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The spleen is the central organ for clearance of infected red blood cells and regulation of immunity, yet paradoxically also serves as a site of parasite sequestration. Splenic fibroblasts may contribute to this process through adhesion mechanisms, but their role remains poorly defined. This study investigated P. yoelii tryptophan-rich antigen 7 (PyTRAg7), a member of the TRAg protein family, in splenic parasite\u2013host interactions. TRAgs constitute a conserved protein family present in multiple Plasmodium species, including human malaria parasites, suggesting the relevance of PyTRAg7-associated mechanisms to human infection. Using protein binding assays and gene-edited parasites, PyTRAg7 was shown to interact with vimentin on mouse splenic fibroblasts, activating NF-\u03baB p65 signaling and increasing ICAM-1 and integrin \u03b21 expression. Deletion of PyTRAg7 reduced infected red blood cells adhesion to mouse splenic fibroblasts, lowered splenic parasite burden, delayed parasitemia onset, and prolonged host survival. Histological analysis showed preserved splenic architecture and reduced hemozoin deposition in the absence of PyTRAg7. The murine P. yoelii model was used due to its genetic tractability and its suitability for dissecting spleen-dependent sequestration mechanisms not easily studied in human malaria parasites. These findings identify PyTRAg7 as a key mediator of fibroblast\u2013parasite interactions that promote cytoadherence and splenic remodeling, offering a potential target for malaria intervention.<\/jats:p>","DOI":"10.3347\/phd.25086","type":"journal-article","created":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T00:50:46Z","timestamp":1777337446000},"page":"141-152","update-policy":"https:\/\/doi.org\/10.3347\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Plasmodium yoelii tryptophan-rich antigen 7 mediates infected erythrocyte adhesion to splenic fibroblasts via binding to 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