Proteome-wide crosslinking mass spectrometry reveals novel components of essential complexes in Toxoplasma
Protein-protein interactions underpin nearly all cellular processes, yet systematic definition of these networks remains limited outside a few model organisms. As a result, the architectures of essential complexes in many divergent lineages remain poorly characterized. Here we developed a high-coverage crosslinking mass spectrometry framework to map the proteome-wide interactome of the model…
A new study employs a comprehensive crosslinking mass spectrometry approach to map the entire interactome of the apicomplexan parasite Toxoplasma gondii at the proteome level. By analyzing 29,624 crosslinked peptide pairs, researchers have uncovered a network of 2,859 protein-protein interactions. Integrating these findings with structural modeling, they were able to pinpoint interaction interfaces, offering valuable insights into the parasite's molecular architecture.
The investigation revealed previously unrecognized components within essential protein complexes, such as a structurally unique ATP synthase subcomplex. This subcomplex contains a highly divergent, apicomplexan-specific subunit that is essential for the parasite's survival. The study not only highlights the unexpected diversification of core mitochondrial machinery but also presents a general strategy for defining the molecular architecture of diverse organisms.
This novel resource serves as a foundation for generating hypotheses, inferring protein structures, and identifying unique vulnerabilities in pathogen biology, potentially paving the way for the development of targeted therapies against Toxoplasma gondii and other apicomplexan parasites.
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