ArticleClinical proteomics2023
sBioSITe enables sensitive identification of the cell surface proteome through direct enrichment of biotinylated peptides.
Article in Clinical proteomics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Cell surface oncofetal antigens in prostate cancer: therapeutic potential and radioligand targeting.EJNMMI research · 2026Review
- Optimization of Methods for the Quantitative Analysis of Global Cell Surface Proteome and Cell Surface Polarization.International journal of molecular sciences · 2025Article
- Proteomics-Based Approaches to Decipher the Molecular Strategies ofJournal of fungi (Basel, Switzerland) · 2025Review
- A Straightforward Interpretation of Proximity Labeling through Direct Biotinylation Analysis.ACS omega · 2025Article
- Mapping the cancer surface proteome in search of target antigens for immunotherapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Review
- Improved elution strategy and new monoclonal anti-biotin antibody for LC-MS/MS characterization of protein biotinylation sites.Biochemistry and biophysics reports · 2024Article
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundCell surface proteins perform critical functions related to immune response, signal transduction, cell-cell interactions, and cell migration. Expression of specific cell surface proteins can determine cell-type identity, and can be altered in diseases including infections, cancer and genetic disorders. Identification of the cell surface proteome remains a challenge despite several enrichment methods exploiting their biochemical and biophysical properties.
methodsHere, we report a novel method for enrichment of proteins localized to cell surface. We developed this new approach designated surface Biotinylation Site Identification Technology (sBioSITe) by adapting our previously published method for direct identification of biotinylated peptides. In this strategy, the primary amine groups of lysines on proteins on the surface of live cells are first labeled with biotin, and subsequently, biotinylated peptides are enriched by anti-biotin antibodies and analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS).
resultsBy direct detection of biotinylated lysines from PC-3, a prostate cancer cell line, using sBioSITe, we identified 5851 peptides biotinylated on the cell surface that were derived from 1409 proteins. Of these proteins, 533 were previously shown or predicted to be localized to the cell surface or secreted extracellularly. Several of the identified cell surface markers have known associations with prostate cancer and metastasis including CD59, 4F2 cell-surface antigen heavy chain (SLC3A2) and adhesion G protein-coupled receptor E5 (CD97). Importantly, we identified several biotinylated peptides derived from plectin and nucleolin, both of which are not annotated in surface proteome databases but have been shown to have aberrant surface localization in certain cancers highlighting the utility of this method.
conclusionsDetection of biotinylation sites on cell surface proteins using sBioSITe provides a reliable method for identifying cell surface proteins. This strategy complements existing methods for detection of cell surface expressed proteins especially in discovery-based proteomics approaches.
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