Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 23, Pages 7237-7242Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1505924112
Keywords
DEC205; pH dependence; apoptosis; cryoEM; mannose receptor family
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Funding
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDB08020102]
- National Natural Science Foundation of China [31270772]
- One Hundred Talents Program of the Chinese Academy of Sciences [2012OHTP03]
- Shanghai Pujiang Program [13PJ1409700]
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Dendritic cells play important roles in regulating innate and adaptive immune responses. DEC205 (CD205) is one of the major endocytotic receptors on dendritic cells and has been widely used for vaccine generation against viruses and tumors. However, little is known about its structure and functional mechanism. Here we determine the structure of the human DEC205 ectodomain by cryoelectron microscopy. The structure shows that the 12 extracellular domains form a compact double ring-shaped conformation at acidic pH and become extended at basic pH. Biochemical data indicate that the pH-dependent conformational change of DEC205 is correlated with ligand binding and release. DEC205 only binds to apoptotic and necrotic cells at acidic pH, whereas live cells cannot be recognized by DEC205 at either acidic or basic conditions. These results suggest that DEC205 is an immune receptor that recognizes apoptotic and necrotic cells specifically through a pH-dependent mechanism.
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