摘要：SummaryToxoplasma gondiisurface antigen 1 (TgSAG1) is a surface protein of tachyzoites, which plays a crucial role intoxoplasma gondiiinfection and host cell immune regulation. However, howTgSAG1 regulates these processes remains elucidated. We utilized the biotin ligase -TurboID fusion withTgSAG1 to identify the host proteins interacting withTgSAG1, and identified that S100A6 was co-localized withTgSAG1 whenT. gondiiattached to the host cell. S100A6, either knocking down or blocking its functional epitopes resulted in inhibited parasites invasion. Meanwhile, S100A6 overexpression in host cells promotedT. gondiiinfection. We further verified thatTgSAG1 could inhibit the interaction of host cell vimentin with S100A6 for cytoskeleton organization duringT. gondiiinvasion. As an immunogen,TgSAG1 could promote the secretion of tumor necrosis factor alpha (TNF-α) through S100A6-Vimentin/PKCθ-NF-κB signaling pathway. In summary, our findings revealed a mechanism for howTgSAG1 functioned in parasitic invasion and host immune regulation.Graphical abstractDisplay OmittedHighlights•TgSAG1 interacts with host protein S100A6 then regulatesT. gondiiinfection•TgSAG1 could regulate binding vimentin with S100A6 duringT. gondiiinfection•TgSAG1 regulate TNFα secretion through S100A6-vimentin/PKCθ-NF-κB signaling pathwayMolecular biology; Immune response; Parasitology
