Barrenechea Victor, Vargas-Reyes Maryhory, Quiliano Miguel, Milón Pohl
Faculty of Health Sciences, Centre for Research and Innovation, Universidad Peruana de Ciencias Aplicadas (UPC), Lima, Peru.
Postgraduate Unit, Medicine Faculty, Universidad Nacional Mayor de San Marcos, Lima, Peru.
Front Microbiol. 2021 Jun 28;12:682682. doi: 10.3389/fmicb.2021.682682. eCollection 2021.
Tetracycline has positively impacted human health as well as the farming and animal industries. Its extensive usage and versatility led to the spread of resistance mechanisms followed by the development of new variants of the antibiotic. Tetracyclines inhibit bacterial growth by impeding the binding of elongator tRNAs to the ribosome. However, a small number of reports indicated that Tetracyclines could also inhibit translation initiation, yet the molecular mechanism remained unknown. Here, we use biochemical and computational methods to study how Oxytetracycline (Otc), Demeclocycline (Dem), and Tigecycline (Tig) affect the translation initiation phase of protein synthesis. Our results show that all three Tetracyclines induce Initiation Factor IF3 to adopt a compact conformation on the 30S ribosomal subunit, similar to that induced by Initiation Factor IF1. This compaction was faster for Tig than Dem or Otc. Furthermore, all three tested tetracyclines affected IF1-bound 30S complexes. The dissociation rate constant of IF1 in early 30S complexes was 14-fold slower for Tig than Dem or Otc. Late 30S initiation complexes (30S pre-IC or IC) exhibited greater IF1 stabilization by Tig than for Dem and Otc. Tig and Otc delayed 50S joining to 30S initiation complexes (30S ICs). Remarkably, the presence of Tig considerably slowed the progression to translation elongation and retained IF1 in the resulting 70S initiation complex (70S IC). Molecular modeling of Tetracyclines bound to the 30S pre-IC and 30S IC indicated that the antibiotics binding site topography fluctuates along the initiation pathway. Mainly, 30S complexes show potential contacts between Dem or Tig with IF1, providing a structural rationale for the enhanced affinity of the antibiotics in the presence of the factor. Altogether, our data indicate that Tetracyclines inhibit translation initiation by allosterically perturbing the IF3 layout on the 30S, retaining IF1 during 70S IC formation, and slowing the transition toward translation elongation. Thus, this study describes a new complementary mechanism by which Tetracyclines may inhibit bacterial protein synthesis.
四环素对人类健康以及农业和畜牧业都产生了积极影响。其广泛的使用和多功能性导致了耐药机制的传播,随后出现了新的抗生素变体。四环素通过阻止延伸tRNA与核糖体的结合来抑制细菌生长。然而,少数报告表明四环素也可以抑制翻译起始,但其分子机制仍然未知。在这里,我们使用生化和计算方法来研究土霉素(Otc)、地美环素(Dem)和替加环素(Tig)如何影响蛋白质合成的翻译起始阶段。我们的结果表明,所有三种四环素都能诱导起始因子IF3在30S核糖体亚基上形成紧凑构象,类似于起始因子IF1诱导的构象。替加环素诱导这种构象紧凑的速度比地美环素或土霉素更快。此外,所有三种测试的四环素都会影响与IF1结合的30S复合物。在早期30S复合物中,替加环素存在时IF1的解离速率常数比地美环素或土霉素慢14倍。晚期30S起始复合物(30S预起始复合物或起始复合物)中,替加环素对IF1的稳定作用比对地美环素和土霉素更强。替加环素和土霉素会延迟50S与30S起始复合物(30S起始复合物)的结合。值得注意的是,替加环素的存在显著减缓了向翻译延伸的进程,并使IF1保留在形成的70S起始复合物(70S起始复合物)中。与30S预起始复合物和30S起始复合物结合的四环素的分子模型表明,抗生素结合位点的拓扑结构在起始途径中会发生波动。主要是,30S复合物显示地美环素或替加环素与IF1之间存在潜在接触,这为在该因子存在时抗生素亲和力增强提供了结构依据。总之,我们的数据表明,四环素通过变构干扰30S上的IF3布局、在70S起始复合物形成过程中保留IF1以及减缓向翻译延伸的转变来抑制翻译起始。因此,本研究描述了四环素抑制细菌蛋白质合成的一种新的互补机制。