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ORIGINAL RESEARCH article
Front. Bioeng. Biotechnol.
Sec. Synthetic Biology
Volume 13 - 2025 | doi: 10.3389/fbioe.2025.1529655
This article is part of the Research TopicFusion Proteins for the Detection of Pathogens or Pathogen ReceptorsView all 4 articles
In Situ Intein-Mediated Multiprotein Assembly via Engineered Cross-Species Consortia
Provisionally accepted- 1MGI Tech Co., Ltd., Shenzhen, China
- 2Shenzhen Haolthy Biotechnology Co., Ltd,, Shenzhen,, China
- 3Shenzhen Bay Laboratory, Institute of Molecular Physiology, Shenzhen, China
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Inteins can connect flanking external proteins into a new protein fragment and excise themselves. Here, we report the in situ splicing of proteins by engineered microbial consortia. This study pioneers a programmable microbial consortia platform enabling in situ protein splicing through split intein-mediated assembly. Engineered E. coli with the ePop autolysis system release intein-fused protein fragments via synchronized lysis, while Pichia pastoris secretes complementary domains, enabling extracellular reconstitution directly in culture. With the application of integrating quorum-sensing controls and eukaryotic secretion pathways, this approach bypasses in vitro purification, supporting scalable one-pot synthesis of multiple functional proteins. The platform's versatility in logic computation and antibiotic resistance engineering highlights its potential for adaptive biomanufacturing and context-aware biomaterial design.
Keywords: Protein Splicing, E. coli, P. pastoris, Consortia, Split intein
Received: 17 Nov 2024; Accepted: 09 Apr 2025.
Copyright: © 2025 Wang, Kang and Gao. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence:
Hao Wang, MGI Tech Co., Ltd., Shenzhen, China
Hui Gao, Shenzhen Bay Laboratory, Institute of Molecular Physiology, Shenzhen, China
Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.