lutkenhaus, J., Z ring as executor of bacterial cell division (2006) J. Mol. Microbiol. Biotechnol., 11 (3-5), pp. 140-151
Lutkenhaus, J.F., Wolf-Watz, H., Donachie, W.D., Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ) (1980) J. Bacteriol., 142 (2), pp. 615-620
Loose, M., Mitchison, T.J., The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns (2014) Nat. Cell Biol., 16 (1), pp. 38-46
Margolin, W., FtsZ and the division of prokaryotic cells and organelles (2005) Nat Rev Mol Cell Biol, 6 (11), pp. 862-871
Koppelman, C.M., Aarsman, M.E., Postmus, J., Pas, E., Muijsers, A.O., Scheffers, D.J., Nanninga, N., Den Blaauwen, T., R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division (2004) Mol. Microbiol., 51 (3), pp. 645-657
Hett, E.C., Rubin, E.J., Bacterial growth and cell division: A mycobacterial perspective (2008) MMBR, 72 (1), pp. 126-156
Dziadek, J., Rutherford, S.A., Madiraju, M.V., Atkinson, M.A., Rajagopalan, M., Conditional expression of Mycobacterium smegmatis ftsZ, an essential cell division gene (2003) Microbiology, 149, pp. 1593-1603
Mukamolova, G.V., Turapov, O.A., Kazarian, K., Telkov, M., Kaprelyants, A.S., Kell, D.B., Young, M., The rpf gene of Micrococcus luteus encodes an essential secreted growth factor (2002) Mol. Microbiol., 46 (3), pp. 611-621
Mukamolova, G.V., Kaprelyants, A.S., Young, D.I., Young, M., Kell, D.B., A bacterial cytokine (1998) Proc. Natl. Acad. Sci. U. S. A., 95 (15), pp. 8916-8921
Tufariello, J.M., Mi, K., Xu, J., Manabe, Y.C., Kesavan, A.K., Drumm, J., Tanaka, K., Chan, J., Deletion of the Mycobacterium tuberculosis resuscitation-promoting factor Rv1009 gene results in delayed reactivation from chronic tuberculosis (2006) Infect. Immun., 74 (5), pp. 2985-2995
Ruggiero, A., Tizzano, B., Pedone, E., Pedone, C., Wilmanns, M., Berisio, R., Crystal structure of the resuscitation-promoting factor (DeltaDUF)RpfB from M. Tuberculosis (2009) J. Mol. Biol., 385 (1), pp. 153-162
Chauviac, F.X., Robertson, G., Quay, D.H., Bagneris, C., Dumas, C., Henderson, B., Ward, J., Cohen-Gonsaud, M., The RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation-promoting factor catalytic domain Acta Crystallogr. F Struct. Biol. Commun., 70, pp. 1022-1026
Mavrici, D., Prigozhin, D.M., Alber, T., Mycobacterium tuberculosis RpfE crystal structure reveals a positively charged catalytic cleft (2014) Protein Sci., 23 (4), pp. 481-487
Phillips, D.C., The hen egg white lysozyme molecule (1967) Proc. Natl. Acad. Sci. U. S. A., 57, pp. 483-495
Koshland, D.E., Stereochemistry and mechanism of enzymatic reactions (1953) Biol Rev., 28 (4), pp. 416-436
Vocadlo, D.J., Davies, G.J., Laine, R., Withers, S.G., Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate (2001) Nature, 412 (6849), pp. 835-838
Inoue, M., Yamada, H., Yasukochi, T., Kuroki, R., Miki, T., Horiuchi, T., Imoto, T., Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: Structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35 (1992) Biochemistry, 31 (24), pp. 5545-5553
Maenaka, K., Matsushima, M., Song, H., Sunada, F., Watanabe, K., Kumagai, I., Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity (1995) J. Mol. Biol., 247, pp. 281-293
Squeglia, F., Romano, M., Ruggiero, A., Vitagliano, L., De Simone, A., Berisio, R., Carbohydrate recognition by RpfB from Mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses (2013) Biophys. J., 104 (11), pp. 2530-2539
Artola-Recolons, C., Lee, M., Bernardo-Garcia, N., Blazquez, B., Hesek, D., Bartual, S.G., Mahasenan, K.V., Hermoso, J.A., Structure and Cell Wall Cleavage by Modular Lytic Transglycosylase MltC of Escherichia coli (2014) ACS Chem. Biol., 9 (9), pp. 2058-2066
