dc.date.accessioned | 2020-09-14T18:03:22Z | |
dc.date.available | 2020-09-14T18:03:22Z | |
dc.date.created | 2020-09-09T09:35:27Z | |
dc.date.issued | 2020 | |
dc.identifier.citation | Hatlem, Daniel Trunk, Thomas Linke, Dirk Leo, Jack Christopher . Catching a SPY: Using the SpyCatcher-SpyTag and Related Systems for Labeling and Localizing Bacterial Proteins. Microbial Virulence Factors. 2020, 371-400 MDPI | |
dc.identifier.uri | http://hdl.handle.net/10852/79370 | |
dc.description.abstract | The SpyCatcher-SpyTag system was developed seven years ago as a method for protein ligation. It is based on a modified domain from a Streptococcus pyogenes surface protein (SpyCatcher), which recognizes a cognate 13-amino-acid peptide (SpyTag). Upon recognition, the two form a covalent isopeptide bond between the side chains of a lysine in SpyCatcher and an aspartate in SpyTag. This technology has been used, among other applications, to create covalently stabilized multi-protein complexes, for modular vaccine production, and to label proteins (e.g., for microscopy). The SpyTag system is versatile as the tag is a short, unfolded peptide that can be genetically fused to exposed positions in target proteins; similarly, SpyCatcher can be fused to reporter proteins such as GFP, and to epitope or purification tags. Additionally, an orthogonal system called SnoopTag-SnoopCatcher has been developed from an S. pneumoniae pilin that can be combined with SpyCatcher-SpyTag to produce protein fusions with multiple components. Furthermore, tripartite applications have been produced from both systems allowing the fusion of two peptides by a separate, catalytically active protein unit, SpyLigase or SnoopLigase. Here, we review the current state of the SpyCatcher-SpyTag and related technologies, with a particular emphasis on their use in vaccine development and in determining outer membrane protein localization and topology of surface proteins in bacteria. | |
dc.language | EN | |
dc.publisher | MDPI | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.title | Catching a SPY: Using the SpyCatcher-SpyTag and Related Systems for Labeling and Localizing Bacterial Proteins | |
dc.type | Chapter | |
dc.creator.author | Hatlem, Daniel | |
dc.creator.author | Trunk, Thomas | |
dc.creator.author | Linke, Dirk | |
dc.creator.author | Leo, Jack Christopher | |
cristin.unitcode | 185,15,29,0 | |
cristin.unitname | Institutt for biovitenskap | |
cristin.ispublished | true | |
cristin.fulltext | original | |
dc.identifier.cristin | 1828269 | |
dc.identifier.bibliographiccitation | info:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:book&rft.btitle=Microbial Virulence Factors&rft.spage=371&rft.date=2020 | |
dc.identifier.startpage | 371 | |
dc.identifier.endpage | 400 | |
dc.identifier.pagecount | 400 | |
dc.identifier.doi | https://doi.org/10.3390/ijms20092129 | |
dc.identifier.urn | URN:NBN:no-82474 | |
dc.type.document | Bokkapittel | |
dc.type.peerreviewed | Peer reviewed | |
dc.source.isbn | 978-3-03936-946-1 | |
dc.identifier.fulltext | Fulltext https://www.duo.uio.no/bitstream/handle/10852/79370/4/ijms-20-02129.pdf | |
dc.type.version | PublishedVersion | |
cristin.btitle | Microbial Virulence Factors | |
dc.relation.project | NFR/267434 | |
dc.relation.project | NFR/230576 | |
dc.relation.project | EC/H2020/765042 | |