Cloning cDNA sequence coding the KSA-1 lectin from red alga Kappaphycus striatum cultivated in Vietnam


  • Le Dinh Hung Nha Trang Institute of Technology Research and Application, Vietnam Academy of Science and Technology
  • Dinh Thanh Trung Nha Trang Institute of Technology Research and Application, Vietnam Academy of Science and Technology



Amino acid sequence, cDNA of KSA-1, Kappaphycus striatum, Lectin, Lower organisms, mRNA, Red alga


The red alga Kappaphycus striatum is economically important food species and extensively cultivated in Vietnam. This cultivated alga may thus now contribute as a source of not only carrageenan, but also other bioactive compounds for biochemical and medicinal uses. KSA-1 lectin from this alga has been evaluated for biochemical properties, including high-mannose binding specificity, N-terminal amino acid sequence and molecular mass. In this study, we have cloned the cDNA clone encoding the lectin KSA-1. The full-length sequence of cDNA clone of KSA-1 lectin encoded a polypeptide of 268 amino acids including initiating methionine, with four tandemly repeated domains of about 67 amino acids, and sharing 43% sequence identity. The primary structure and the amino acid residues interact with mannopentaose core structure per a repeat domain of the KSA-1 lectin highly resemble and match those of anti-virus the lectin family in lower organinsms, including bacteria [BOA from Burkholderia oklahomensis EO147, MBHA from Myxococcus xanthus and PFA from Pseudomonas fluorescens Pf0-1], cyanobacteria [OAA from Oscillatoria agardhii] and red algae [ESA-2 from Eucheuma serra, EDA-2 from Eucheuma denticulatum, KAA-1 and KAA-2 from Kappaphycus alvarezii and KSA-2 from K. striatum]. Analysis of predicted secondary structure of KSA-1 showed twenty β-strands. Each repeated domain comprises the five β-strands and matches with number of β-strands of BOA lectin. Therefore, the red alga K. striatum could be a good source for application in biomedicine and biochemistry as materials for production of the functional lectin(s).


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