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Your search keyword '"Palčeková, Zuzana"' showing total 17 results
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17 results on '"Palčeková, Zuzana"'

1. Acylation of glycerolipids in mycobacteria

Author

Angala, Shiva Kumar, Carreras-Gonzalez, Ana, Huc-Claustre, Emilie, Anso, Itxaso, Kaur, Devinder, Jones, Victoria, Palčeková, Zuzana, Belardinelli, Juan M., de Sousa-d’Auria, Célia, Shi, Libin, Slama, Nawel, Houssin, Christine, Quémard, Annaïk, McNeil, Michael, Guerin, Marcelo E., and Jackson, Mary

Published
2023
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2. Lipoarabinomannan modification as a source of phenotypic heterogeneity in host-adapted Mycobacterium abscessus isolates

Author

De, Kavita, primary, Belardinelli, Juan M., additional, Pandurangan, Arun Prasad, additional, Ehianeta, Teddy, additional, Lian, Elena, additional, Palčeková, Zuzana, additional, Lam, Ha, additional, Gonzalez-Juarrero, Mercedes, additional, Bryant, Josephine M., additional, Blundell, Tom L., additional, Parkhill, Julian, additional, Floto, R. Andres, additional, Lowary, Todd L., additional, Wheat, William H., additional, and Jackson, Mary, additional

Published
2024
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4. Role of succinyl substituents in the mannose-capping of lipoarabinomannan and control of inflammation in Mycobacterium tuberculosis infection

Author

Palčeková, Zuzana, primary, Obregón-Henao, Andrés, additional, De, Kavita, additional, Walz, Amanda, additional, Lam, Ha, additional, Philp, Jamie, additional, Angala, Shiva Kumar, additional, Patterson, Johnathan, additional, Pearce, Camron, additional, Zuberogoitia, Sophie, additional, Avanzi, Charlotte, additional, Nigou, Jérôme, additional, McNeil, Michael, additional, Muñoz Gutiérrez, Juan F., additional, Gilleron, Martine, additional, Wheat, William H., additional, Gonzalez-Juarrero, Mercedes, additional, and Jackson, Mary, additional

Published
2023
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5. Acylation of glycerolipids in mycobacteria

Author

National Institute of Allergy and Infectious Diseases (US), National Institutes of Health (US), Ministerio de Economía y Competitividad (España), Ministerio de Ciencia, Innovación y Universidades (España), Ministerio de Ciencia e Innovación (España), Agencia Estatal de Investigación (España), Kumar Angala, Shiva, Carreras-Gonzalez, Ana, Huc-Claustre, Emilie, Anso, Itxaso, Kaur, Devinder, Jones, Victoria, Palčeková, Zuzana, Belardinelli, Juan M., Sousa-d’Auria, Célia de, Shi, Libin, Slama, Nawel, Houssin, Christine, Quémard, Annaïk, McNeil, Michael, Guerin, Marcelo E., Jackson, Mary, National Institute of Allergy and Infectious Diseases (US), National Institutes of Health (US), Ministerio de Economía y Competitividad (España), Ministerio de Ciencia, Innovación y Universidades (España), Ministerio de Ciencia e Innovación (España), Agencia Estatal de Investigación (España), Kumar Angala, Shiva, Carreras-Gonzalez, Ana, Huc-Claustre, Emilie, Anso, Itxaso, Kaur, Devinder, Jones, Victoria, Palčeková, Zuzana, Belardinelli, Juan M., Sousa-d’Auria, Célia de, Shi, Libin, Slama, Nawel, Houssin, Christine, Quémard, Annaïk, McNeil, Michael, Guerin, Marcelo E., and Jackson, Mary

