Journal
JOURNAL OF INNATE IMMUNITY
Volume 7, Issue 1, Pages 37-46Publisher
KARGER
DOI: 10.1159/000365112
Keywords
Drosophila; Innate immunity; Innate immune receptor; Innate immune signalling; Imd; Nonaspanins; Plasma membrane receptor; Phagocytosis; Transmembrane 9 proteins
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Funding
- Fondation ARC
- Region Rhone-Alpes
- FINOVI foundation
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Transmembrane 9 (TM9) proteins, or nonaspanins, are a family of proteins conserved throughout evolution and characterized by 9 transmembrane domains. In Drosophila, TM9 superfamily protein member 4 (TM9SF4) and its closest paralogue, TM9SF2, contribute to phagocytosis of various types of particles, while TM9SF4 displays non-redundant requirement in Gram-negative bacteria engulfment. In addition, the two TM9 proteins control the actin cytoskeleton in larval haemocytes and in Drosophila S2 cells. Here, we show that TM9SF4 and TM9SF2 co-immunoprecipitate with the peptidoglycan recognition protein (PGRP)-LC, which triggers the Drosophila immune response to bacterial infection. Furthermore, both TM9 proteins co-localize with this receptor in intracellular vesicles and at the plasma membrane in Drosophila S2 cells in culture and in the fly fat body. Silencing TM9SF4 prevents plasma membrane localization of PGRP-LC, whereas silencing TM9SF2 does not, which may account for the non- redundant role of TM9SF4 in phagocytosis of Gramnegative bacteria. Finally, we provide a set of data suggesting that TM9 proteins can prevent inappropriate signalling from the unstimulated receptor. (C) 2014 S. Karger AG, Basel
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