Design and characterization of peptide-responsive biosensors

Abstract

Gram-positive bacteria use secreted peptides and peptide-responsive transcription factors for quorum sensing. Here, we demonstrate that intracellular expression of these peptide effectors with their cognate transcription factors leads to regulation of gene expression in both in vitro and in vivo systems. Because both effector and regulatory parts can be readily expressed, complex circuits, including auto-activation schemes, can be developed, with switch-like behaviors. Moreover, the peptide effectors can be fused to proteins, enabling a direct intracellular readout of translation and potentially allowing any protein to encode regulatory interactions in cells. Our results support a foundation for regulatory circuits that extend beyond canonical components such as LacI and TetR.

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BibTeX RIS

BibTeX

@misc{brown2026design,
  title = {{Design and characterization of peptide-responsive biosensors}},
  author = {D. M. Brown and A. Clark-ElSayed and M. T. Mott and I. Madrigal Harrison and B. Graham Hendrickson and J. B. Lucks and A. D. Ellington},
  howpublished = {bioRxiv},
  year = {2026},
  month = oct,
  doi = {10.64898/2026.10.03.755986},
  url = {https://www.biorxiv.org/content/10.64898/2026.10.03.755986v1},
  note = {CC BY-NC-ND},
}

RIS

TY  - UNPB
TI  - Design and characterization of peptide-responsive biosensors
AU  - D. M. Brown
AU  - A. Clark-ElSayed
AU  - M. T. Mott
AU  - I. Madrigal Harrison
AU  - B. Graham Hendrickson
AU  - J. B. Lucks
AU  - A. D. Ellington
PY  - 2026
DA  - 2026/10/03
PB  - bioRxiv
DO  - 10.64898/2026.10.03.755986
UR  - https://www.biorxiv.org/content/10.64898/2026.10.03.755986v1
AB  - Gram-positive bacteria use secreted peptides and peptide-responsive transcription factors for quorum sensing. Here, we demonstrate that intracellular expression of these peptide effectors with their cognate transcription factors leads to regulation of gene expression in both in vitro and in vivo systems. Because both effector and regulatory parts can be readily expressed, complex circuits, including auto-activation schemes, can be developed, with switch-like behaviors. Moreover, the peptide effectors can be fused to proteins, enabling a direct intracellular readout of translation and potentially allowing any protein to encode regulatory interactions in cells. Our results support a foundation for regulatory circuits that extend beyond canonical components such as LacI and TetR.
ER  -

Abstract

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