Document Detail


An ancient C-type lectin in Chlamys farreri (CfLec-2) that mediate pathogen recognition and cellular adhesion.
MedLine Citation:
PMID:  20638410     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
C-type lectins are a superfamily of Ca(2+) dependent carbohydrate-recognition proteins which play significant diverse roles in nonself-recognition and clearance of invaders. In the present study, a C-type lectin (CfLec-2) from Zhikong scallop Chlamys farreri was selected to investigate its functions in innate immunity. The mRNA expression of CfLec-2 in hemocytes was significantly up-regulated (P<0.01) after scallops were stimulated by LPS, PGN or β-glucan, and reached the highest expression level at 12h post-stimulation, which was 72.5-, 23.6- or 43.8-fold compared with blank group, respectively. The recombinant CfLec-2 (designated as rCfLec-2) could bind LPS, PGN, mannan and zymosan in vitro, but it could not bind β-glucan. Immunofluorescence assay with polyclonal antibody specific for CfLec-2 revealed that CfLec-2 was mainly located in the mantle, kidney and gonad. Furthermore, rCfLec-2 could bind to the surface of scallop hemocytes, and then initiated cellular adhesion and recruited hemocytes to enhance their encapsulation in vitro, and this process could be specifically blocked by anti-rCfLec-2 serum. These results collectively suggested that CfLec-2 from the primitive deuterostome C. farreri could perform two distinct immune functions, pathogen recognition and cellular adhesion synchronously, while these functions were performed by collectins and selectins in vertebrates, respectively. The synchronous functions of pathogen recognition and cellular adhesion performed by CfLec-2 tempted us to suspect that CfLec-2 was an ancient form of C-type lectin, and apparently the differentiation of these two functions mediated by C-type lectins occurred after mollusk in phylogeny.
Authors:
Jialong Yang; Limei Qiu; Xiumei Wei; Leilei Wang; Lingling Wang; Zhi Zhou; Huan Zhang; Lin Liu; Linsheng Song
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-07-24
Journal Detail:
Title:  Developmental and comparative immunology     Volume:  34     ISSN:  1879-0089     ISO Abbreviation:  Dev. Comp. Immunol.     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-09-24     Completed Date:  2011-01-20     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7708205     Medline TA:  Dev Comp Immunol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1274-82     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Ltd. All rights reserved.
Affiliation:
The Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, 7 Nanhai Rd., Qingdao 266071, China.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Blotting, Western
Cell Adhesion
Collectins / chemistry,  immunology
Electrophoresis, Polyacrylamide Gel
Fluorescent Antibody Technique
Gene Expression
Hemocytes / immunology
Immunity, Innate*
Lectins, C-Type / chemistry,  genetics,  immunology*,  metabolism
Lipopolysaccharides / immunology
Mannans / immunology
Models, Molecular
Pectinidae / genetics,  immunology*,  metabolism
Phylogeny
Protein Structure, Tertiary
Recombinant Proteins
Selectins / chemistry,  immunology
Sequence Alignment
Shellfish
Up-Regulation
Zymosan / immunology
Chemical
Reg. No./Substance:
0/Collectins; 0/Lectins, C-Type; 0/Lipopolysaccharides; 0/Mannans; 0/Recombinant Proteins; 0/Selectins; 9010-72-4/Zymosan

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