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Last update 08 May 2025

EF-Tu

Last update 08 May 2025

Basic Info

Synonyms-

Introduction-

Drugs associated with EF-Tu

GE-2270 factor A

Target

23S rRNA x 50S subunit x EF-Tu

Mechanism

23S rRNA modulators [+2]

Active Org.-

Originator Org.

Sanofi

Active Indication-

Inactive Indication

Bacterial Infections [+1]

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

GE-37468A

Target

23S rRNA x 50S subunit x EF-Tu

Mechanism

23S rRNA modulators [+2]

Active Org.-

Originator Org.

Hoechst Marion Roussel SA

Active Indication-

Inactive Indication

Bacterial Infections [+2]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

X-5108

Target

EF-Tu

Mechanism

EF-Tu inhibitors

Active Org.-

Originator Org.

Hoffmann-La Roche, Inc.

Active Indication-

Inactive Indication

Gram-Positive Bacterial Infections

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with EF-Tu

NCT01232595

/ CompletedPhase 2

Multi-center, Randomized, Evaluator-blind, Active-controlled,Parallel-group Design to Determine Safety, Tolerability, and Efficacy of Multiple Daily Administration of LFF571 for 10 Days in Patients With Moderate Clostridium Difficile Infections

This study will assess the safety and efficacy of multiple daily dosing of oral LFF571 in patients who have moderate Clostridium difficile infections.

Start Date01 Oct 2010

Sponsor / Collaborator

Novartis Pharmaceuticals Corp.

100 Clinical Results associated with EF-Tu

100 Translational Medicine associated with EF-Tu

0 Patents (Medical) associated with EF-Tu

1,648

Literatures (Medical) associated with EF-Tu

01 Jul 2025·Microbial Pathogenesis

Evaluation of immune effect to recombinant potential protective antigens of Mycoplasma ovipneumoniae in mice

Article

Author: Chen, Yi ; Liu, Diyue ; Liu, Maojun ; Chen, Siyu ; Wang, Jinquan ; Shan, Yiyi ; Wang, Xiaonan ; Du, Gaimei ; Cheng, Zilong ; Zhang, Wenwen ; Zhang, Mengjie ; Yang, Leilei ; Li, Wenliang ; Chu, Yuefeng

Mycoplasma ovipneumoniae is a primary causative agent of pneumonia in ruminants, causing chronic non-progressive pneumonia in domestic sheep and goats, but leading to higher morbidity and mortality in bighorn sheep and wild small ruminants. This disease has become a widespread epidemic, resulting in significant losses to the sheep industry. In this study, we evaluated the immunogenicity and initial protective effects of four antigenic proteins of M. ovipneumoniae, namely Eno, EF-Tu, Ulad, and T4SS. These proteins were used to immunize BALB/c mice either individually or in a combination (rProteins group). The mice were intranasally infected with 10⁹ CCU₅₀/mL M. ovipneumoniae strain NJ01 twice, on days 28 and 30 after immunization. Among the four recombinant proteins, rEno demonstrated the most promising results in terms of inducing specific humoral and cellular immune responses. It also resulted in the lowest lung lesion scores and the lowest M. ovipneumoniae loads in the lungs and bronchoalveolar lavage fluid (BALF). Compared to the other three proteins, rEno provided superior protection. Furthermore, the rEno vaccine significantly reduced the inflammatory response in the lungs of mice, as evidenced by the evaluation of pro-inflammatory cytokines. The expression of IL-1β and NF-κB was significantly reduced, while the expression of IL-4 was significantly increased. In conclusion, the rEno vaccine elicited a favorable immunological response and conferred protection against M. ovipneumoniae. This finding presents a novel approach to controlling the global spread of this pathogen.

01 May 2025·Biochimie

Macrolactin a is an inhibitor of protein biosynthesis in bacteria

Article

Author: Dilbaryan, Diana S ; Teslya, Anastasia V ; Luzgina, Natalia G ; Imamutdinova, Arina N ; Klochkova, Evelina A ; Poshvina, Darya V ; Rusanov, Alexander L ; Bikmullin, Aydar G ; Usachev, Konstantin S ; Vasilchenko, Alexey S ; Taldaev, Amir Kh ; Lukyanov, Dmitry A ; Nikandrova, Arina A ; Sergiev, Petr V ; Romashin, Daniil D ; Garaeva, Natalia S ; Osterman, Ilya A

Macrolactin A (McA) is a secondary metabolite produced by Bacillus species. It has been known for its antimicrobial properties since the late 1980s, although the exact mechanism of its antibacterial activity remains unknown. In this study, we have found that McA is an inhibitor of protein synthesis in bacteria. Our conclusion is based on the results obtained by in vivo and in vitro bioreporter systems. We demonstrated that the inhibitory activity of McA is independent of bacterial species. However, the concentration of McA required to inhibit protein synthesis in the E. coli cell-free translational model was found to be 50 times lower than the concentration required in the S. aureus cell-free translational model. To investigate the mechanism of McA's inhibitory activity, we conducted a toe-printing assay, sequenced and annotated the genomes of McA-resistant Bacillus pumilus McA^R and its parental strain. The results showed that McA inhibits the initial step of the elongation phase of protein synthesis. We identified single and multiple nucleotide polymorphisms in the gene encoding the translation elongation factor Tu (EF-Tu). Molecular modeling showed that the McA molecule can form non-covalent bonds with amino acids at the interface of domains 1 and 2 of EF-Tu. A cross-resistance assay was conducted using kirromycin on B. pumilus McA^R. The results confirmed the assumption that McA has a mode of action similar to that of other elfamycin-like antibiotics (targeting EF-Tu). Overall, our study addresses a significant gap in our understanding of the mechanism of action of McA, a representative member of the macrolide antibiotics.

01 Apr 2025·RNA

Role of the sarcin-ricin loop of 23S rRNA in biogenesis of the 50S ribosomal subunit

Article

Author: Moon, Kyung-Mee ; Aval, Sepideh Fakhretaha ; Ortega, Joaquin ; Seffouh, Amal ; Fredrick, Kurt ; Foster, Leonard J

The sarcin-ricin loop (SRL) is one of the most conserved segments of ribosomal RNA (rRNA). Translational GTPases (trGTPases), such as EF-G, EF-Tu, and IF2, form contacts with the SRL that are critical for GTP hydrolysis and factor function. Previous studies showed that expression of 23S rRNA lacking the SRL confers a dominant lethal phenotype inEscherichia coli. Isolated ΔSRL particles were found to be not only inactive in protein synthesis but also incompletely assembled. In particular, block 4 of the subunit, which includes the peptidyl transferase center, remained unfolded. Here, we explore the basis of this assembly defect. We find that 23S rRNA extracted from ΔSRL subunits can be efficiently reconstituted into 50S subunits, and these reconstituted ΔSRL particles exhibit full peptidyl transferase activity. We also further characterize ΔSRL particles purified from cells, using cryo-EM and proteomic methods. These particles lack density for rRNA and r-proteins of block 4, consistent with earlier chemical probing data. Incubation of these particles with excess total r-protein of the large subunit (TP50) fails to restore substantial peptidyl transferase activity. Interestingly, proteomic analysis of control and mutant particles shows an overrepresentation of multiple assembly factors in the ΔSRL case. We propose that one or more GTPases normally act to release assembly factors, and this activity is blocked in the absence of the SRL.

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EF-Tu

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