Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2008-3-10
pubmed:abstractText
Lectins as carbohydrate-binding proteins have been employed in various biological assays for the detection and characterization of glycan structures on glycoproteins, including clinical biomarkers in disease states. A mannose-specific banana lectin (BanLec) is unique in its specificity for internal alpha1,3 linkages as well as beta1,3 linkages at the reducing termini. The immunomodulatory potential of natural BanLec was recognized by a strong immunoglobulin G4 antibody response and T cell mitogen activity in humans. To explore its applicability in glycoproteomics and its modulatory potential, the gene of banana lectin was cloned, sequenced and a recombinant protein was produced in Escherichia coli. The obtained cDNA revealed a novel banana lectin isoform, with an open reading frame of 426 nucleotides, encoding a cytoplasmatic protein of 141 amino acids. The molecular mass of rBanLec determined by ESI FT-MS and N-terminal sequencing confirmed the cDNA at the protein level. The specificity of rBanLec for detection glycan structures was the same as for natural BanLec as examined with five protein extracts rich in glycoprotein content, as well as with horseradish peroxidase glycoprotein. Besides, the immunomodulatory potential of rBanLec and nBanLec were comparable as assessed by an inhibition assay and a human T cell proliferation assay where they induced a strong proliferation response in CD3+, CD4+, and CD8+ populations of human PBMCs. This recombinant BanLec is a useful reagent for glycoproteomics and lectin microarrays, with a potential for modulation of the immune response.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1357-2725
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
929-41
pubmed:meshHeading
pubmed-meshheading:18083059-Amino Acid Sequence, pubmed-meshheading:18083059-Antigens, CD3, pubmed-meshheading:18083059-CD4-Positive T-Lymphocytes, pubmed-meshheading:18083059-CD8-Positive T-Lymphocytes, pubmed-meshheading:18083059-Cell Proliferation, pubmed-meshheading:18083059-Cloning, Molecular, pubmed-meshheading:18083059-Glycomics, pubmed-meshheading:18083059-Glycoproteins, pubmed-meshheading:18083059-Humans, pubmed-meshheading:18083059-Immunoglobulin G, pubmed-meshheading:18083059-Immunologic Factors, pubmed-meshheading:18083059-Mannose, pubmed-meshheading:18083059-Mannose-Binding Lectins, pubmed-meshheading:18083059-Molecular Sequence Data, pubmed-meshheading:18083059-Monosaccharides, pubmed-meshheading:18083059-Musa, pubmed-meshheading:18083059-Plant Lectins, pubmed-meshheading:18083059-Protein Isoforms, pubmed-meshheading:18083059-Proteomics, pubmed-meshheading:18083059-Recombinant Proteins, pubmed-meshheading:18083059-Sequence Alignment
pubmed:year
2008
pubmed:articleTitle
A novel recombinantly produced banana lectin isoform is a valuable tool for glycoproteomics and a potent modulator of the proliferation response in CD3+, CD4+, and CD8+ populations of human PBMCs.
pubmed:affiliation
Department of Biochemistry, Faculty of Chemistry, University of Belgrade, Belgrade, Serbia. mgavrov@chem.bg.ac.yu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't