Chen, ZhonghaiKai, GuoyinLiu, XiaojunLin, JuanSun, XiaofenTang, Kexuan2005-03-122009-06-012005-03-122009-06-012005-03-12Chen Z, Kai G, Liu X, Lin J, Sun X, Tang K. cDNA cloning and characterization of a mannose-binding lectin from Zingiber officinale Roscoe (ginger) rhizomes. Journal of Biosciences. 2005 Mar; 30(2): 213-20http://imsear.searo.who.int/handle/123456789/111342Using RNA extracted from Zingiber officinale rhizomes and primers designed according to the conservative regions of monocot mannose-binding lectins, the full-length cDNA of Z. officinale agglutinin (ZOA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA of zoa was 746 bp and contained a 510 bp open reading frame (ORF) encoding a lectin precursor of 169 amino acids with a signal peptide. ZOA was a mannose-binding lectin with three typical mannose-binding sites (QDNY). Semi-quantitative RT-PCR analysis revealed that zoa expressed in all the tested tissues of Z. officinale including leaf, root and rhizome, suggesting it to be a constitutively expressing form. ZOA protein was successfully expressed in Escherichia coli with the molecular weight expected. To our knowledge, this is the first mannose-binding lectin cDNA cloned from the family Zingiberaceae. Our results demonstrate that monocot mannose-binding lectins also occur within the family Zingiberaceae.engAmino Acid SequenceBase SequenceBinding SitesCloning, MolecularCluster AnalysisComputational BiologyDNA PrimersDNA, Complementary --geneticsGene ExpressionGinger --geneticsHemagglutinationMannose-Binding Lectin --geneticsMolecular Sequence DataPhylogenyReverse Transcriptase Polymerase Chain ReactionRhizome --chemistrySequence Analysis, DNAComparative Study