Chemogenetic Control of Nanobodies
We introduce an engineered nanobody whose affinity to green fluorescent protein (GFP) can be switched on and off with small molecules. By controlling the cellular localization of GFP fusion proteins, the engineered nanobody allows interrogation of their roles in basic biological processes, an approa...
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| Veröffentlicht in: | Nature methods 2020-03, Vol.17 (3), p.279-282 |
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| container_title | Nature methods |
| container_volume | 17 |
| creator | Farrants, Helen Tarnawski, Miroslaw Müller, Thorsten G. Otsuka, Shotaro Hiblot, Julien Koch, Birgit Kueblbeck, Moritz Kräusslich, Hans-Georg Ellenberg, Jan Johnsson, Kai |
| description | We introduce an engineered nanobody whose affinity to green fluorescent protein (GFP) can be switched on and off with small molecules. By controlling the cellular localization of GFP fusion proteins, the engineered nanobody allows interrogation of their roles in basic biological processes, an approach that should be applicable to numerous previously described GFP fusions. We also outline how the binding affinities of other nanobodies can be controlled by small molecules.
Engineered nanobody allows reversible control of activity in cells through the binding of small molecules. |
| doi_str_mv | 10.1038/s41592-020-0746-7 |
| format | Article |
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Engineered nanobody allows reversible control of activity in cells through the binding of small molecules.</description><identifier>ISSN: 1548-7091</identifier><identifier>EISSN: 1548-7105</identifier><identifier>DOI: 10.1038/s41592-020-0746-7</identifier><identifier>PMID: 32066961</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/1647/338/469 ; 631/61/338/552 ; 631/92/469 ; Affinity ; Antibodies ; Binding ; Bioinformatics ; Biological activity ; Biological Microscopy ; Biological Techniques ; Biology ; Biomedical and Life Sciences ; Biomedical Engineering/Biotechnology ; Brief Communication ; Crystallography, X-Ray ; Databases, Protein ; Dihydrofolate reductase ; DNA - chemistry ; Escherichia coli ; Fluorescence ; Fluorescence Resonance Energy Transfer ; Gene Products, gag - chemistry ; Genetic aspects ; Genetic engineering ; Genetic research ; Green fluorescent protein ; Green Fluorescent Proteins - chemistry ; Health aspects ; HEK293 Cells ; HeLa Cells ; HIV-1 - chemistry ; Humans ; Immunoglobulin Fragments - chemistry ; Interrogation ; Kinetics ; Life Sciences ; Ligands ; Localization ; Medical research ; Medicine, Experimental ; Microscopy, Fluorescence ; Mitosis ; Nanobodies ; Nanomedicine ; Nanoparticles - chemistry ; nef Gene Products, Human Immunodeficiency Virus - chemistry ; Physiological aspects ; Protein Domains ; Proteins ; Proteomics ; Single-Domain Antibodies - chemistry ; Viral antibodies</subject><ispartof>Nature methods, 2020-03, Vol.17 (3), p.279-282</ispartof><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2020</rights><rights>COPYRIGHT 2020 Nature Publishing Group</rights><rights>2020© The Author(s), under exclusive licence to Springer Nature America, Inc. 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-992be37e616ff537efbf46a3c374cab87d4b03821057e59408ef2d2310ee8a253</citedby><cites>FETCH-LOGICAL-c482t-992be37e616ff537efbf46a3c374cab87d4b03821057e59408ef2d2310ee8a253</cites><orcidid>0000-0002-8002-1981</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41592-020-0746-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41592-020-0746-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32066961$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Farrants, Helen</creatorcontrib><creatorcontrib>Tarnawski, Miroslaw</creatorcontrib><creatorcontrib>Müller, Thorsten G.</creatorcontrib><creatorcontrib>Otsuka, Shotaro</creatorcontrib><creatorcontrib>Hiblot, Julien</creatorcontrib><creatorcontrib>Koch, Birgit</creatorcontrib><creatorcontrib>Kueblbeck, Moritz</creatorcontrib><creatorcontrib>Kräusslich, Hans-Georg</creatorcontrib><creatorcontrib>Ellenberg, Jan</creatorcontrib><creatorcontrib>Johnsson, Kai</creatorcontrib><title>Chemogenetic Control of Nanobodies</title><title>Nature methods</title><addtitle>Nat Methods</addtitle><addtitle>Nat Methods</addtitle><description>We introduce an engineered nanobody whose affinity to green fluorescent protein (GFP) can be switched on and off with small molecules. By controlling the cellular localization of GFP fusion proteins, the engineered nanobody allows interrogation of their roles in basic biological processes, an approach that should be applicable to numerous previously described GFP fusions. We also outline how the binding affinities of other nanobodies can be controlled by small molecules.
Engineered nanobody allows reversible control of activity in cells through the binding of small molecules.</description><subject>631/1647/338/469</subject><subject>631/61/338/552</subject><subject>631/92/469</subject><subject>Affinity</subject><subject>Antibodies</subject><subject>Binding</subject><subject>Bioinformatics</subject><subject>Biological activity</subject><subject>Biological Microscopy</subject><subject>Biological Techniques</subject><subject>Biology</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedical Engineering/Biotechnology</subject><subject>Brief Communication</subject><subject>Crystallography, X-Ray</subject><subject>Databases, Protein</subject><subject>Dihydrofolate reductase</subject><subject>DNA - chemistry</subject><subject>Escherichia coli</subject><subject>Fluorescence</subject><subject>Fluorescence Resonance Energy Transfer</subject><subject>Gene Products, gag - chemistry</subject><subject>Genetic aspects</subject><subject>Genetic 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By controlling the cellular localization of GFP fusion proteins, the engineered nanobody allows interrogation of their roles in basic biological processes, an approach that should be applicable to numerous previously described GFP fusions. We also outline how the binding affinities of other nanobodies can be controlled by small molecules.
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| subjects | 631/1647/338/469 631/61/338/552 631/92/469 Affinity Antibodies Binding Bioinformatics Biological activity Biological Microscopy Biological Techniques Biology Biomedical and Life Sciences Biomedical Engineering/Biotechnology Brief Communication Crystallography, X-Ray Databases, Protein Dihydrofolate reductase DNA - chemistry Escherichia coli Fluorescence Fluorescence Resonance Energy Transfer Gene Products, gag - chemistry Genetic aspects Genetic engineering Genetic research Green fluorescent protein Green Fluorescent Proteins - chemistry Health aspects HEK293 Cells HeLa Cells HIV-1 - chemistry Humans Immunoglobulin Fragments - chemistry Interrogation Kinetics Life Sciences Ligands Localization Medical research Medicine, Experimental Microscopy, Fluorescence Mitosis Nanobodies Nanomedicine Nanoparticles - chemistry nef Gene Products, Human Immunodeficiency Virus - chemistry Physiological aspects Protein Domains Proteins Proteomics Single-Domain Antibodies - chemistry Viral antibodies |
| title | Chemogenetic Control of Nanobodies |
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