A proteome-wide XL-MS map of Toxoplasma (29,624 crosslinked pairs, 2,859 interactions) plus structure models turns up new essential-complex members, including an apicomplexan-specific ATP-synthase alpha in a structurally distinct subcomplex required for fitness. Core mitochondrial machinery diversified, and that is a drug-shaped hole.
Mito.news · at a glance
OXPHOS · infection · structural biology
Editorial signal profile from the abstract (importance score, mito keywords, dysfunction tags, evidence density, translational cues). Not a figure reproduced from the preprint PDF.
Finding. Butterworth, Lourido, Sheiner and colleagues crosslink the Toxoplasma proteome (29,624 pairs, 2,859 interactions) and model the contacts. Among new essential-complex parts is a structurally odd ATP-synthase subcomplex whose alpha subunit is apicomplexan-specific and required for fitness. Mitochondrial core machines in this parasite are not just smaller. They are rebuilt.
Score 84. Pathogen ATP synthase, essential, interactome-scale. High confidence for the fitness claim as stated.
Free HTML is above. Bots pay for JSON at /api/v1/papers/10-64898-2026-09-01-748362. Optional wallet tester: MetaMask ($0.005).
Proteome-wide crosslinking mass spectrometry reveals novel components of essential complexes in Toxoplasma
10.64898/2026.09.01.748362
Butterworth S, Gin AL, Shikha S, Tengganu I, Rush J, Duraisingh T, Sodeinde V, Lemgruber L, Schulte F, Hu K, Sheiner L, Ovchinnikov S, Lourido S.
