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<p>Antimicrobial peptides with broad-spectrum antibacterial properties have emerged as promising candidates for combating bacterial infections. Laterosporulin (LS), a class II bacteriocin initially isolated from <i>Brevibacillus</i> sp. strain GI-9, has demonstrated broad-spectrum antibacterial activity and notable biochemical characteristics. However, the limited expression levels of LS in <i>Brevibacillus</i> sp. GI-9 restrict its potential for large-scale production and therapeutic and food preservation applications. In this study, a triple peptide comprising three tandem repeats of LS (3 × LS), tagged with C-terminal hemagglutinin (HA) and 6 × His, was successfully expressed heterologously in <i>Chlamydomonas reinhardtii</i>. The purified 3 × LS-HA-6 × His effectively inhibited the growth of both Gram-positive and Gram-negative bacteria. Additionally, 3 × LS-HA-6 × His demonstrated stable antibacterial activity over a wide range of temperatures and pH values and showed significant resistance to multiple proteolytic enzymes. Furthermore, 3 × LS-HA-6 × His disrupted bacterial cell membrane integrity while exhibiting nonhemolytic activity toward rabbit erythrocytes and noncytotoxicity toward HEK293T cells. These findings underscore the potential of <i>C. reinhardtii</i> as a promising host for the production of bioactive and biosafe LS, providing valuable insights for the development of alternative antimicrobial strategies.</p>

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Expression and Characterization of Recombinant Triple Laterosporulin in Chlamydomonas reinhardtii

  • 期刊论文

  • 发表日期：

    2025年3月25日

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  • Bin Xue,
  • Yang-Yang Li,
  • Bei-Feng-Chu Zheng,
  • Chan Zhang,
  • Hadiatullah Hadiatullah,
  • Wen-Ting Dai,
  • Ya-Jun Wang,
  • Zhen-Chuan Fan

摘要

Antimicrobial peptides with broad-spectrum antibacterial properties have emerged as promising candidates for combating bacterial infections. Laterosporulin (LS), a class II bacteriocin initially isolated from Brevibacillus sp. strain GI-9, has demonstrated broad-spectrum antibacterial activity and notable biochemical characteristics. However, the limited expression levels of LS in Brevibacillus sp. GI-9 restrict its potential for large-scale production and therapeutic and food preservation applications. In this study, a triple peptide comprising three tandem repeats of LS (3 × LS), tagged with C-terminal hemagglutinin (HA) and 6 × His, was successfully expressed heterologously in Chlamydomonas reinhardtii. The purified 3 × LS-HA-6 × His effectively inhibited the growth of both Gram-positive and Gram-negative bacteria. Additionally, 3 × LS-HA-6 × His demonstrated stable antibacterial activity over a wide range of temperatures and pH values and showed significant resistance to multiple proteolytic enzymes. Furthermore, 3 × LS-HA-6 × His disrupted bacterial cell membrane integrity while exhibiting nonhemolytic activity toward rabbit erythrocytes and noncytotoxicity toward HEK293T cells. These findings underscore the potential of C. reinhardtii as a promising host for the production of bioactive and biosafe LS, providing valuable insights for the development of alternative antimicrobial strategies.