A horseshoe crab receptor structurally related to Drosophila Toll
Open Access
- 1 October 2000
- journal article
- other
- Published by SAGE Publications in Innate Immunity
- Vol. 6 (5) , 397-399
- https://doi.org/10.1177/09680519000060051201
Abstract
Innate immunity against microbial pathogens relies on the pattern recognition of cell wall components on invading microbes. Recent evidence has shown that a mammalian Toll-like receptor (TLR) is activated by bacterial lipopolysaccharides (LPS). The innate immunity in invertebrates is also triggered by LPS, as seen in the hemolymph coagulation in horseshoe crab. We report the cloning of a TLR from the Japanese horseshoe crab Tachypleus tridentatus. A cDNA coding for Tachypleus Toll was isolated from a hemocyte cDNA library and the open reading frame codes for a proprotein including a signal sequence. Like Drosophila Toll, Tachypleus Toll is a type I transmembrane protein with an extracellular domain consisting of two leucine-rich repeats flanked by two cystein-rich clusters and a cytoplasmic domain exhibiting striking similarity with the cytoplasmic domain of interleukin-1 receptor. Tachypleus Toll is most similar to Drosophila Toll in the domain architecture and the overall length.Keywords
This publication has 18 references indexed in Scilit:
- Phylogenetic Perspectives in Innate ImmunityScience, 1999
- Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signallingNature, 1998
- Getting knotted: a model for the structure and activation of SpätzleTrends in Biochemical Sciences, 1998
- A human homologue of the Drosophila Toll protein signals activation of adaptive immunityNature, 1997
- A CONSERVED SIGNALING PATHWAY: The Drosophila Toll-Dorsal PathwayAnnual Review of Cell and Developmental Biology, 1996
- The Dorsoventral Regulatory Gene Cassette spätzle/Toll/cactus Controls the Potent Antifungal Response in Drosophila AdultsCell, 1996
- The Instructive Role of Innate Immunity in the Acquired Immune ResponseScience, 1996
- Ventralizing signal determined by protease activation in Drosophila embryogenesisNature, 1994
- A common domain within the proenzyme regions of the drosophila snake and easter proteins and tachypleus proclotting enzyme defines a new subfamily of serine proteasesProtein Science, 1992
- Information for the dorsal–ventral pattern of the Drosophila embryo is stored as maternal mRNANature, 1984