Abstract

We report on the existence of two phosphatidic acid biosynthetic pathways in mycobacteria, a classical one wherein the acylation of the sn-1 position of glycerol-3-phosphate (G3P) precedes that of sn-2 and another wherein acylations proceed in the reverse order. Two unique acyltransferases, PlsM and PlsB2, participate in both pathways and hold the key to the unusual positional distribution of acyl chains typifying mycobacterial glycerolipids wherein unsaturated substituents principally esterify position sn-1 and palmitoyl principally occupies position sn-2. While PlsM selectively transfers a palmitoyl chain to the sn-2 position of G3P and sn-1-lysophosphatidic acid (LPA), PlsB2 preferentially transfers a stearoyl or oleoyl chain to the sn-1 position of G3P and an oleyl chain to sn-2-LPA. PlsM is the first example of an sn-2 G3P acyltransferase outside the plant kingdom and PlsB2 the first example of a 2-acyl-G3P acyltransferase. Both enzymes are unique in their ability to catalyze acyl transfer to both G3P and LPA.

Published
2023

7. Unique Features of Mycobacterium abscessus Biofilms Formed in Synthetic Cystic Fibrosis Medium

Author

Belardinelli, Juan M., primary, Li, Wei, additional, Avanzi, Charlotte, additional, Angala, Shiva K., additional, Lian, Elena, additional, Wiersma, Crystal J., additional, Palčeková, Zuzana, additional, Martin, Kevin H., additional, Angala, Bhanupriya, additional, de Moura, Vinicius C. N., additional, Kerns, Callan, additional, Jones, Victoria, additional, Gonzalez-Juarrero, Mercedes, additional, Davidson, Rebecca M., additional, Nick, Jerry A., additional, Borlee, Bradley R., additional, and Jackson, Mary, additional

Published
2021
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8. Polysaccharide Succinylation Enhances the Intracellular Survival of Mycobacterium abscessus

Author

Palčeková, Zuzana, Gilleron, Martine, Angala, Shiva Kumar, Belardinelli, Juan Manuel, McNeil, Michael, Bermudez, Luiz, Jackson, Mary, Mycobacteria Research Laboratories, Colorado State University [Fort Collins] (CSU), Institut de pharmacologie et de biologie structurale (IPBS), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Carlson College of Veterinary Medicine [Oregon State University], and Oregon State University (OSU)

Subjects
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2020

10. Disruption of the SucT acyltransferase in Mycobacterium smegmatis abrogates succinylation of cell envelope polysaccharides

Author

Palčeková, Zuzana, primary, Angala, Shiva K., additional, Belardinelli, Juan Manuel, additional, Eskandarian, Haig A., additional, Joe, Maju, additional, Brunton, Richard, additional, Rithner, Christopher, additional, Jones, Victoria, additional, Nigou, Jérôme, additional, Lowary, Todd L., additional, Gilleron, Martine, additional, McNeil, Michael, additional, and Jackson, Mary, additional

Published
2019
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11. A multitarget approach to drug discovery inhibiting Mycobacterium tuberculosis PyrG and PanK

