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mRNA Display Pipeline for Protein Biosensor Construction

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Titel: mRNA Display Pipeline for Protein Biosensor Construction
Autoren: Cui, Zhenling, Ayva, Cagla Ergun, Liew, Yi Jin, Guo, Zhong, Mutschler, Roxane, Dreier, Birgit, Fiorito, Maria M, Walden, Patricia, Howard, Christopher B, Ely, Fernanda, Plückthun, Andreas, Pretorius, Carel, Ungerer, Jacobus Pj, Buckle, Ashley M, Alexandrov, Kirill
Weitere Verfasser: University of Zurich, Alexandrov, Kirill
Quelle: ACS Sens
Verlagsinformationen: American Chemical Society (ACS), 2024.
Publikationsjahr: 2024
Schlagwörter: 1502 Bioengineering, Calmodulin, 3105 Instrumentation, 1507 Fluid Flow and Transfer Processes, 10019 Department of Biochemistry, 570 Life sciences, biology, Humans, 610 Medicine & health, Biosensing Techniques, RNA, Messenger, 1508 Process Chemistry and Technology
Beschreibung: Despite the significant potential of protein biosensors, their construction remains a trial-and-error process. The most obvious approach for addressing this is to utilize modular biosensor architectures where specificity-conferring modalities can be readily generated to recognize new targets. Toward this goal, we established a workflow that uses mRNA display-based selection of hyper-stable monobody domains for the target of choice or ribosome display to select equally stable DARPins. These binders were integrated into a two-component allosteric biosensor architecture based on a calmodulin-reporter chimera. This workflow was tested by developing biosensors for liver toxicity markers such as cytosolic aspartate aminotransferase, mitochondrial aspartate aminotransferase, and alanine aminotransferase 1. We demonstrate that our pipeline consistently produced >103 unique binders for each target within a week. Our analysis revealed that the affinity of the binders for their targets was not a direct predictor of the binder's performance in a biosensor context. The interactions between the binding domains and the reporter module affect the biosensor activity and the dynamic range. We conclude that following binding domain selection, the multiplexed biosensor assembly and prototyping appear to be the most promising approach for identifying biosensors with the desired properties.
Publikationsart: Article
Other literature type
Dateibeschreibung: ZORA261909.pdf - application/pdf
Sprache: English
ISSN: 2379-3694
DOI: 10.1021/acssensors.3c02471
DOI: 10.5167/uzh-261909
Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/38807313
Rights: CC BY NC ND
Dokumentencode: edsair.doi.dedup.....2b067d8145890c3d2d3f5ebfcfccb7b5
Datenbank: OpenAIRE
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  Data: mRNA Display Pipeline for Protein Biosensor Construction
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  Data: <searchLink fieldCode="AR" term="%22Cui%2C+Zhenling%22">Cui, Zhenling</searchLink><br /><searchLink fieldCode="AR" term="%22Ayva%2C+Cagla+Ergun%22">Ayva, Cagla Ergun</searchLink><br /><searchLink fieldCode="AR" term="%22Liew%2C+Yi+Jin%22">Liew, Yi Jin</searchLink><br /><searchLink fieldCode="AR" term="%22Guo%2C+Zhong%22">Guo, Zhong</searchLink><br /><searchLink fieldCode="AR" term="%22Mutschler%2C+Roxane%22">Mutschler, Roxane</searchLink><br /><searchLink fieldCode="AR" term="%22Dreier%2C+Birgit%22">Dreier, Birgit</searchLink><br /><searchLink fieldCode="AR" term="%22Fiorito%2C+Maria+M%22">Fiorito, Maria M</searchLink><br /><searchLink fieldCode="AR" term="%22Walden%2C+Patricia%22">Walden, Patricia</searchLink><br /><searchLink fieldCode="AR" term="%22Howard%2C+Christopher+B%22">Howard, Christopher B</searchLink><br /><searchLink fieldCode="AR" term="%22Ely%2C+Fernanda%22">Ely, Fernanda</searchLink><br /><searchLink fieldCode="AR" term="%22Plückthun%2C+Andreas%22">Plückthun, Andreas</searchLink><br /><searchLink fieldCode="AR" term="%22Pretorius%2C+Carel%22">Pretorius, Carel</searchLink><br /><searchLink fieldCode="AR" term="%22Ungerer%2C+Jacobus+Pj%22">Ungerer, Jacobus Pj</searchLink><br /><searchLink fieldCode="AR" term="%22Buckle%2C+Ashley+M%22">Buckle, Ashley M</searchLink><br /><searchLink fieldCode="AR" term="%22Alexandrov%2C+Kirill%22">Alexandrov, Kirill</searchLink>
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  Data: University of Zurich<br />Alexandrov, Kirill
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  Data: ACS Sens
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  Data: American Chemical Society (ACS), 2024.
