Distinct nanoscale membrane organizations of mucins and trans-sialidases in Trypanosoma cruzi
Escalante, G.; Parada-Puig, R.; Lopez, L. F.; Szalai, A. M.; Camara, M. d. l. M.; Masullo, L. A.; Campetella, O. E.; Mucci, J.; Stefani, F. D.
Show abstract
Trypanosoma cruzi, the causative agent of Chagas disease, relies on surface sialylation to evade host immunity and invade cells. This process is mediated by trans-sialidases (TS) and mucins--an enzyme-substrate pair anchored to distinct lipid environments--yet how these molecules are organized at the nanoscale has remained unknown. Using dual-color super- resolution microscopy, we show that [~]60% of mucins and TS are segregated into nanoclusters ([~]100 nm) that rarely contact each other, indicating that these abundant domains are unlikely to serve as primary sites of sialylation. In contrast, the [~]40% fraction of non-clustered mucins and TS exhibit significantly shorter than random separation distances, consistent with organization on a shared fibrillar network. This architecture positions non-clustered molecules within proximity compatible with catalytic activity, revealing a previously unrecognized spatial pathway for sialylation. Together, these findings uncover fundamental principles of T. cruzi surface organization with important implications for the regulation of host-parasite interactions.
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