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J Biol Chem, Vol. 273, Issue 38, 24948-24954, September 18, 1998

Identification and Cloning of a Glucan- and Lipopolysaccharide-binding Protein from Eisenia foetida Earthworm Involved in the Activation of Prophenoloxidase Cascade

Alain Beschin, Martin Bilej, Filip Hanssens, Jos Raymakersparallel , Els Van Dyck, Hilde Revets, Lea Brys, Julio Gomez, Patrick De Baetselier, and Miet Timmermans

From the Unit of Cellular Immunology, Flemish Interuniversity Institute for Biotechnology, VIB-VUB, Paardenstraat 65, B-1640 St-Genesius-Rode, Belgium, the  Department of Immunology, Institute of Microbiology, Academy of Sciences of the Czech Republic, Videnska 1083, 142 20 Prague 4, Czech Republic, and parallel  N. V. Innogenetics, Industriepark 7, B-9052 Zwijnaarde, Belgium

Coelomic fluid of Eisenia foetida earthworms contains a 42-kDa protein named coelomic cytolytic factor 1 (CCF-1) that was described previously to be involved in cytolytic, opsonizing, and hemolytic properties of the coelomic fluid. Cloning and sequencing of CCF-1 reveal significant homology with the putative catalytic region of beta -1,3- and beta -1,3-1,4-glucanases. CCF-1 also displays homology with coagulation factor G from Limulus polyphemus and with Gram-negative bacteria-binding protein of Bombyx mori silkworm, two proteins involved in invertebrate defense mechanisms. We show that CCF-1 efficiently binds both beta -1,3-glucan and lipopolysaccharide. Moreover, CCF-1 participates in the activation of prophenoloxidase cascade via recognition of yeast and Gram-negative bacteria cell wall components. These results suggest that the 42-kDa CCF-1 protein of E. foetida coelomic fluid likely plays a role in the protection of earthworms against microbes.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.