Anaplasma phagocytophilum Ats-1 modulates host ER translocation-coupled N-glycosylation through SDCBP and SEC61A2

Anaplasma phagocytophilum remodels host-cell processes through secreted effectors, but whether it targets ER translocation-coupled N-glycosylation remains unclear. Here, we investigated the role of the effector Ats-1 in this pathway. Ats-1 associated with SEC61A2 and modulated the SEC61A2-associated ER translocation-N-glycosylation pathway in an SDCBP-dependent manner. Ats-1 increased the abundance of the OST-associated components RPN2 and DDOST and altered the N-glycosylation status of representative membrane glycoproteins, including integrin β1, CD63, and transferrin receptor (TfR). Perturbation of the SDCBP-SEC61A2 axis attenuated these effects and was accompanied by changes in UPR- and autophagy-related markers. Together, these findings define an SDCBP-dependent Ats-1-SEC61A2 regulatory framework linking ER protein translocation to OST-associated glycoprotein processing and provide a basis for testing its relevance during authentic A. phagocytophilum infection.