Author

Chiarelli, L, Mori, G, Orena, B, Esposito, M, Lane, T, De Jesus Lopes Ribeiro, A, Degiacomi, G, Zemanová, J, Szádocka, S, Huszár, S, Palčeková, Z, Manfredi, M, Gosetti, F, Lelièvre, J, Ballell, L, Kazakova, E, Makarov, V, Marengo, E, Mikusova, K, Cole, S, Riccardi, G, Ekins, S, Pasca, M, Chiarelli, Laurent R., Mori, Giorgia, Orena, Beatrice Silvia, Esposito, Marta, Lane, Thomas, De Jesus Lopes Ribeiro, Ana Luisa, Degiacomi, Giulia, Zemanová, Júlia, Szádocka, Sára, Huszár, Stanislav, Palčeková, Zuzana, Manfredi, Marcello, Gosetti, Fabio, Lelièvre, Joël, Ballell, Lluis, Kazakova, Elena, Makarov, Vadim, Marengo, Emilio, Mikusova, Katarina, Cole, Stewart T., Riccardi, Giovanna, Ekins, Sean, Pasca, Maria Rosalia, Chiarelli, L, Mori, G, Orena, B, Esposito, M, Lane, T, De Jesus Lopes Ribeiro, A, Degiacomi, G, Zemanová, J, Szádocka, S, Huszár, S, Palčeková, Z, Manfredi, M, Gosetti, F, Lelièvre, J, Ballell, L, Kazakova, E, Makarov, V, Marengo, E, Mikusova, K, Cole, S, Riccardi, G, Ekins, S, Pasca, M, Chiarelli, Laurent R., Mori, Giorgia, Orena, Beatrice Silvia, Esposito, Marta, Lane, Thomas, De Jesus Lopes Ribeiro, Ana Luisa, Degiacomi, Giulia, Zemanová, Júlia, Szádocka, Sára, Huszár, Stanislav, Palčeková, Zuzana, Manfredi, Marcello, Gosetti, Fabio, Lelièvre, Joël, Ballell, Lluis, Kazakova, Elena, Makarov, Vadim, Marengo, Emilio, Mikusova, Katarina, Cole, Stewart T., Riccardi, Giovanna, Ekins, Sean, and Pasca, Maria Rosalia

Abstract

Mycobacterium tuberculosis, the etiological agent of the infectious disease tuberculosis, kills approximately 1.5 million people annually, while the spread of multidrug-resistant strains is of great global concern. Thus, continuous efforts to identify new antitubercular drugs as well as novel targets are crucial. Recently, two prodrugs activated by the monooxygenase EthA, 7947882 and 7904688, which target the CTP synthetase PyrG, were identified and characterized. In this work, microbiological, biochemical, and in silico methodologies were used to demonstrate that both prodrugs possess a second target, the pantothenate kinase PanK. This enzyme is involved in coenzyme A biosynthesis, an essential pathway for M. tuberculosis growth. Moreover, compound 11426026, the active metabolite of 7947882, was demonstrated to directly inhibit PanK, as well. In an independent screen of a compound library against PyrG, two additional inhibitors were also found to be active against PanK. In conclusion, these direct PyrG and PanK inhibitors can be considered as leads for multitarget antitubercular drugs and these two enzymes could be employed as a "double-tool" in order to find additional hit compounds.

Published
2018

12. A multitarget approach to drug discovery inhibiting Mycobacterium tuberculosis PyrG and PanK

Author

Chiarelli, Laurent R., primary, Mori, Giorgia, additional, Orena, Beatrice Silvia, additional, Esposito, Marta, additional, Lane, Thomas, additional, de Jesus Lopes Ribeiro, Ana Luisa, additional, Degiacomi, Giulia, additional, Zemanová, Júlia, additional, Szádocka, Sára, additional, Huszár, Stanislav, additional, Palčeková, Zuzana, additional, Manfredi, Marcello, additional, Gosetti, Fabio, additional, Lelièvre, Joël, additional, Ballell, Lluis, additional, Kazakova, Elena, additional, Makarov, Vadim, additional, Marengo, Emilio, additional, Mikusova, Katarina, additional, Cole, Stewart T., additional, Riccardi, Giovanna, additional, Ekins, Sean, additional, and Pasca, Maria Rosalia, additional

Published
2018
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14. Identification of aminopyrimidine-sulfonamides as potent modulators of Wag31-mediated cell elongation in mycobacteria.

