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Updated: Jan 23, 2026

Label-Free Quantitative Proteomics Workflow for Discovery-Driven Host-Pathogen Interactions
Published on: October 20, 2020
Decoding the host-pathogen proteomic dialogue using surface labeling tools
Oceane Dubois1, Abdelrahim Zoued1
1CIRI, Centre International de Recherche en Infectiologie, CNRS UMR5308, Inserm U1111, Université Claude Bernard Lyon 1, ENS de Lyon, France.
Abstract:
Understanding molecular interactions at the host-pathogen interface is essential to decipher infection mechanisms and develop new therapies. Bacterial surface proteins and host-derived bacterial binding proteins (HBBPs) govern colonization, adhesion, and immune modulation, but are difficult to study due to low abundance and transient interactions. Advances in chemical biology and proteomics now enable high-resolution mapping of these dynamic surfaces. Techniques such as bioorthogonal labeling, photo-crosslinking, click chemistry, and enzymatic proximity labeling expand our ability to identify surface-exposed and transient complexes. Combined with mass spectrometry and bioinformatics, they offer an integrated view of host-microbe crosstalk, revealing novel virulence factors and antigenic targets. This review highlights innovative labeling strategies advancing infection biology and immune recognition.
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