Back

Nucleosides drive histiocytosis in SLC29A3 disorders by activating TLR7

Shibata, T.; Taoka, M.; Saitoh, S.-I.; Yamauchi, Y.; Motoi, Y.; Komine, M.; Fujita, E.; Sato, R.; Sagara, H.; Ichinohe, T.; Kawazoe, M.; Kato, C.; Furusho, K.; Murakami, Y.; Fukui, R.; Ohtsuki, M.; Ohto, U.; Shimizu, T.; Yoshida, N.; Isobe, T.; MIYAKE, K.

2019-12-16 immunology
10.1101/2019.12.16.877357 bioRxiv
Show abstract

A lysosomal transmembrane protein SLC29A3 transports nucleosides from lysosomes to the cytoplasm. Loss-of-function mutations of the SLC29A3 gene cause lysosomal nucleoside storage in monocyte/macrophages, leading to their accumulation called histiocytosis in humans and mice. Little is known, however, about a mechanism behind nucleoside-dependent histiocytosis. TLR7, an innate immune sensors for single stranded RNA, bind and respond to nucleosides. We here show that they drive nucleoside-mediated histiocytosis. Patrolling monocyte/macrophages accumulate in the spleen of Slc29a3-/- mice but not Slc29a3-/- Tlr7-/- mice. Accumulated patrolling monocyte/macrophages stored nucleosides derived from cell corpse. TLR7 was recruited to phagosomes and activated as evidenced by TLR7-dependent phagosomal maturation. TLR7 induced hyper-responsiveness to M-CSF in Slc29a3-/- monocyte/macrophages. These results suggest that TLR7 drives histiocytosis in SLC29A3 disorders. One Sentence SummarySLC29A3 disorders are caused by activation of TLR7 with accumulated nucleosides in lysosomes.

Matching journals

The top 6 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.