A Pattern-recognition Protein for β-1,3-Glucan
By M. Ochiai, M. Ashida. Journal of Biological Chemistry, 2000
196 citations recorded by the source corpus.
The β-1,3-glucan recognition protein (βGRP) has strong specific affinity for β-1,3-glucan, a component of the fungal cell wall. Its interaction with β-1,3-glucan initiates the activation of the prophenoloxidase cascade, which is an important defense system in invertebrates of many species. We cloned the cDNA of the βGRP of the silkworm Bombyx mori. The βGRP mRNA transcript was constitutively expressed in the hemocytes, fat body, and epithelial cells of the naive silkworm. At the same time, a bacterial or yeast challenge was indicated to intensify the transcription. Comparison of the deduced amino acid sequence with known sequences revealed that the βGRP contained a region (Thr264 to Pro386) displaying significant similarity to the catalytic regions of bacterial β-1,3-glucanases and much higher similarity to the glucanase-like regions of Gram-negative bacteria-binding proteins found in the silkworm B. moriand the mosquito Anopheles gambiae. The region (Thr264 to Pro386) of the βGRP, however, was demonstrated not to have appreciable affinity for β-1,3-glucan. A recombinant peptide corresponding to an N-terminal region (Tyr1 to Ala102) of the βGRP bound strongly to β-1,3-glucan. These results indicate that the binding domain of the βGRP for β-1,3-glucan is located in the N-terminal region. Glucanases and the current pattern-recognition proteins that contain a glucanase-like region seem to have a common origin in their molecular evolution.
Subfields: Biotechnology, Nutrition and Dietetics, Plant Science
View Paper: https://www.semanticscholar.org/paper/0379247233ee946ee82b8fabec2e426e480cc1ae
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Citations in the corpus
- The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections (2007, background): “, and by GNBP1 , a member of the Gram-negative binding proteins (GNBPs; also known as β-glucan recognition proteins (βGRP)) famil”
- Eicosanoid actions in insect cellular immune functions (2006, background): “Interaction between laminarin and β (1-3)-glucan pattern recognition proteins launches prophenoloxidase (proPO) activation and cellular immune responses in insects (Ochiai & Ashida, 2000; Wang et al., 2005).”
- The immune response of Drosophila (2003, background): “GNBPs are 50-kDa proteins with a C-terminal, 200-residue β-glucanase-like domain and an N-terminal, 100-residue domain reported to bind β-(1,3)-gluca”