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Peer-reviewedCC BYAdvanced Science

Streptavidins Coordinate Biotin Sequestration and Self‐Resistance Within a Biotin‐Pathway Antibiotic Network

  • Sumire Kurosawa1,2,3
  • Jingjun Mo1,2,3
  • Xiaotong Diao4
  • Feng Xie2,3
  • Tingting Wang2,3
  • Haowen Zhao1,2,3
  • Dalei Wu4
  • Rolf Müller1,5,2,3,6
  • Chengzhang Fu2,3,6
6 affiliations
  1. 1Department of Pharmacy Saarland University Saarbrücken Germany
  2. 2Helmholtz Institute for Pharmaceutical Research Saarland (HIPS) Helmholtz Centre for Infection Research (HZI) Saarbrücken Germany
  3. 3Helmholtz International Lab for Anti‐Infectives Helmholtz Center for Infection Research Braunschweig Germany
  4. 4Helmholtz International Lab for Anti‐Infectives State Key Laboratory of Microbial Technology Shandong University Qingdao China
  5. 5German Centre for Infection Research (DZIF) Braunschweig Germany
  6. 6PharmaScienceHub Saarbrücken Germany
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Abstract

Streptavidin, the well-known biotin-binding protein extensively used in biotechnology, is naturally co-produced in Streptomyces avidinii alongside stravidins-inhibitors of biotin biosynthesis. Here, we uncover and activate a conserved genomic region flanked by two streptavidin genes, revealing multiple biosynthetic gene clusters that produce diverse biotin-related metabolites, including stravidins, acidomycin, α-methyl-KAPA, α-methyldesthiobiotin, and the novel non-proteinogenic amino acid 2-aminonona-5,7-dienedioic acid (ANDA). We show α-methyldesthiobiotin arises from α-methyl-KAPA, illustrating how methylated analogues interfere with distinct steps of biotin biosynthesis. Contrary to the view that streptavidin functions solely by sequestering biotin, our biochemical, structural, and bioactivity analyses demonstrate that it also binds acidomycin, neutralizing its antibacterial activity to protect the producer while likely facilitating compound secretion. The crystal structure of the streptavidin-acidomycin complex reveals the molecular basis for this dual functionality. Our findings establish a multifunctional streptavidin that integrates biotin sequestration and self-resistance to balance an antibiotic network targeting the biotin pathway in microbial competition.

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Cite

BibTeXRIS
BibTeX
@article{kurosawa2026streptavidins,
  title = {{Streptavidins Coordinate Biotin Sequestration and Self‐Resistance Within a Biotin‐Pathway Antibiotic Network}},
  author = {Sumire Kurosawa and Jingjun Mo and Xiaotong Diao and Feng Xie and Tingting Wang and Haowen Zhao and Dalei Wu and Rolf Müller and Chengzhang Fu},
  journal = {Advanced Science},
  year = {2026},
  month = may,
  doi = {10.1002/advs.202523813},
  url = {https://doi.org/10.1002/advs.202523813},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Streptavidins Coordinate Biotin Sequestration and Self‐Resistance Within a Biotin‐Pathway Antibiotic Network
AU  - Sumire Kurosawa
AU  - Jingjun Mo
AU  - Xiaotong Diao
AU  - Feng Xie
AU  - Tingting Wang
AU  - Haowen Zhao
AU  - Dalei Wu
AU  - Rolf Müller
AU  - Chengzhang Fu
PY  - 2026
DA  - 2026/05/23
JO  - Advanced Science
DO  - 10.1002/advs.202523813
UR  - https://doi.org/10.1002/advs.202523813
AB  - Streptavidin, the well-known biotin-binding protein extensively used in biotechnology, is naturally co-produced in Streptomyces avidinii alongside stravidins-inhibitors of biotin biosynthesis. Here, we uncover and activate a conserved genomic region flanked by two streptavidin genes, revealing multiple biosynthetic gene clusters that produce diverse biotin-related metabolites, including stravidins, acidomycin, α-methyl-KAPA, α-methyldesthiobiotin, and the novel non-proteinogenic amino acid 2-aminonona-5,7-dienedioic acid (ANDA). We show α-methyldesthiobiotin arises from α-methyl-KAPA, illustrating how methylated analogues interfere with distinct steps of biotin biosynthesis. Contrary to the view that streptavidin functions solely by sequestering biotin, our biochemical, structural, and bioactivity analyses demonstrate that it also binds acidomycin, neutralizing its antibacterial activity to protect the producer while likely facilitating compound secretion. The crystal structure of the streptavidin-acidomycin complex reveals the molecular basis for this dual functionality. Our findings establish a multifunctional streptavidin that integrates biotin sequestration and self-resistance to balance an antibiotic network targeting the biotin pathway in microbial competition.
SN  - 2198-3844
ER  -