---
title: "TurboID-based proximity labelling detects extracellular protein interactions in the plant apoplast"
id: "biorxiv-15-a-turboid-based-proximity-labelling-method-for-detecting-extracellular-protein"
canonical_url: "https://medichelpline.com/clinical-feed/biorxiv-15-a-turboid-based-proximity-labelling-method-for-detecting-extracellular-protein"
content_type: "clinical_feed_article"
specialty: "General"
source_name: "bioRxiv (Biomedical Preprints)"
source_url: "https://www.biorxiv.org/content/10.64898/2026.09.22.753433v1?rss=1"
published_at: "2026-09-23T09:50:14.000Z"
evidence_level: "Verified Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# TurboID-based proximity labelling detects extracellular protein interactions in the plant apoplast
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/biorxiv-15-a-turboid-based-proximity-labelling-method-for-detecting-extracellular-protein
- **Specialty:** [General](https://medichelpline.com/clinical-feed/general.md)
- **Primary Source:** bioRxiv (Biomedical Preprints)
- **Source URL:** [Original Journal Publication](https://www.biorxiv.org/content/10.64898/2026.09.22.753433v1?rss=1)
- **Published At:** 2026-09-23T09:50:14.000Z
- **Evidence Rating:** Verified Feed
## Executive GIST (TL;DR)
- The apoplast is a key extracellular compartment where plant–pathogen interactions and perception of secreted effectors by cell-surface immune receptors occur, but its harsh environment makes protein interaction studies difficult. - **TurboID-based proximity labelling (PL)** has been effective for intracellular protein interaction mapping in plants; this study adapts TurboID for use in the leaf apoplast. - The authors engineered secreted TurboID fusion constructs: SP-INF1-TurboID (INF1-T) and SP-eGFP-TurboID (eGFP-T) for use in Nicotiana benthamiana. - Transient expression of INF1-T triggered a cell death response similar to native INF1, indicating that fusion to TurboID did not block recognition by the receptor-like protein **REL**. - Both INF1-T and eGFP-T were confirmed to localise to the apoplast, validating their suitability for extracellular PL experiments. - Effective TurboID-mediated biotinylation in the apoplast required co-infiltration of exogenous **biotin**, **ATP**, and **magnesium acetate** to support enzyme activity in the extracellular compartment. - Streptavidin-HRP immunoblotting revealed different biotinylation patterns for INF1-T and eGFP-T, consistent with distinct proximal protein environments. - Co-immunoprecipitation experiments showed specific biotinylation of **REL** by INF1-T but not by eGFP-T across wild-type, bak1, and sobir1/sobir1-like N. benthamiana backgrounds. - The results provide a proof-of-concept that TurboID-based PL is functional in the apoplast and can detect elicitor–receptor interactions extracellularly. - The article is a preprint and has not undergone peer review; competing interests were declared as none. Details beyond these reported results (e.g., quantitative metrics, full experimental parameters) were not reported in the source abstract.
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Abdelrahman M Qutb 1 School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, United Kingdom; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Abdelrahman%2BM%2BQutb%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Qutb%20AM&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AAbdelrahman%2BM%2BQutb%2B) * [ORCID record for Abdelrahman M Qutb](http://orcid.org/0000-0003-1779-8015 "Open in new tab") Camille-Madeleine Szymansky 2 The Sainsbury Laboratory, Norwich Research Park, Norwich, NR4 7UH, United Kingdom * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Camille-Madeleine%2BSzymansky%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Szymansky%20C&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3ACamille-Madeleine%2BSzymansky%2B) * [ORCID record for Camille-Madeleine Szymansky](http://orcid.org/0000-0001-8338-721X "Open in new tab") Graeme J Kettles 1 School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, United Kingdom; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Graeme%2BJ%2BKettles%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Kettles%20GJ&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AGraeme%2BJ%2BKettles%2B) * [ORCID record for Graeme J Kettles](http://orcid.org/0000-0003-1230-9024 "Open in new tab") * For correspondence: g.j.kettles@bham.ac.uk * [Abstract](https://www.biorxiv.org/content/10.64898/2026.09.22.753433v1)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_art/node:5802702/1) * [Info/History](https://www.biorxiv.org/content/10.64898/2026.09.22.753433v1.article-info)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_info/node:5802702/1) * [Metrics](https://www.biorxiv.org/content/10.64898/2026.09.22.753433v1.article-metrics)[](https://www.biorxiv.org/panels_ajax_tab/article_tab_metrics/node:5802702/1) * [Supplementary material](https://www.biorxiv.org/content/10.64898/2026.09.22.753433v1.supplementary-material)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_data/node:5802702/1) * [ Preview PDF](https://www.biorxiv.org/content/10.64898/2026.09.22.753433v1.full.pdf+html)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_pdf/node:5802702/1) ![Loading](https://www.biorxiv.org/sites/all/modules/contrib/panels_ajax_tab/images/loading.gif) ## Abstract The apoplast is a primary location for interactions between plants and invasive pathogens and is the site where many pathogen-secreted effectors are perceived by cell surface immune receptors to activate defence responses. However, our understanding of apoplastic interactions remains limited because protein interactions are difficult to investigate in this harsh extracellular environment. TurboID-based proximity labelling (PL) has emerged as a powerful approach for studying protein interactions in plants, though its application has to date been restricted to intracellular proteins. Here, we designed and validated a TurboID-based PL strategy for investigating protein interactions in the leaf apoplast using the well-characterised interaction between the Phytophthora infestans elicitor INF1 and the receptor-like protein (RLP) REL in Nicotiana benthamiana. Transient expression of SP-INF1-TurboID (INF1-T) induced a cell death (CD) response comparable to that triggered by native INF1, demonstrating that fusion of the TurboID tag did not impair INF1 recognition by REL. Apoplastic localisation of both INF1-T and the control construct SP-eGFP-TurboID (eGFP-T) was confirmed, validating their suitability for PL experiments. Efficient TurboID-mediated biotinylation was achieved in the apoplast using co-infiltration of biotin, ATP and magnesium acetate. Streptavidin-HRP immunoblotting revealed distinct biotinylation profiles for INF1-T and eGFP-T. Furthermore, co-immunoprecipitation demonstrated specific biotinylation of REL by INF1-T, but not by eGFP-T, in wild-type, bak1 and sobir1/sobir1-like N. benthamiana. These findings demonstrate that TurboID-based PL is functional in the apoplast and provides a proof-of-concept for investigating elicitor-receptor interactions in this compartment. ### Competing Interest Statement The authors have declared no competing interest. Copyright The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a [CC-BY-NC 4.0 International license](http://creativecommons.org/licenses/by-nc/4.0/). bioRxiv and medRxiv thank the following for their generous financial support: > The Chan Zuckerberg Initiative, Cold Spring Harbor Laboratory, the Sergey Brin Family Foundation, California Institute of Technology, Centre National de la Recherche Scientifique, Fred Hutchinson Cancer Center, Imperial College London, Massachusetts Institute of Technology, Stanford University, The University of Edinburgh, University of Washington, and Vrije Universiteit Amsterdam. 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