Author

Singh, Vinayak, Dhar, Neeraj, Pató, János, Kolly, Gaëlle S, Korduláková, Jana, Forbak, Martin, Evans, Joanna C, Székely, Rita, Rybniker, Jan, Palčeková, Zuzana, Zemanová, Júlia, Santi, Isabella, Signorino-Gelo, François, Rodrigues, Liliana, Vocat, Anthony, Covarrubias, Adrian Suarez, Rengifo, Monica G, Johnsson, Kai, Mowbray, Sherry, Buechler, Joseph, Delorme, Vincent, Brodin, Priscille, Knott, Graham W, Aínsa, José A, Warner, Digby F, Kéri, György, Mikušová, Katarína, McKinney, John D, Cole, Stewart T, Mizrahi, Valerie, Hartkoorn, Ruben C, Singh, Vinayak, Dhar, Neeraj, Pató, János, Kolly, Gaëlle S, Korduláková, Jana, Forbak, Martin, Evans, Joanna C, Székely, Rita, Rybniker, Jan, Palčeková, Zuzana, Zemanová, Júlia, Santi, Isabella, Signorino-Gelo, François, Rodrigues, Liliana, Vocat, Anthony, Covarrubias, Adrian Suarez, Rengifo, Monica G, Johnsson, Kai, Mowbray, Sherry, Buechler, Joseph, Delorme, Vincent, Brodin, Priscille, Knott, Graham W, Aínsa, José A, Warner, Digby F, Kéri, György, Mikušová, Katarína, McKinney, John D, Cole, Stewart T, Mizrahi, Valerie, and Hartkoorn, Ruben C

Abstract

There is an urgent need to discover new anti-tubercular agents with novel mechanisms of action in order to tackle the scourge of drug-resistant tuberculosis. Here, we report the identification of such a molecule - an AminoPYrimidine-Sulfonamide (APYS1) that has potent, bactericidal activity against M. tuberculosis. Mutations in APYS1-resistant M. tuberculosis mapped exclusively to wag31, a gene that encodes a scaffolding protein thought to orchestrate cell elongation. Recombineering confirmed that a Gln201Arg mutation in Wag31 was sufficient to cause resistance to APYS1, however, neither overexpression nor conditional depletion of wag31 impacted M. tuberculosis susceptibility to this compound. In contrast, expression of the wildtype allele of wag31 in APYS1-resistant M. tuberculosis was dominant and restored susceptibility to APYS1 to wildtype levels. Time-lapse imaging and scanning electron microscopy revealed that APYS1 caused gross malformation of the old pole of M. tuberculosis, with eventual lysis. These effects resembled the morphological changes observed following transcriptional silencing of wag31 in M. tuberculosis. These data show that Wag31 is likely not the direct target of APYS1, but the striking phenotypic similarity between APYS1 exposure and genetic depletion of Wag31 in M. tuberculosis suggests that APYS1 might indirectly affect Wag31 through an as yet unknown mechanism.

Published
2017
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15. Identification of aminopyrimidine-sulfonamides as potent modulators of Wag31-mediated cell elongation in mycobacteria

Author

Singh, Vinayak, primary, Dhar, Neeraj, additional, Pató, János, additional, Kolly, Gaëlle S., additional, Korduláková, Jana, additional, Forbak, Martin, additional, Evans, Joanna C., additional, Székely, Rita, additional, Rybniker, Jan, additional, Palčeková, Zuzana, additional, Zemanová, Júlia, additional, Santi, Isabella, additional, Signorino-Gelo, François, additional, Rodrigues, Liliana, additional, Vocat, Anthony, additional, Covarrubias, Adrian S., additional, Rengifo, Monica G., additional, Johnsson, Kai, additional, Mowbray, Sherry, additional, Buechler, Joseph, additional, Delorme, Vincent, additional, Brodin, Priscille, additional, Knott, Graham W., additional, Aínsa, José A., additional, Warner, Digby F., additional, Kéri, György, additional, Mikušová, Katarína, additional, McKinney, John D., additional, Cole, Stewart T., additional, Mizrahi, Valerie, additional, and Hartkoorn, Ruben C., additional

Published
2016
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16. Polysaccharide Succinylation Enhances the Intracellular Survival of Mycobacterium abscessus .