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  Data: 2024
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  Data: <searchLink fieldCode="DE" term="%221502+Bioengineering%22">1502 Bioengineering</searchLink><br /><searchLink fieldCode="DE" term="%22Calmodulin%22">Calmodulin</searchLink><br /><searchLink fieldCode="DE" term="%223105+Instrumentation%22">3105 Instrumentation</searchLink><br /><searchLink fieldCode="DE" term="%221507+Fluid+Flow+and+Transfer+Processes%22">1507 Fluid Flow and Transfer Processes</searchLink><br /><searchLink fieldCode="DE" term="%2210019+Department+of+Biochemistry%22">10019 Department of Biochemistry</searchLink><br /><searchLink fieldCode="DE" term="%22570+Life+sciences%22">570 Life sciences</searchLink><br /><searchLink fieldCode="DE" term="%22biology%22">biology</searchLink><br /><searchLink fieldCode="DE" term="%22Humans%22">Humans</searchLink><br /><searchLink fieldCode="DE" term="%22610+Medicine+%26+health%22">610 Medicine & health</searchLink><br /><searchLink fieldCode="DE" term="%22Biosensing+Techniques%22">Biosensing Techniques</searchLink><br /><searchLink fieldCode="DE" term="%22RNA%2C+Messenger%22">RNA, Messenger</searchLink><br /><searchLink fieldCode="DE" term="%221508+Process+Chemistry+and+Technology%22">1508 Process Chemistry and Technology</searchLink>
– Name: Abstract
  Label: Description
  Group: Ab
  Data: Despite the significant potential of protein biosensors, their construction remains a trial-and-error process. The most obvious approach for addressing this is to utilize modular biosensor architectures where specificity-conferring modalities can be readily generated to recognize new targets. Toward this goal, we established a workflow that uses mRNA display-based selection of hyper-stable monobody domains for the target of choice or ribosome display to select equally stable DARPins. These binders were integrated into a two-component allosteric biosensor architecture based on a calmodulin-reporter chimera. This workflow was tested by developing biosensors for liver toxicity markers such as cytosolic aspartate aminotransferase, mitochondrial aspartate aminotransferase, and alanine aminotransferase 1. We demonstrate that our pipeline consistently produced >103 unique binders for each target within a week. Our analysis revealed that the affinity of the binders for their targets was not a direct predictor of the binder's performance in a biosensor context. The interactions between the binding domains and the reporter module affect the biosensor activity and the dynamic range. We conclude that following binding domain selection, the multiplexed biosensor assembly and prototyping appear to be the most promising approach for identifying biosensors with the desired properties.
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  Data: 2379-3694
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  Data: 10.1021/acssensors.3c02471
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  Data: 10.5167/uzh-261909
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  Data: <link linkTarget="URL" linkTerm="https://pubmed.ncbi.nlm.nih.gov/38807313" linkWindow="_blank">https://pubmed.ncbi.nlm.nih.gov/38807313</link>
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  Data: CC BY NC ND
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  Data: edsair.doi.dedup.....2b067d8145890c3d2d3f5ebfcfccb7b5
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