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<identifier>oai:HAL:hal-00746015v1</identifier>
<datestamp>2017-12-21</datestamp>
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<publisher>HAL CCSD</publisher>
<title lang=en>Analysis of a cDNA-derived sequence of a novel mannose-binding lectin, codakine, from the tropical clam Codakia orbicularis.</title>
<creator>Gourdine, Jean-Philippe</creator>
<creator>Smith-Ravin, Emilie Juliette</creator>
<contributor>Dynamique des écosystèmes Caraïbe et biologie des espèces associées (DYNECAR EA 926) ; Université des Antilles et de la Guyane (UAG)</contributor>
<contributor>Conseil régional de Guadeloupe</contributor>
<description>International audience</description>
<source>ISSN: 1050-4648</source>
<source>EISSN: 1095-9947</source>
<source>Fish and Shellfish Immunology</source>
<publisher>Elsevier</publisher>
<identifier>hal-00746015</identifier>
<identifier>https://hal.univ-antilles.fr/hal-00746015</identifier>
<source>https://hal.univ-antilles.fr/hal-00746015</source>
<source>Fish and Shellfish Immunology, Elsevier, 2007, 22 (5), pp.498-509. 〈10.1016/j.fsi.2006.06.013〉</source>
<identifier>DOI : 10.1016/j.fsi.2006.06.013</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fsi.2006.06.013</relation>
<identifier>PUBMED : 17169576</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/17169576</relation>
<language>en</language>
<subject>[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>This work relates to the characterisation of the predominant gill protein of the white clam, Codakia orbicularis (Linné, 1758), which harbours endosymbiotic sulphur-oxidising chemoautotrophic bacteria. Total RNA was extracted from the clam to perform 3'rapid amplification of cDNA ends (3'RACE) using degenerate oligonucleotides prepared from a partial sequence of a predominant protein of about 14kDa, termed codakine. The partial peptide sequence was obtained by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and Edman degradation. Clones isolated from the cDNA library and containing the gene of interest were used in polymerase chain reaction (PCR). The PCR and RACE-PCR products were sequenced to determine the entire coding DNA sequence of codakine. BLAST analysis revealed about 23% to 29% sequence identity between codakine and various animal C-type lectins that are often involved in symbiosis and immune defences. Codakine also contains the motifs and domains of Ca(2+)-dependent C-type lectins, and in particular the tripeptide EPN motif frequently found in mannose-binding lectins (MBLs). Analysis of the protein by affinity chromatography on a mannose-agarose column is consistent with the findings that codakine is a dimeric Ca(2+)-dependent MBL of about 29kDa. Based on the present results, it is hypothesised that this novel C. orbicularis gill protein is involved in the recognition of symbiotic and pathogenic bacteria.</description>
<date>2007-05</date>
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