Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
38
pubmed:dateCreated
1998-10-15
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acute-Phase Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Catechol Oxidase, http://linkedlifedata.com/resource/pubmed/chemical/Cytotoxins, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors, http://linkedlifedata.com/resource/pubmed/chemical/Glucans, http://linkedlifedata.com/resource/pubmed/chemical/Glucosidases, http://linkedlifedata.com/resource/pubmed/chemical/Lectins, http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/coelomic cytolytic factor 1..., http://linkedlifedata.com/resource/pubmed/chemical/glucan-binding proteins, http://linkedlifedata.com/resource/pubmed/chemical/laminaran, http://linkedlifedata.com/resource/pubmed/chemical/lipopolysaccharide-binding protein, http://linkedlifedata.com/resource/pubmed/chemical/pro-phenoloxidase
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24948-54
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9733802-Acute-Phase Proteins, pubmed-meshheading:9733802-Amino Acid Sequence, pubmed-meshheading:9733802-Animals, pubmed-meshheading:9733802-Base Sequence, pubmed-meshheading:9733802-Binding, Competitive, pubmed-meshheading:9733802-Carrier Proteins, pubmed-meshheading:9733802-Catechol Oxidase, pubmed-meshheading:9733802-Cloning, Molecular, pubmed-meshheading:9733802-Cytotoxins, pubmed-meshheading:9733802-Enzyme Activation, pubmed-meshheading:9733802-Enzyme Precursors, pubmed-meshheading:9733802-Glucans, pubmed-meshheading:9733802-Glucosidases, pubmed-meshheading:9733802-Kinetics, pubmed-meshheading:9733802-Lectins, pubmed-meshheading:9733802-Lipopolysaccharides, pubmed-meshheading:9733802-Membrane Glycoproteins, pubmed-meshheading:9733802-Molecular Sequence Data, pubmed-meshheading:9733802-Oligochaeta, pubmed-meshheading:9733802-Polysaccharides, pubmed-meshheading:9733802-Recombinant Proteins, pubmed-meshheading:9733802-Sequence Alignment, pubmed-meshheading:9733802-Sequence Homology, Amino Acid
pubmed:year
1998
pubmed:articleTitle
Identification and cloning of a glucan- and lipopolysaccharide-binding protein from Eisenia foetida earthworm involved in the activation of prophenoloxidase cascade.
pubmed:affiliation
Unit of Cellular Immunology, Flemish Interuniversity Institute for Biotechnology, VIB-VUB, Paardenstraat 65, B-1640 St-Genesius-Rode, Belgium. abeschin@vub.ac.be
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't