Identification of (L)-fucose-binding proteins from the Nile tilapia (Oreochromis niloticus L.) serum.
Lectins are carbohydrate-binding proteins with many biological functions including cellular recognition and innate immunity. In this study, a major l-fucose-binding lectin from the serum of Nile tilapia (Oreochromis niloticus L.), designated as TFBP, was isolated by l-fucose-BSA Sepharose CL6B affinity chromatography. The SDS-PAGE (10%) analysis of TFBP revealed a major band of approximately 23 kDa with an N-terminal amino acid sequence of DQTETAGQQSXPQDIHAVLREL which did not give significant similarities to the protein databases using BLASTp searches. Ruthenium red staining indicate positive calcium-binding property of TFBP. The purified TFBP agglutinated human type O erythrocytes but not the type A and B fresh erythrocytes. Live Aeromonas hydrophila and Enterococcus faecalis cells were also agglutinated by the lectin. The fucose-binding proteins were detected in the soluble protein extracts from the gills, gut, head kidneys, liver, serum and spleen using a fucose-binding protein probe (l-fucose-BSA-horseradish peroxidase). The binding of TFBP with the l-fucose-BSA probe was inhibited by l-fucose but not by alpha-methyl-d-mannose.
Argayosa
Anacleto M
AM
Y.C. Lee Laboratory, Department of Biology, Johns Hopkins University, MD, USA. litoargayosa@science.upd.edu.ph
Lee
Yuan C
YC
D000372:Agglutination Tests; D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D023681:Cichlids / Q000235:genetics* / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism; D005643:Fucose / Q000378:metabolism; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight
D001798:Blood Proteins; D037102:Lectins; D005643:Fucose; D002118:Calcium