Article ; Online: Cell surface β-lactamase recruitment: A facile selection to identify protein-protein interactions.
Protein science : a publication of the Protein Society
2024 Volume 33, Issue 4, Page(s) e4919
Abstract: Protein-protein interactions (PPIs) are central to many cellular processes, and the identification of novel PPIs is a critical step in the discovery of protein therapeutics. Simple methods to identify naturally existing or laboratory evolved PPIs are ... ...
Abstract | Protein-protein interactions (PPIs) are central to many cellular processes, and the identification of novel PPIs is a critical step in the discovery of protein therapeutics. Simple methods to identify naturally existing or laboratory evolved PPIs are therefore valuable research tools. We have developed a facile selection that links PPI-dependent β-lactamase recruitment on the surface of Escherichia coli with resistance to ampicillin. Bacteria displaying a protein that forms a complex with a specific protein-β-lactamase fusion are protected from ampicillin-dependent cell death. In contrast, bacteria that do not recruit β-lactamase to the cell surface are killed by ampicillin. Given its simplicity and tunability, we anticipate this selection will be a valuable addition to the palette of methods for illuminating and interrogating PPIs. |
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MeSH term(s) | beta-Lactamases/genetics ; beta-Lactamases/metabolism ; Ampicillin/pharmacology ; Ampicillin/metabolism ; Bacteria/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Cell Membrane/metabolism ; Anti-Bacterial Agents/metabolism |
Chemical Substances | beta-Lactamases (EC 3.5.2.6) ; Ampicillin (7C782967RD) ; Anti-Bacterial Agents |
Language | English |
Publishing date | 2024-03-19 |
Publishing country | United States |
Document type | Journal Article |
ZDB-ID | 1106283-6 |
ISSN | 1469-896X ; 0961-8368 |
ISSN (online) | 1469-896X |
ISSN | 0961-8368 |
DOI | 10.1002/pro.4919 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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