Human lysosomal acid lipase inhibitor lalistat impairs: Mycobacterium tuberculosis growth by targeting bacterial hydrolases

J. Lehmann; J. Vomacka; K. Esser; M. Nodwell; K. Kolbe; P. Rämer; U. Protzer; N. Reiling; S. A. Sieber

doi:10.1039/c6md00231e

Human lysosomal acid lipase inhibitor lalistat impairs: Mycobacterium tuberculosis growth by targeting bacterial hydrolases

J. Lehmann, J. Vomacka, K. Esser, M. Nodwell, K. Kolbe, P. Rämer, U. Protzer, N. Reiling, S. A. Sieber

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15 Scopus citations

Abstract

Lalistat inhibits growth of Mycobacterium tuberculosis in bacterial culture as well as in infected macrophages. Target identification by quantitative proteomics revealed a cluster of 20 hydrolytic proteins including members of the lipase family. Lipases are essential for M. tuberculosis fatty acid production and energy storage thus representing promising antibiotic targets.

Original language	English
Pages (from-to)	1797-1801
Number of pages	5
Journal	MedChemComm
Volume	7
Issue number	9
DOIs	https://doi.org/10.1039/c6md00231e
State	Published - 2016

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title = "Human lysosomal acid lipase inhibitor lalistat impairs: Mycobacterium tuberculosis growth by targeting bacterial hydrolases",

abstract = "Lalistat inhibits growth of Mycobacterium tuberculosis in bacterial culture as well as in infected macrophages. Target identification by quantitative proteomics revealed a cluster of 20 hydrolytic proteins including members of the lipase family. Lipases are essential for M. tuberculosis fatty acid production and energy storage thus representing promising antibiotic targets.",

author = "J. Lehmann and J. Vomacka and K. Esser and M. Nodwell and K. Kolbe and P. R{\"a}mer and U. Protzer and N. Reiling and Sieber, {S. A.}",

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AU - Lehmann, J.

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AU - Esser, K.

AU - Nodwell, M.

AU - Kolbe, K.

AU - Rämer, P.

AU - Protzer, U.

AU - Reiling, N.

AU - Sieber, S. A.

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AB - Lalistat inhibits growth of Mycobacterium tuberculosis in bacterial culture as well as in infected macrophages. Target identification by quantitative proteomics revealed a cluster of 20 hydrolytic proteins including members of the lipase family. Lipases are essential for M. tuberculosis fatty acid production and energy storage thus representing promising antibiotic targets.

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Human lysosomal acid lipase inhibitor lalistat impairs: Mycobacterium tuberculosis growth by targeting bacterial hydrolases

Abstract

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