CJ-21,058, a New SecA Inhibitor Isolated from a Fungus.

Sugie, Yutaka; Inagaki, Sae; Kato, Yoshinao; Nishida, Hiroyuki; Pang, Chang‐Hong; Saito, Toshiyuki; Sakemi, Shinichi; Dib-Hajj, Fadia; Mueller, John P.; Sutcliffe, Joyce A.; Kojima, Yasuhiro

doi:10.7164/antibiotics.55.25

Cited by 61 publications

(62 citation statements)

References 13 publications

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“…This antisense strain has increased sensitivity to inhibitors of SecA, which makes them easier to identify [100]. One of these compounds identified is pannomycin, which is structurally similar to a demonstrated SecA inhibitor identified independently in another study [100,101]. While pannomycin has low antibacterial activity against a panel of bacteria tested, there is potential in optimizing its activity [99,100].…”

Section: Protein Export Systems As Targets For New Drug Developmentmentioning

confidence: 99%

Protein Export Systems of Mycobacterium Tuberculosis : Novel Targets for Drug Development?

Feltcher

Sullivan

Braunstein³

2010

Future Microbiol.

105

104

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Protein export is essential in all bacteria and many bacterial pathogens depend on specialized protein export systems for virulence. In Mycobacterium tuberculosis, the etiological agent of the disease tuberculosis, the conserved general secretion (Sec) and twin-arginine translocation (Tat) pathways perform the bulk of protein export and are both essential. M. tuberculosis also has specialized export pathways that transport specific subsets of proteins. One such pathway is the accessory SecA2 system, which is important for M. tuberculosis virulence. There are also specialized ESX export systems that function in virulence (ESX-1) or essential physiologic processes (ESX-3). The increasing prevalence of drug-resistant M. tuberculosis strains makes the development of novel drugs for tuberculosis an urgent priority. In this article, we discuss our current understanding of the protein export systems of M. tuberculosis and consider the potential of these pathways to be novel targets for tuberculosis drugs.

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Section: Protein Export Systems As Targets For New Drug Developmentmentioning

confidence: 99%

Protein Export Systems of Mycobacterium Tuberculosis : Novel Targets for Drug Development?

Feltcher

Sullivan

Braunstein³

2010

Future Microbiol.

105

104

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“…This cis-decalin natural product is structurally similar to known inhibitors of SecA cissetin and CJ-21,058. 58,59 When the compound was tested on a panel of microorganisms, only weak antimicrobial activity was observed with MICs of 1.4 mM against S. aureus Smith and Enterococcus faecalis, and activity was observed at this concentration against Streptococcus pneumoniae, H. influenzae and Escherichia coli. 58 …”

Section: Novel Approaches To Exploit Natural Products From Microbial mentioning

confidence: 94%

Chapter 11. Novel Approaches to Exploit Natural Products from Microbial Resources

Genilloud¹,

Vicente²

2012

Drug Discovery

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“…A particularly attractive feature of this activity is that it appears to be controlled by several regions of the molecule (Karamanou et al 1999. High throughput screening efforts by a number of companies employing mainly the in vivo assays have identified inhibitors of the SecA ATPase activity (Alksne et al 2000, Sugie et al 2002. However, these small-size inhibitors were of limited value in the former case since they were shown to be general inhibitors of many other ATPases.…”

Section: Exploiting the Secretome: Novel Antibioticsmentioning

confidence: 97%

Bacterial secretome: the assembly manual and operating instructions (Review)

Economou

2002

Molecular Membrane Biology

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Bacterial protein secretion is a complex multi-stage reaction that is central to membrane and cell wall biosynthesis and essential for cell viability. An impressive array of experimental tools have been used to dissect this reaction into discreet sub-reactions. Synthesis of these data reveals a fascinating cascade of inter- and intra-molecular interactions that select, sort and target secretory polypeptides to the membrane and then spend metabolic energy to bias their vectorial movement across the membrane plane through a lipid-inaccessible proteinaceous environment. Transmembrane crossing is catalyzed by protein translocase, an astonishingly dynamic molecular machine. The unusual molecular features of the Sec pathway components allows a handful of proteins to catalyze the export of hundreds of secretory polypeptide substrates with astonishing fidelity. Knowledge of the molecular details of the secretion pathway allows us to rationally exploit these features in heterologous protein production biotechnologies and in the development of novel antibiotics.

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CJ-21,058, a New SecA Inhibitor Isolated from a Fungus.

Cited by 61 publications

References 13 publications

Protein Export Systems of Mycobacterium Tuberculosis : Novel Targets for Drug Development?

Protein Export Systems of Mycobacterium Tuberculosis : Novel Targets for Drug Development?

Chapter 11. Novel Approaches to Exploit Natural Products from Microbial Resources

Bacterial secretome: the assembly manual and operating instructions (Review)

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