Hett, E.C., Chao, M.C., Deng, L.L., Rubin, E.J., A mycobacterial enzyme essential for cell division synergizes with resuscitationpromoting factor (2008) PLoS Pathog., 4 (2), p. e1000001
Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., Berisio, R., Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (2010) Structure, 18 (9), pp. 1184-1190
Kaprelyants, A.S., Mukamolova, G.V., Ruggiero, A., Makarov, V.A., Demina, G.R., Shleeva, M.O., Potapov, V.D., Shramko, P.A., Resuscitation-promoting Factors (Rpf): In Search of Inhibitors (2012) Protein Pep. Lett., 19 (10), pp. 1026-1034
Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F., Berisio, R., Bacterial cell division regulation by Ser/Thr kinases: A structural perspective (2012) Curr. Protein Pept. Sci., 13 (8), pp. 756-766
Fukushima, T., Kitajima, T., Yamaguchi, H., Ouyang, Q., Furuhata, K., Yamamoto, H., Shida, T., Sekiguchi, J., Identification and characterization of novel cell wall hydrolase CwlT: A two-domain autolysin exhibiting n-acetylmuramidase and DL-endopeptidase activities (2008) J. Biol. Chem., 283 (17), pp. 11117-11125
Aramini, J.M., Rossi, P., Huang, Y.J., Zhao, L., Jiang, M., Maglaqui, M., Xiao, R., Montelione, G.T., Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: Structural evidence for a novel cysteine peptidase catalytic triad (2008) Biochemistry, 47 (37), pp. 9715-9717
Eldholm, V., Johnsborg, O., Straume, D., Ohnstad, H.S., Berg, K.H., Hermoso, J.A., Havarstein, L.S., Pneumococcal CbpD is a murein hydrolase that requires a dual cell envelope binding specificity to kill target cells during fratricide (2010) Mol. Microbiol, 76 (4), pp. 905-917
Bartual, S.G., Straume, D., Stamsas, G.A., Munoz, I.G., Alfonso, C., Martinez-Ripoll, M., Havarstein, L.S., Hermoso, J.A., Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae (2014) Nat. Commun., 5, p. 3842
Squeglia, F., Ruggiero, A., Romano, M., Vitagliano, L., Berisio, R., Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: Evidence for the L-to-D inversion of configuration of the catalytic cysteine (2014) Acta Crystallogr. D Biol. Crystallogr., 70, pp. 2295-2300
Chao, M.C., Kieser, K.J., Minami, S., Mavrici, D., Aldridge, B.B., Fortune, S.M., Alber, T., Rubin, E.J., Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria (2013) PLoS Pathog., 9 (2), p. e1003197
Hussain, H., Branny, P., Allan, E., A eukaryotic-type serine/threonine protein kinase is required for biofilm formation, genetic competence, and acid resistance in Streptococcus mutans (2006) J. Bacteriol., 188 (4), pp. 1628-1632
Fiuza, M., Canova, M.J., Zanella-Cleon, I., Becchi, M., Cozzone, A.J., Mateos, L.M., Kremer, L., Molle, V., From the characterization of the four serine/threonine protein kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the role of PknA and PknB in cell division (2008) J. Biol. Chem., 283 (26), pp. 18099-18112
Madec, E., Laszkiewicz, A., Iwanicki, A., Obuchowski, M., Seror, S., Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes (2002) Mol. Microbiol., 46 (2), pp. 571-586
Madec, E., Stensballe, A., Kjellstrom, S., Cladiere, L., Obuchowski, M., Jensen, O.N., Seror, S.J., Mass spectrometry and sitedirected mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis (2003) J. Mol. Biol., 330 (3), pp. 459-472
Absalon, C., Obuchowski, M., Madec, E., Delattre, D., Holland, I.B., Seror, S.J., CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis (2009) Microbiology, 155, pp. 932-943
Jones, G., Dyson, P., Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: Inside versus outside (2006) J. Bacteriol., 188 (21), pp. 7470-7476
