GRA9 is a Toxoplasma gondii dense granule protein that shapes the parasitophorous vacuole and cyst-wall environment and modulates host immunity during infection (PMID:15491588, PMID:31266861). After secretion from the anterior end of the parasite, GRA9 associates with the intravacuolar network (IVN) of tubular membranes, existing in both soluble and membrane-associated forms; its amphipathic and hydrophobic alpha-helices account for these dual solubility properties despite an overall hydrophilic character (PMID:15491588). During bradyzoite differentiation GRA9 dynamically redistributes to the cyst periphery and then into the inner layers of the maturing cyst wall, where it associates with cyst-wall components including the pseudokinase BPK1, and its loss slows the accumulation of cyst-wall proteins at the periphery (PMID:23291621, PMID:31619500). Consistent with this role, deletion of gra9 in type II strains causes severe chronic-stage cyst defects in vivo and impairs plaque formation, egress from the vacuole, and virulence, whereas the type I RH knockout instead shows an invasion defect, defining a strain-specific requirement (PMID:31266861, PMID:30849416). Beyond the parasite, the GRA9 C-terminal domain binds host NLRP3 through residue Q200 and blocks ASC recruitment to NLRP3, suppressing inflammasome assembly and promoting an anti-inflammatory M2 macrophage state (PMID:33182702).