Eric Cundliffe

University of Leicester

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Neil Bate

University of Leicester

Andrew R. Butler

International Centre for Radio Astronomy Research

Jill Thompson

Brown University

George Stratigopoulos

Columbia University Irving Medical Center

Richard Skinner

George Washington University

Jessica Thompson

Center for Clinical Research (United States)

Michael J. R. Stark

University of Dundee

Atul R. Gandecha

University of Leicester

Magdalena Zalacaín

GlaxoSmithKline (United States)

Michael Cannon

Los Alamos National Laboratory

Cooperative Institutions

University of Leicester

Bristol-Myers Squibb (United States)

Max Planck Institute for Molecular Genetics

Cornell University

University of Cambridge

Tufts University

Massachusetts Institute of Technology

Brown University

University of Manchester

Centre National de la Recherche Scientifique

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The Antibiotic Micrococcin Is a Potent Inhibitor of Growth and Protein Synthesis in the Malaria Parasite

Antimicrobial Agents and Chemotherapy (1998)

Michael J. Rogers Eric Cundliffe Thomas F. McCutchan

ABSTRACT The antibiotic micrococcin is a potent growth inhibitor of the human malaria parasite Plasmodium falciparum , with a 50% inhibitory concentration of 35 nM. This is comparable to or less than the corresponding levels of commonly used antimalarial drugs. Micrococcin, like thiostrepton, putatively targets protein synthesis in the plastid-like organelle of the parasite.

Thiostrepton

Apicoplast

Plasmodium (life cycle)

10.1128/aac.42.3.715

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Citations (98)

On the biological role of ribosomal protein BM-L11 of Bacillus megaterium, homologous with Escherichia coli ribosomal protein L11

Journal of Molecular Biology (1979)

Michael J. R. Stark Eric Cundliffe

Ribosomal protein

Bacillus megaterium

Thiostrepton

Eukaryotic Ribosome

Elongation factor

50S

10.1016/0022-2836(79)90485-6

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Citations (49)

Antibiotics as probes of ribosomal structure and function

Palgrave Macmillan UK eBooks (1983)

Eric Cundliffe

Ribosomal protein

Eukaryotic Ribosome

10.1007/978-1-349-06540-0_5

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Citations (4)

Studies of the GTPase domain of archaebacterial ribosomes

European Journal of Biochemistry (1985)

Alan A. D. BEAUCLERK H. Hummel David Holmes August Böck Eric Cundliffe

Ribosomes from the methanogens Methanococcus vannielii and Methanobacterium formicicum catalyse uncoupled hydrolysis of GTP in the presence of factor EF-2 from rat liver (but not factor EF-G from Escherichia coli). In this assay, and in poly(U)-dependent protein synthesis, they were sensitive to thiostrepton. In contrast, ribosomes from Sulfolobus solfataricus did not respond to factor EF-2 (or factor EF-G) but possessed endogenous GTPase activity, which was also sensitive to thiostrepton. Ribosomes from the methanogens did not support (p)ppGpp production, but did appear to possess the equivalent of protein L11, which in E. coli is normally required for guanosine polyphosphate synthesis. Protein L11 from E. coli bound well to 23S rRNA from all three archaebacteria (as did thiostrepton) and oligonucleotides protected by the protein were sequenced and compared with rRNA sequences from other sources.

Thiostrepton

Sulfolobus solfataricus

Methanococcus

Ribosomal protein

Eukaryotic Ribosome

10.1111/j.1432-1033.1985.tb09095.x

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Citations (62)

Influence of dimethylsulfoxide on tylosin production in Streptomyces fradiae

Journal of Industrial Microbiology & Biotechnology (2001)

A. Butler Eric Cundliffe

Streptomyces fradiae

Tylosin

Streptomycetaceae

10.1038/sj.jim.7000160

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Citations (12)

Resistance to macrolides and lincosamides in Streptomyces lividans and to aminoglycosides in Micromonospora purpurea

Gene (1992)

Eric Cundliffe

Tylosin

Lincomycin

23S ribosomal RNA

Oleandomycin

Peptidyl transferase

Lincosamides

Spiramycin

Streptomycetaceae

10.1016/0378-1119(92)90543-x

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Citations (19)

Inhibition of Initiation, Elongation, and Termination of Eukaryotic Protein Synthesis by Trichothecene Fungal Toxins

Antimicrobial Agents and Chemotherapy (1977)

Eric Cundliffe Julian Davies

The 12,13-epoxytrichothecenes, specific inhibitors of protein synthesis in eukaryotes, can be subdivided further in terms of their mode of action. In addition to the I-type (initiation inhibitors) and E-types (elongation inhibitors), we found that some E-types apparently exhibit inhibition of chain termination at low concentrations. The nature of substituents on C4 may determine the type of inhibitory activity observed.

Elongation

Elongation factor

Mode of Action

Mechanism of Action

10.1128/aac.11.3.491

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Citations (110)

Site-specific methylation of 16S rRNA caused by pct, a pactamycin resistance determinant from the producing organism, Streptomyces pactum

Journal of Bacteriology (1991)

Juan P. G. Ballesta Eric Cundliffe

Ribosomal resistance to pactamycin in clones of Streptomyces lividans containing DNA (pct) from Streptomyces pactum, the pactamycin producer, involves methylation of 16S RNA. The modified residue A-941 in S. lividans 16S rRNA (A-964 in the homologous Escherichia coli sequence) is converted to 1-methyladenosine, and the ribosomal ability to bind pactamycin is reduced or abolished.

10.1128/jb.173.22.7213-7218.1991

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Citations (35)

Inactivation of a transcriptional repressor during empirical improvement of the tylosin producer, Streptomyces fradiae

Journal of Industrial Microbiology & Biotechnology (2002)

George Stratigopoulos Eric Cundliffe

Streptomyces fradiae

Tylosin

10.1038/sj.jim.7000234

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Citations (13)

Self‐Protection Mechanisms in Antibiotic Producers

Novartis Foundation symposium (2007)

Eric Cundliffe

Various ways in which antibiotic-producing organisms are able to resist the actions of their products are discussed. Examples are given of antibiotic inactivation and also the modification of antibiotic target sites (most notably, ribosomes) to which drugs would otherwise bind and thereby exert their usual inhibitory effects. An interesting variation on the latter theme involves the duplication of target enzymes so that both sensitive and resistant versions are produced, the latter inducibly. Speculative discussion of antibiotic efflux leads to examples of cloned resistance determinants that probably encode components of efflux systems. Although of interest in their own right, resistance mechanisms should not be viewed narrowly when the physiology of antibiotic producers is considered. Thus, chemical modification of drug molecules may not only fulfil a protective role within the cell but may also provide substrates for efflux. Recent evidence that such considerations apply to macrolide antibiotics is presented. The control of resistance in producing organisms is also discussed with particular reference to the induction of novobiocin resistance in Streptomyces sphaeroides. This involves the interplay of novobiocin-sensitive and -resistant forms of DNA gyrase and features a promoter that displays a dramatic response to changes in DNA topology.

Novobiocin

Efflux

Viomycin

10.1002/9780470514344.ch12

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Citations (41)