TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Poulsen, Knud
AU  - Brckalo, Tamara
AU  - Bobic, Sonja
AU  - Lindner, Buko
AU  - Petersen, Arnd
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/929
AB  - 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 alpha 1,3 linkages as well as beta 1,3 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 glycoprotcomics and lectin microarrays, with a potential for modulation of the immune response. (C) 2007 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - International Journal of Biochemistry and Cell Biology
T1  - 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
VL  - 40
IS  - 5
SP  - 929
EP  - 941
DO  - 10.1016/j.biocel.2007.10.033
ER  - 

@article{
author = "Gavrović-Jankulović, Marija and Poulsen, Knud and Brckalo, Tamara and Bobic, Sonja and Lindner, Buko and Petersen, Arnd",
year = "2008",
abstract = "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 alpha 1,3 linkages as well as beta 1,3 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 glycoprotcomics and lectin microarrays, with a potential for modulation of the immune response. (C) 2007 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "International Journal of Biochemistry and Cell Biology",
title = "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",
volume = "40",
number = "5",
pages = "929-941",
doi = "10.1016/j.biocel.2007.10.033"
}

Gavrović-Jankulović, M., Poulsen, K., Brckalo, T., Bobic, S., Lindner, B.,& Petersen, A.. (2008). 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. in International Journal of Biochemistry and Cell Biology
Pergamon-Elsevier Science Ltd, Oxford., 40(5), 929-941.
https://doi.org/10.1016/j.biocel.2007.10.033

Gavrović-Jankulović M, Poulsen K, Brckalo T, Bobic S, Lindner B, Petersen A. 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. in International Journal of Biochemistry and Cell Biology. 2008;40(5):929-941.
doi:10.1016/j.biocel.2007.10.033 .

Gavrović-Jankulović, Marija, Poulsen, Knud, Brckalo, Tamara, Bobic, Sonja, Lindner, Buko, Petersen, Arnd, "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" in International Journal of Biochemistry and Cell Biology, 40, no. 5 (2008):929-941,
https://doi.org/10.1016/j.biocel.2007.10.033 . .