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Comparative study of the CCF-like pattern recognition protein in different Lumbricid species
Silerová M, Procházková P, Josková R, Josens G, Beschin A, De Baetselier P, Bilej M.
Language English Country United States
Document type Comparative Study
- MeSH
- Cytotoxins pharmacology genetics metabolism MeSH
- Disaccharides metabolism MeSH
- Financing, Organized MeSH
- Phylogeny MeSH
- Catechol Oxidase metabolism MeSH
- Lectins pharmacology genetics metabolism MeSH
- Humans MeSH
- Molecular Sequence Data MeSH
- Cell Line, Tumor MeSH
- Oligochaeta genetics metabolism MeSH
- Enzyme Precursors metabolism MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Alignment MeSH
- Substrate Specificity MeSH
- Random Amplified Polymorphic DNA Technique MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Comparative Study MeSH
Coelomic fluid of the Lumbricid Eisenia fetida contains a 42-kDa pattern recognition protein named coelomic cytolytic factor (CCF) that binds microbial cell wall components and triggers the activation of the prophenoloxidase cascade, an important invertebrate defense pathway. Here we report on the sequence characterization of CCF-like molecules of other Lumbricids: Aporrectodea caliginosa, Aporrectodea icterica, Aporrectodea longa, Aporrectodea rosea, Dendrobaena veneta, Lumbricus rubellus and Lumbricus terrestris, and show that CCF from E. fetida has a broader saccharide-binding specificity, being the only one recognizing N,N'-diacetylchitobiose. We suggest that the broad recognition repertoire of E. fetida CCF reflects a particular microbial environment this species lives in.
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- $a Department of Immunology, Institute of Microbiology, Academy of Sciences of the Czech Republic, Videnska 1083, 142 20 Prague 4, Czech Republic
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- $a Coelomic fluid of the Lumbricid Eisenia fetida contains a 42-kDa pattern recognition protein named coelomic cytolytic factor (CCF) that binds microbial cell wall components and triggers the activation of the prophenoloxidase cascade, an important invertebrate defense pathway. Here we report on the sequence characterization of CCF-like molecules of other Lumbricids: Aporrectodea caliginosa, Aporrectodea icterica, Aporrectodea longa, Aporrectodea rosea, Dendrobaena veneta, Lumbricus rubellus and Lumbricus terrestris, and show that CCF from E. fetida has a broader saccharide-binding specificity, being the only one recognizing N,N'-diacetylchitobiose. We suggest that the broad recognition repertoire of E. fetida CCF reflects a particular microbial environment this species lives in.
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