Proximity labeling approaches to study protein complexes during virus infection

Area of Science:

• Cellular and Molecular Biology
• Infection Biology
• Proteomics

Background:

• Cellular compartmentalization and protein complex formation are key to biological process control.
• Understanding protein localization and interactions is vital for elucidating protein function.
• Traditional methods face challenges in studying certain protein complexes, like transmembrane proteins.

Purpose of the Study:

• To introduce proximity labeling (PL) enzymes and recent advancements in the field.
• To summarize achievements in organelle mapping and nucleic acid PL.
• To comprehensively review host-pathogen interaction research using PL, with a focus on virology.

Main Methods:

• Proximity labeling (PL) utilizes genetically modified enzymes to covalently label proteins in close proximity.
• Fusion of PL enzymes to antibodies or 'bait' proteins.
• Affinity enrichment mass spectrometry (AE-MS) for isolation and identification of the proximity proteome ('proxisome').

Main Results:

• PL has reshaped cellular proteomics, particularly in infection biology.
• PL is effective for mapping membrane and membraneless organelles.
• PL facilitates the study of challenging protein complexes and host-pathogen interactions.

Conclusions:

• Proximity labeling is a powerful methodology for uncovering protein functions and interactions.
• PL offers significant potential for advancing infection biology research, especially in virology.
• Continued advancements in PL promise broader applications in cellular and molecular studies.