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| Reference : Distinct carbohydrate recognition domains of an invertebrate defense molecule recognize ... |
| Scientific journals : Article | |||
| Life sciences : Biochemistry, biophysics & molecular biology Life sciences : Biotechnology | |||
| http://hdl.handle.net/2268/32935 | |||
| Distinct carbohydrate recognition domains of an invertebrate defense molecule recognize Gram-negative and Gram-positive bacteria. | |
| English | |
| Bilej, M. [>Academy of Sciences of the Czech Republic, Prague > > >Dpt of Immunology, Institute of Microbiology > > >] | |
| De Baetselier, P. [>Free University of Brussels > > >Dpt of Immunology, Parasitology and Ultrastructure, Flemish Interuniversity - Institute for Biotechnology > > >] | |
| Van Dijck, E. [>Free University of Brussels > > >Dpt of Immunology, Parasitology and Ultrastructure, Flemish Interuniversity - Institute for Biotechnology > > >] | |
| Stijlemans, B. [>Free University of Brussels > > >Dpt of Immunology, Parasitology and Ultrastructure, Flemish Interuniversity - Institute for Biotechnology > > >] | |
Colige, Alain  [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Laboratoire de Biologie des tissus conjonctifs > > >] | |
| Beschin, A. [>Free University of Brussels > > >Dpt of Immunology, Parasitology and Ultrastructure, Flemish Interuniversity - Institute for Biotechnology > > >] | |
| 2001 | |
| Journal of Biological Chemistry | |
| American Society for Biochemistry and Molecular Biology | |
| 276 | |
| 49 | |
| 45840-7 | |
| International | |
| 0021-9258 | |
| 1083-351X | |
| Baltimore | |
| MD | |
| [en] Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Carbohydrate Metabolism ; Cytotoxins/chemistry/metabolism ; DNA Primers ; Enzyme Activation ; Gram-Negative Bacteria/metabolism ; Gram-Positive Bacteria/metabolism ; Lectins ; Molecular Sequence Data ; Monophenol Monooxygenase/metabolism ; Oligochaeta/enzymology/metabolism | |
| [en] Coelomic fluid of Eisenia foetida earthworms (Oligochaeta, Annelida) contains a 42-kDa defense molecule named CCF for coelomic cytolytic factor. By binding microbial antigens, namely the O-antigen of lipopolysaccharide (LPS), beta-1,3-glucans, or N,N'-diacetylchitobiose present, respectively, on Gram-negative bacteria or yeast cell walls, CCF triggers the prophenoloxidase activating pathway. We report that CCF recognizes lysozyme-predigested Gram-positive bacteria or the peptidoglycan constituent muramyl dipeptide as well as muramic acid. To identify the pattern recognition domains of CCF, deletion mutants were tested for their ability to reconstitute the prophenoloxidase cascade in E. foetida coelomic fluid depleted of endogenous CCF in the presence of LPS, beta-1,3-glucans, N,N'-diacetylchitobiose, and muramic acid. In addition, affinity chromatography of CCF peptides was performed on immobilized beta-1,3-glucans or N,N'-diacetylchitobiose. We found that the broad specificity of CCF for pathogen-associated molecular patterns results from the presence of two distinct pattern recognition domains. One domain, which shows homology with the polysaccharide and glucanase motifs of beta-1,3-glucanases and invertebrate defense molecules located in the central part of the CCF polypeptide chain, interacts with LPS and beta-1,3-glucans. The C-terminal tryptophan-rich domain mediates interactions of CCF with N,N'-diacetylchitobiose and muramic acid. These data provide evidence for the presence of spatially distinct carbohydrate recognition domains within this invertebrate defense molecule. | |
| Researchers | |
| http://hdl.handle.net/2268/32935 | |
| 10.1074/jbc.M107220200 |
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