Scholarlink

<p><i>Rhodococcus equi</i> is an important veterinary and zoonotic pathogen that survives inside macrophage phagolysosomes. Nitrate reductase NarGHI is a known virulence factor for this pathogen. This enzyme complex serves as the terminal electron acceptor in anaerobic respiration in other pathogens, such as the phylogenetically related <i>Mycobacterium tuberculosis</i>. A recent study demonstrated that <i>R. equi</i> survives under anaerobic conditions. In this work, we endeavored to uncover the electron transport chain complexes of <i>R. equi</i>. By in silico comparison to known complexes in the Transporter Classification Database, 67 putative respiratory chain proteins were identified in <i>R. equi </i>103S. Their distribution was evaluated in the genomes of 37 clinical (animal and human infections) and 297 non-clinical (environmental) <i>Rhodococcus</i> isolates from the NCBI RefSeq database. NarGHI subunits were found in 100% of clinical and 35% of non-clinical genomes. Loci encoding four potential electron donor complexes (a membrane-bound formate dehydrogenase, a succinate dehydrogenase, and two Ni-Fe hydrogenases) were present in &gt; 80% of clinical and &lt; 50% of non-clinical isolates. Loci encoding a nitric oxide reductase, a potential terminal electron acceptor, were identified in 40.5% of clinical and 2% of non-clinical isolates. The results show that the respiratory chain in <i>R. equi</i> is highly complex, and point to potential metabolic adaptations of this species to hypoxic conditions.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Adaptations in electron transport chain complexes of clinical Rhodococcus equi revealed through comparative genomics

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年7月4日

查看全文
  • João Pedro Vasques da Conceição,
  • Fabio Faria da Mota

摘要

Rhodococcus equi is an important veterinary and zoonotic pathogen that survives inside macrophage phagolysosomes. Nitrate reductase NarGHI is a known virulence factor for this pathogen. This enzyme complex serves as the terminal electron acceptor in anaerobic respiration in other pathogens, such as the phylogenetically related Mycobacterium tuberculosis. A recent study demonstrated that R. equi survives under anaerobic conditions. In this work, we endeavored to uncover the electron transport chain complexes of R. equi. By in silico comparison to known complexes in the Transporter Classification Database, 67 putative respiratory chain proteins were identified in R. equi 103S. Their distribution was evaluated in the genomes of 37 clinical (animal and human infections) and 297 non-clinical (environmental) Rhodococcus isolates from the NCBI RefSeq database. NarGHI subunits were found in 100% of clinical and 35% of non-clinical genomes. Loci encoding four potential electron donor complexes (a membrane-bound formate dehydrogenase, a succinate dehydrogenase, and two Ni-Fe hydrogenases) were present in > 80% of clinical and < 50% of non-clinical isolates. Loci encoding a nitric oxide reductase, a potential terminal electron acceptor, were identified in 40.5% of clinical and 2% of non-clinical isolates. The results show that the respiratory chain in R. equi is highly complex, and point to potential metabolic adaptations of this species to hypoxic conditions.