Development of conformation-selective antibodies targeting human SLC15A4
SLC15A4, an endolysosomal solute carrier family transporter, plays a critical role in TLR7/8/9-induced immune responses through assembling a complex with the downstream adaptor TASL in a conformation-dependent manner. Despite its close functional association and promising therapeutic potential in infections, tumors, and autoimmune diseases, the development of conformation-specific antibodies for human SLC15A4 (hSLC15A4) remains challenging. Here, using a systematic screening and validation approach, we identify a pair of conformation-selective antibodies, clones 107 and 235, targeting the endolysosomal lumen surface of hSLC15A4 with opposite conformation-regulatory activities. Specifically, clone 107 selectively binds to hSLC15A4 in a TASL binding-incompetent luminal-open state; whereas clone 235 stabilizes hSLC15A4 in a TASL binding-competent cytoplasmic-open state. Our research identifies antibodies that recognize distinct conformations of hSLC15A4, potentially enabling modulation of the TLR7/8/9 pathway and contributing to the development of targeted therapies and research tools selectively targeting hSLC15A4.
Authors
- Yalan Zhu
- Qixiang Zhang (ORCID: https://orcid.org/0000-0001-7879-171X)
- Songqin Liu (ORCID: https://orcid.org/0000-0002-4686-5291)
- Panpan Sun (ORCID: https://orcid.org/0000-0002-4993-6614)
- Yina Gao
- K. Liu (ORCID: https://orcid.org/0009-0002-2768-0088)
- Pu Gao (ORCID: https://orcid.org/0000-0002-5328-9755)
- Ang Gao (ORCID: https://orcid.org/0000-0001-8834-9781)
- Junxiao Ma (ORCID: https://orcid.org/0000-0003-3332-3001)
- Liwei Zhang
- Liguo Zhang (ORCID: https://orcid.org/0000-0002-9795-0314)
- Xuyuan Zhang (ORCID: https://orcid.org/0000-0002-6305-1556)
- Xiaohua Nie
- Yong Wang (ORCID: https://orcid.org/0000-0003-0695-5273)
Institutions
- Beijing Institute of Technology (CN)
- Chinese Academy of Sciences (CN)
- Institute of Biophysics (CN)
- Shandong First Medical University (CN)
- University of Chinese Academy of Sciences (CN)
- China Agricultural University (CN)
Publication Details
- Journal
- Nature Communications
- Published
- 2025-08-08
- DOI
- https://doi.org/10.1038/s41467-025-62759-x
- Primary Topic
- Glycosylation and Glycoproteins Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- Chinese Academy of Sciences
- China Postdoctoral Science Foundation
- Institute of Biophysics, Chinese Academy of Sciences