Abstract
Toxoplasma gondii surface antigen 1 (Tg SAG1) is a major surface antigen of tachyzoites, which plays a crucial role in host cell recognition, invasion, and immune regulation. However, how TgSAG1 regulate these processes has not been fully elucidated. We utilized the sensitive biotin ligase TurboID to identify host proteins interacting with TgSAG1. String database network analysis for the TgSAG1 interactome identified host S100 Calcium Binding Protein A6 (S100A6) as a hub-protein, which was co-localized with TgSAG1 when T. gondii attached to the host cell. S100A6 knocking down or blocking its epitopes resulted inhibited parasites attachment and invasion efficiency. On the contrary, S100A6 overexpression in host cells promoted T. gondii infection. We further found that TgSAG1 could inhibit the interaction of vimentin with S100A6 for cytoskeleton organization during T. gondii invasion. As an immunogen, TgSAG1 could promote the secretion of tumor necrosis factor α (TNF-α) through S100A6-Vimentin /PKCθ-NF-κB signaling pathway. In summary, our findings revealed a mechanism for how TgSAG1 functioned in parasitic invasion and host immune regulation.
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