Addendum: Biotinylation by antibody recognition—a method for proximity labeling

Bar, Daniel; Atkatsh, Kathleen; Tavarez, Urraca; Erdos, Michael R.; Gruenbaum, Yosef; Collins, Francis S.

doi:10.1038/s41592-018-0073-4

Cited by 6 publications

(6 citation statements)

References 4 publications

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“…1) (12). These elegant strategies have primarily been applied to the proteomic profiling and imaging of larger protein architectures such as mitochondria, lipid droplets, and nuclear pores (13)(14)(15) as well as regions such as synaptic clefts (16), lipid rafts (9), nuclear lamina (17,18), and protein clusters (19,20).…”

mentioning

confidence: 99%

Microenvironment mapping via Dexter energy transfer on immune cells

Geri

Oakley

Reyes‐Robles

et al. 2020

Science

276

278

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Many disease pathologies can be understood through the elucidation of localized biomolecular networks, or microenvironments. To this end, enzymatic proximity labeling platforms are broadly applied for mapping the wider spatial relationships in subcellular architectures. However, technologies that can map microenvironments with higher precision have long been sought. Here, we describe a microenvironment-mapping platform that exploits photocatalytic carbene generation to selectively identify protein-protein interactions on cell membranes, an approach we term MicroMap (μMap). By using a photocatalyst-antibody conjugate to spatially localize carbene generation, we demonstrate selective labeling of antibody binding targets and their microenvironment protein neighbors. This technique identified the constituent proteins of the programmed-death ligand 1 (PD-L1) microenvironment in live lymphocytes and selectively labeled within an immunosynaptic junction.

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mentioning

confidence: 99%

Microenvironment mapping via Dexter energy transfer on immune cells

Geri

Oakley

Reyes‐Robles

et al. 2020

Science

276

278

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“…The proximity labeling method ( 16 , 17 , 18 , 19 ) has recently been used to analyze the physiological protein interactions. We developed a simple physiological method, termed E nzyme- M ediated A ctivation of R adical S ource (EMARS) ( 20 ), that uses horseradish peroxidase (HRP)-induced radicals derived from arylazide or tyramide compounds ( 21 ).…”

Section: Introductionmentioning

confidence: 99%

Host cell membrane proteins located near SARS-CoV-2 spike protein attachment sites are identified using proximity labeling and proteomic analysis

Kotani¹,

Nakano²,

Kuwahara³

2022

Journal of Biological Chemistry

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“…The proximity labeling method (16)(17)(18)(19) has recently been used to analyze the physiological protein interactions. We developed a simple physiological method, termed Enzyme-Mediated Activation of Radical Source (EMARS) (20), that uses horseradish peroxidase (HRP)-induced radicals derived from arylazide or tyramide compounds (21).…”

Section: Introductionmentioning

confidence: 99%

Screening of candidate host cell membrane proteins involved in SARS-CoV-2 entry

Kotani

Nakano

2020

Preprint

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COVID-19 represents a real threat to the global population, and understanding the biological features of the causative virus (SARS-CoV-2) is imperative to aid in mitigating this threat. Analyses of proteins such as primary receptors and co-receptors (co-factors) that are involved in SARS-CoV-2 entry into host cells will provide important clues to help control the virus. Here, we identified host cell membrane protein candidates that were present in proximity to the attachment sites of SARS-CoV-2 spike proteins through the use of proximity labeling and proteomics analysis. The identified proteins represent candidate key factors that may be required for viral entry. Our results indicated that a number of membrane proteins, including DPP4, Cadherin-17, and CD133, were identified to co-localize with cell membrane-bound SARS-CoV-2 spike proteins in Caco-2 cells that were used to expand the SARS-CoV-2 virion. We anticipate that the information regarding these protein candidates will be utilized for the future development of vaccines and antiviral agents against SARS-CoV-2.

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Addendum: Biotinylation by antibody recognition—a method for proximity labeling

Cited by 6 publications

References 4 publications

Microenvironment mapping via Dexter energy transfer on immune cells

Microenvironment mapping via Dexter energy transfer on immune cells

Host cell membrane proteins located near SARS-CoV-2 spike protein attachment sites are identified using proximity labeling and proteomic analysis

Screening of candidate host cell membrane proteins involved in SARS-CoV-2 entry

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