Source 1primary paper2022
Toolkit/antiGFP nanobody
antiGFP nanobody
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The antiGFP nanobody is used as a targeting domain in an iLID fusion to localize the light-inducible iLID module to GFP-tagged proteins. In this configuration, blue-light illumination induces iLID-SspB heterodimerization while recruitment remains efficient at the GFP-labeled target.
Usefulness & Problems
Why this is useful
This targeting strategy enables light-controlled recruitment to proteins that are already GFP tagged. It is useful because it increases experimental flexibility without requiring direct engineering of the iLID target protein beyond the existing GFP tag.
Problem solved
It addresses the problem of how to position the iLID optogenetic module at a chosen intracellular target when that target is available as a GFP fusion rather than as a bespoke iLID fusion partner. The reported solution is to fuse iLID to an antiGFP nanobody so that recruitment can be directed to GFP-tagged proteins.
Problem links
Need inducible protein relocalization or recruitment
DerivedThe antiGFP nanobody is used as a targeting domain by fusion to iLID, allowing iLID localization to GFP-tagged proteins. In this configuration, blue-light illumination drives iLID–SspB heterodimerization while preserving efficient light-dependent recruitment at the GFP-labeled target.
Need precise spatiotemporal control with light input
DerivedThe antiGFP nanobody is used as a targeting domain by fusion to iLID, allowing iLID localization to GFP-tagged proteins. In this configuration, blue-light illumination drives iLID–SspB heterodimerization while preserving efficient light-dependent recruitment at the GFP-labeled target.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
gfp bindinggfp bindinggfp bindinglight-induced heterodimerizationlight-induced heterodimerizationlight-induced heterodimerizationTechniques
No technique tags yet.
Target processes
localizationInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: actuatoroperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment
The described construct design is a fusion of an antiGFP nanobody to iLID. Operation depends on a GFP-tagged target protein and blue-light activation of the iLID-SspB interaction; no additional expression, delivery, or cofactor details are provided in the supplied evidence.
The supplied evidence only supports use of the antiGFP nanobody as part of an iLID fusion for recruitment to GFP-tagged proteins. No quantitative binding, kinetic, spectral, organism-specific, or independent validation data are provided here for the nanobody alone or for broader applications.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug antigfp-nanobody
we fuse an antiGFP nanobody to the iLID
Source:
functional compatibilitysupports
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
Source:
targeting functionsupports
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
Source:
Comparisons
Source-backed strengths
The reported configuration preserves efficient light-dependent recruitment of SspB when iLID is targeted through the antiGFP nanobody to a GFP-tagged protein. A stated advantage is increased flexibility for recruitment experiments at GFP-labeled targets.
Compared with BcLOV4 photoreceptor
antiGFP nanobody and BcLOV4 photoreceptor address a similar problem space because they share localization.
Shared frame: same top-level item type; shared target processes: localization; same primary input modality: light
Compared with CIB1
antiGFP nanobody and CIB1 address a similar problem space because they share localization.
Shared frame: same top-level item type; shared target processes: localization; shared mechanisms: light-induced heterodimerization
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with SspB
antiGFP nanobody and SspB address a similar problem space because they share localization.
Shared frame: same top-level item type; shared target processes: localization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
- 1.