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

Authors

Zhe Yan, Ruirui Li, Jiayin Liang, Guangyan Wang, Fei Wang, Chuangfu Chen, Hui Zhang, Zhongchen Ma, Yong Wang

Published in

International journal of biological macromolecules. Pages 154735. Oct 05, 2026. Epub Oct 05, 2026.

Abstract

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.

PMID:
42833323
Bibliographic data and abstract were imported from PubMed on 06 Oct 2026.

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