Author

Palčeková Z, Gilleron M, Angala SK, Belardinelli JM, McNeil M, Bermudez LE, and Jackson M

Subjects
Cell Wall, Humans, Macrophages, Polysaccharides, Mycobacterium abscessus, Mycobacterium tuberculosis
Abstract

Lipoarabinomannan (LAM) and its biosynthetic precursors, phosphatidylinositol mannosides (PIMs) and lipomannan (LM) play important roles in the interactions of Mycobacterium tuberculosis with phagocytic cells and the modulation of the host immune response, but nothing is currently known of the impact of these cell envelope glycoconjugates on the physiology and pathogenicity of nontuberculous mycobacteria. We here report on the structures of Mycobacterium abscessus PIM, LM, and LAM. Intriguingly, these structures differ from those reported previously in other mycobacterial species in several respects, including the presence of a methyl substituent on one of the mannosyl residues of PIMs as well as the PIM anchor of LM and LAM, the size and branching pattern of the mannan backbone of LM and LAM, and the modification of the arabinan domain of LAM with both succinyl and acetyl substituents. Investigations into the biological significance of some of these structural oddities point to the important role of polysaccharide succinylation on the ability of M. abscessus to enter and survive inside human macrophages and epithelial cells and validate for the first time cell envelope polysaccharides as important modulators of the virulence of this emerging pathogen.

Published
2020
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17. Identification of aminopyrimidine-sulfonamides as potent modulators of Wag31-mediated cell elongation in mycobacteria.

Author

Singh V, Dhar N, Pató J, Kolly GS, Korduláková J, Forbak M, Evans JC, Székely R, Rybniker J, Palčeková Z, Zemanová J, Santi I, Signorino-Gelo F, Rodrigues L, Vocat A, Covarrubias AS, Rengifo MG, Johnsson K, Mowbray S, Buechler J, Delorme V, Brodin P, Knott GW, Aínsa JA, Warner DF, Kéri G, Mikušová K, McKinney JD, Cole ST, Mizrahi V, and Hartkoorn RC

Subjects
Anti-Bacterial Agents pharmacokinetics, Cell Enlargement, Drug Discovery methods, Gene Expression Regulation, Bacterial genetics, Mycobacterium smegmatis genetics, Mycobacterium smegmatis metabolism, Mycobacterium tuberculosis genetics, Mycobacterium tuberculosis metabolism, Pyrimidines chemistry, Pyrimidines metabolism, Sequence Homology, Amino Acid, Sulfonamides metabolism, Sulfonamides pharmacokinetics, Time-Lapse Imaging, Antitubercular Agents metabolism, Bacterial Proteins genetics, Bacterial Proteins metabolism, Pyrimidines pharmacokinetics
Abstract

There is an urgent need to discover new anti-tubercular agents with novel mechanisms of action in order to tackle the scourge of drug-resistant tuberculosis. Here, we report the identification of such a molecule - an AminoPYrimidine-Sulfonamide (APYS1) that has potent, bactericidal activity against M. tuberculosis. Mutations in APYS1-resistant M. tuberculosis mapped exclusively to wag31, a gene that encodes a scaffolding protein thought to orchestrate cell elongation. Recombineering confirmed that a Gln201Arg mutation in Wag31 was sufficient to cause resistance to APYS1, however, neither overexpression nor conditional depletion of wag31 impacted M. tuberculosis susceptibility to this compound. In contrast, expression of the wildtype allele of wag31 in APYS1-resistant M. tuberculosis was dominant and restored susceptibility to APYS1 to wildtype levels. Time-lapse imaging and scanning electron microscopy revealed that APYS1 caused gross malformation of the old pole of M. tuberculosis, with eventual lysis. These effects resembled the morphological changes observed following transcriptional silencing of wag31 in M. tuberculosis. These data show that Wag31 is likely not the direct target of APYS1, but the striking phenotypic similarity between APYS1 exposure and genetic depletion of Wag31 in M. tuberculosis suggests that APYS1 might indirectly affect Wag31 through an as yet unknown mechanism., (© 2016 John Wiley & Sons Ltd.)

Published
2017
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