Ruggiero, A., Squeglia, F., Marasco, D., Marchetti, R., Molinaro, A., Berisio, R., X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus (2011) Biochem. J., 435 (1), pp. 33-41
Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Silipo, A., Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (2011) J. Am. Chem, Soc., 133 (51), pp. 20676-20679
Calvanese, L., Falcigno, L., Maglione, C., Marasco, D., Ruggiero, A., Squeglia, F., Berisio, R., D'Auria, G., Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis (2014) Biopolymers, 101 (7), pp. 712-719
Yeats, C., Finn, R.D., Bateman, A., The PASTA domain: A betalactam-binding domain (2002) Trends Biochem. Sci., 27 (9), p. 438
Patru, M.M., Pavelka, Jr.M.S., A role for the class A penicillinbinding protein PonA2 in the survival of Mycobacterium smegmatis under conditions of nonreplication (2010) J. Bacteriol., 192 (12), pp. 3043-3054
Mir, M., Asong, J., Li, X., Cardot, J., Boons, G., Husson, R.N., The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization PLOS Pathog., 7 (7), p. 1002182
Lim, J.H., Kim, M.S., Kim, H.E., Yano, T., Oshima, Y., Aggarwal, K., Goldman, W.E., Oh, B.H., Structural basis for preferential recognition of diaminopimelic acid-type peptidoglycan by a subset of peptidoglycan recognition proteins (2006) J. Biol. Chem., 281 (12), pp. 8286-8295
Hubbard, S.R., Till, J.H., Protein tyrosine kinase structure and function (2000) Annu. Rev. Biochem., 69, pp. 373-398
Heldin, C.H., Dimerization of cell-surface receptors in signal-transduction (1995) Cell, 80 (2), pp. 213-223
Botos, I., Segal, D.M., Davies, D.R., The structural biology of toll-like receptors (2011) Structure, 19 (4), pp. 447-459
Mieczkowski, C., Iavarone, A.T., Alber, T., Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase Embo J., 27 (23), pp. 3186-3197
Young, T.A., Delagoutte, B., Endrizzi, J.A., Falick, A.M., Alber, T., Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases (2003) Nat. Struc. Biol., 10 (3), pp. 168-174
Damle, N.P., Mohanty, D., Mechanism of autophosphorylation of mycobacterial PknB explored by molecular dynamics simulations (2014) Biochemistry, 53, pp. 4715-4726
Barthe, P., Mukamolova, G.V., Roumestand, C., Cohen-Gonsaud, M., The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation (2010) Structure, 18 (5), pp. 606-615
Telkov, M.V., Demina, G.R., Voloshin, S.A., Salina, E.G., Dudik, T.V., Stekhanova, T.N., Mukamolova, G.V., Kaprelyants, A.S., Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycan hydrolases (2006) Biochemistry (Mosc), 71 (4), pp. 414-422
Atrih, A., Foster, S.J., The role of peptidoglycan structure and structural dynamics during endospore dormancy and germination (1999) Antonie Van Leeuwenhoek, 75 (4), pp. 299-307
Demina, G.R., Makarov, V.A., Nikitushkin, V.D., Ryabova, O.B., Vostroknutova, G.N., Salina, E.G., Shleeva, M.O., Kaprelyants, A.S., Finding of the low molecular weight inhibitors of resuscitation promoting factor enzymatic and resuscitation activity (2009) PloS One, 4 (12), p. e817
Ruggiero, A., Marchant, J., Squeglia, F., Makarov, V., De Simone, A., Berisio, R., Molecular determinants of inactivation of the resuscitation promoting factor B from Mycobacterium tuberculosis (2013) J. Biomol. Struct. Dyn., 31 (2), pp. 195-205
Cohen-Gonsaud, M., Barthe, P., Bagneris, C., Henderson, B., Ward, J., Roumestand, C., Keep, N.H., The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes (2005) Nat. Struct. Mol. Biol., 12, pp. 270-273
Huynh, K.K., Joshi, S.A., Brown, E.J., A delicate dance: Host response to mycobacteria (2011) Curr. Opin. Immunol., 23 (4), pp. 464-472
Exit from mycobacterial dormancy: a structural perspective