Proximity labeling approaches to study protein complexes during virus infection

Zapatero-Belinchón, Francisco José; Carriquí-Madroñal, Belén

doi:10.1016/bs.aivir.2021.02.001

Cited by 5 publications

(1 citation statement)

References 190 publications

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“…Cellular receptors are important targets for antiviral strategies, and the discovery and identification of functional virus receptors is essential for a better understanding of the virus entry mechanism and the prevention and control of viral diseases. Currently, the most commonly used method for virus receptor identification is affinity purification coupled to mass spectrometry (AP-MS) ( Zapatero-Belinchón et al., 2021 ), which has been used to identify the key receptors of a variety of important viruses, such as the receptor sodium taurocholate co-transporting polypeptide (NTCP) of hepatitis B and D viruses ( Yan et al., 2012 ), the receptor neural cell adhesion molecule NCAM1 of Zika virus ( Srivastava et al., 2020 ), and the SARS-CoV-2 receptor AXL identified by Wang et al ( Wang et al., 2021 ). AP-MS typically requires stable interactions, but some non-specifically bound proteins will inevitably be purified during the purification process.…”

Section: Discussionmentioning

confidence: 99%

TurboID-mediated proximity labeling technologies to identify virus co-receptors

Wang,

Yang,

Wang

et al. 2024

Front. Cell. Infect. Microbiol.

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Virus receptors determine the tissue tropism of viruses and have a certain relationship with the clinical outcomes caused by viral infection, which is of great importance for the identification of virus receptors to understand the infection mechanism of viruses and to develop entry inhibitor. Proximity labeling (PL) is a new technique for studying protein-protein interactions, but it has not yet been applied to the identification of virus receptors or co-receptors. Here, we attempt to identify co-receptor of SARS-CoV-2 by employing TurboID-catalyzed PL. The membrane protein angiotensin-converting enzyme 2 (ACE2) was employed as a bait and conjugated to TurboID, and a A549 cell line with stable expression of ACE2-TurboID was constructed. SARS-CoV-2 pseudovirus were incubated with ACE2-TurboID stably expressed cell lines in the presence of biotin and ATP, which could initiate the catalytic activity of TurboID and tag adjacent endogenous proteins with biotin. Subsequently, the biotinylated proteins were harvested and identified by mass spectrometry. We identified a membrane protein, AXL, that has been functionally shown to mediate SARS-CoV-2 entry into host cells. Our data suggest that PL could be used to identify co-receptors for virus entry.

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Section: Discussionmentioning

confidence: 99%

TurboID-mediated proximity labeling technologies to identify virus co-receptors

Wang,

Yang,

Wang

et al. 2024

Front. Cell. Infect. Microbiol.

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Profiling phagosome proteins identifies PD-L1 as a fungal-binding receptor

Li,

Chatterjee,

Qian

et al. 2024

Nature

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Cell surface protein–protein interaction profiling for biological network analysis and novel target discovery

Chen,

Fang,

et al. 2024

Life Medicine

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The secretome is composed of cell-surface membrane proteins and extracellular secreted proteins that are synthesized via secretory machinery, accounting for approximately one-third of human protein-encoding genes and playing central roles in cellular communication with the external environment. Secretome protein–protein interactions (SPPIs) mediate cell proliferation, apoptosis, and differentiation, as well as stimulus/cell-specific responses that regulate diverse range of biological processes. Aberrant SPPIs are associated with diseases including cancer, immune disorders, and illness caused by infectious pathogens. Identifying the receptor/ligand for a secretome protein or pathogen can be a challenging task, and many SPPIs remain obscure, with a large number of orphan receptors and ligands, as well as viruses with unknown host receptors, populating the SPPI network. In addition, proteins with known receptors/ligands may also interact with alternative uncharacterized partners and exert context-dependent effects. In the past few decades, multiple varied approaches have been developed to identify SPPIs, and these methods have broad applications in both basic and translational research. Here, we review and discuss the technologies for SPPI profiling and the application of these technologies in identifying novel targets for immunotherapy and anti-infectious agents.

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Proximity labeling approaches to study protein complexes during virus infection

Cited by 5 publications

References 190 publications

TurboID-mediated proximity labeling technologies to identify virus co-receptors

TurboID-mediated proximity labeling technologies to identify virus co-receptors

Profiling phagosome proteins identifies PD-L1 as a fungal-binding receptor

Cell surface protein–protein interaction profiling for biological network analysis and novel target discovery

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