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. 2003 Dec 1;376(Pt 2):433–440. doi: 10.1042/BJ20030413

Structural and biochemical characterization of a new type of lectin isolated from carp eggs.

Monica Galliano 1, Lorenzo Minchiotti 1, Monica Campagnoli 1, Alberto Sala 1, Livia Visai 1, Angela Amoresano 1, Piero Pucci 1, Annarita Casbarra 1, Marco Cauci 1, Massimiliano Perduca 1, Hugo L Monaco 1
PMCID: PMC1223786  PMID: 12956625

Abstract

A previously unidentified glycoprotein present in the eggs of the carp ( Cyprinus carpio ) was isolated and structurally characterized. The protein binds to a Sepharose 4B matrix and can be eluted with 0.4 M N -acetylglucosamine. The protein has an apparent molecular mass of 26686.3 Da. On the basis of gel-filtration chromatography, the protein appears to be present in solution as a monomer. The sequence of its 238 amino acids, the position of its four disulphide bridges and the composition of its single N-linked carbohydrate chain were determined. The lectin shows a very low agglutinating activity for human A-type erythrocytes and interacts with both Gram-positive and -negative bacteria. These latter interactions are inhibited by N -acetylglucosamine. A database search shows that its amino acid sequence is similar to that of the members of an invertebrate lectin family that includes tachylectin-1. Tachylectin-1 is present in the amoebocytes of the horseshoe crab, Tachypleus tridentatus, and plays a role in the innate defence system of this species. Homologous genes are also present in other fish, having 85% identity with a gene expressed in the oocytes of the crucian carp ( Carassius auratus gibelio ) and 78% identity with a gene in the cDNA library of the zebrafish ( Danio rerio ).

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Selected References

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