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A short-form C-type lectin from amphioxus acts as a direct microbial killing protein via interaction with peptidoglycan and glucan
- Source :
- Journal of immunology (Baltimore, Md. : 1950). 179(12)
- Publication Year :
- 2007
-
Abstract
- To investigate the evolution and immune function of C-type lectin in amphioxus, the primitive representative of the chordate phylum, we identified three C-type lectins consisting solely of a carbohydrate recognition domain and N-terminal signal peptide and found that they had distinct express patterns in special tissues and immune response to stimulations analyzed by quantitative real-time PCR. We characterized the biochemical and biological properties of AmphiCTL1, which was dramatically up-regulated in amphioxus challenged with Staphylococcus aureus, Saccharomyces cerevisiae, and zymosan. Immunohistochemistry demonstrated that the localization of AmphiCTL1 protein was exclusively detected in the inner folding tissues of the hepatic diverticulum. Recombinant AmphiCTL1 was characterized as a typical Ca2+-dependent carbohydrate-binding protein possessing hemagglutinating activity, preferentially bound to all examined four Gram-positive bacteria and two yeast strains, but had little binding activity toward four Gram-negative bacteria we tested. It aggregated S. aureus and S. cerevisiae in a Ca2+-dependent manner and specifically bound to insoluble peptidoglycan and glucan, but not to LPS, lipoteichoic acid, and mannan. Calcium increased the intensity of the interaction between AmphiCTL1 and those components, but was not essential. This lectin directly killed S. aureus and S. cerevisiae in a Ca2+-independent fashion, and its binding to microorganism cell wall polysaccharides such as peptidoglycan and glucan preceded microbial killing activity. These findings suggested that AmphiCTL1 acted as a direct microbial killing C-type lectin through binding microbial targets via interaction with peptidoglycan and glucan. Thus, AmphiCTL1 may be an evolutionarily primitive form of antimicrobial protein involved in lectin-mediated innate immunity.
- Subjects :
- Staphylococcus aureus
Immunology
Molecular Sequence Data
Peptidoglycan
Saccharomyces cerevisiae
Biology
Microbiology
Cell wall
chemistry.chemical_compound
C-type lectin
Immunology and Allergy
Animals
Lectins, C-Type
Amino Acid Sequence
Cloning, Molecular
Chordata
Glucans
Glucan
Mannan
chemistry.chemical_classification
Zymosan
Lectin
Recombinant Proteins
chemistry
Biochemistry
biology.protein
Lipoteichoic acid
Subjects
Details
- ISSN :
- 00221767
- Volume :
- 179
- Issue :
- 12
- Database :
- OpenAIRE
- Journal :
- Journal of immunology (Baltimore, Md. : 1950)
- Accession number :
- edsair.doi.dedup.....5c16c3ec6ff5f5d59e71cf3373e92dc7