Scholarlink

Objective <p>The Type VI Secretion System (T6SS) is a contractile apparatus made of several proteins playing a significant role in the fitness and virulence of many Gram-negative bacteria. The SPI-19 T6SS gene cluster is a virulence factor of <i>Salmonella</i> Dublin contributing to host colonization and antibacterial activity. Previously, we demonstrated that SED_RS06335 (an Rhs protein with a C-terminal M91 domain) is responsible for antibacterial activity of the T6SS<sub>SPI−19</sub>; however, the role of the M91 domain in this phenotype is unknown. Thus, the objective of this study is to provide experimental evidence that the antibacterial activity of SED_RS06335 effector is attributable to its C-terminal M91 domain.</p> Results <p>Here, we determine through interbacterial competition and heterologous expression assays that M91 domain of SED_RS06335 displays antibacterial activity. Furthermore, a three-dimensional structural model of M91 domain revealed a high similarity with the metallopeptidase neurotoxin type A (BotA) from <i>Clostridium botulinum</i>. Interestingly, our results suggest that the M91 domain is responsible for the antibacterial activity of the SED_RS06335 effector in <i>Salmonella</i> Dublin.</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

The M91 metallopeptidase domain of the T6SS effector protein SED_RS06335 encoded in Salmonella Dublin SPI-19 exhibits antibacterial activity

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年6月25日

查看全文
  • Carla Vargas-del Río,
  • Ayleen Parra-Calisto,
  • Carlos J. Blondel,
  • Felipe Reyes-Méndez,
  • Fernando A. Amaya,
  • Carlos A. Santiviago,
  • Andrea Avilés,
  • Victoria Soriano-Mora,
  • Daniel Chacín,
  • David Pezoa

摘要

Objective

The Type VI Secretion System (T6SS) is a contractile apparatus made of several proteins playing a significant role in the fitness and virulence of many Gram-negative bacteria. The SPI-19 T6SS gene cluster is a virulence factor of Salmonella Dublin contributing to host colonization and antibacterial activity. Previously, we demonstrated that SED_RS06335 (an Rhs protein with a C-terminal M91 domain) is responsible for antibacterial activity of the T6SSSPI−19; however, the role of the M91 domain in this phenotype is unknown. Thus, the objective of this study is to provide experimental evidence that the antibacterial activity of SED_RS06335 effector is attributable to its C-terminal M91 domain.

Results

Here, we determine through interbacterial competition and heterologous expression assays that M91 domain of SED_RS06335 displays antibacterial activity. Furthermore, a three-dimensional structural model of M91 domain revealed a high similarity with the metallopeptidase neurotoxin type A (BotA) from Clostridium botulinum. Interestingly, our results suggest that the M91 domain is responsible for the antibacterial activity of the SED_RS06335 effector in Salmonella Dublin.