tetano
Editor, Senior Moderator
J Biol Chem. 2011 Apr 1. [Epub ahead of print]
High mannose-binding lectin with preference for the cluster of {alpha}1-2 mannose from the green alga Boodlea coacta is a potent entry inhibitor of HIV-1 and influenza viruses.
Sato Y, Hirayama M, Morimoto K, Yamamoto N, Okuyama S, Hori K.
Yasuda Women's University;
Abstract
The complete amino acid sequence of a lectin from the green alga Boodlea coacta (BCA), which was determined by a combination of Edman degradation of its peptide fragments and cDNA cloning, revealed that (1) B. coacta used a noncanonical genetic code (where TAA and TAG codons encode glutamine rather than a translation termination), and that (2) BCA consisted of 3 internal tandem-repeated domains, each of which contains the sequence motif similar to the carbohydrate-binding site of GNA (Galanthus nivalis agglutinin)-related lectin family. Carbohydrate-binding specificity of BCA was examined by a centrifugal ultrafiltration-HPLC assay using 42 pyridylaminated oligosaccharides. BCA bound to high mannose-type N-glycans but not to complex type, hybrid type, core structure of N-glycans or oligosaccharides from glycolipids. This lectin had exclusive specificity for α1-2 linked mannose at nonreducing terminal. The binding activity was enhanced as the number of terminal α1-2 linked mannose substitutions increased. Mannobiose, mannotriose, and mannopentaose, were incapable of binding to BCA. Thus, BCA preferentially recognized the nonreducing terminal α1-2 mannose cluster as a primary target. As predicted from carbohydrate-binding propensity, this lectin inhibited the human immunodeficiency virus (HIV)-1 entry into the host cells at an half maximal effective concentration of 8.2 nM. High affinity binding (K(A)= 3.71 ? 108 M(-1)) of BCA to the HIV envelope glycoprotein gp120 was demonstrated by surface plasmon resonance analysis. Moreover, BCA showed the potent anti-influenza activity by directly binding to viral envelope hemagglutinin against various strains including a clinical isolate of pandemic H1N1-2009 virus, revealing its potential as an antiviral reagent.
PMID: 21460211 [PubMed - as supplied by publisher]Free Article
http://www.ncbi.nlm.nih.gov/pubmed/21460211
High mannose-binding lectin with preference for the cluster of {alpha}1-2 mannose from the green alga Boodlea coacta is a potent entry inhibitor of HIV-1 and influenza viruses.
Sato Y, Hirayama M, Morimoto K, Yamamoto N, Okuyama S, Hori K.
Yasuda Women's University;
Abstract
The complete amino acid sequence of a lectin from the green alga Boodlea coacta (BCA), which was determined by a combination of Edman degradation of its peptide fragments and cDNA cloning, revealed that (1) B. coacta used a noncanonical genetic code (where TAA and TAG codons encode glutamine rather than a translation termination), and that (2) BCA consisted of 3 internal tandem-repeated domains, each of which contains the sequence motif similar to the carbohydrate-binding site of GNA (Galanthus nivalis agglutinin)-related lectin family. Carbohydrate-binding specificity of BCA was examined by a centrifugal ultrafiltration-HPLC assay using 42 pyridylaminated oligosaccharides. BCA bound to high mannose-type N-glycans but not to complex type, hybrid type, core structure of N-glycans or oligosaccharides from glycolipids. This lectin had exclusive specificity for α1-2 linked mannose at nonreducing terminal. The binding activity was enhanced as the number of terminal α1-2 linked mannose substitutions increased. Mannobiose, mannotriose, and mannopentaose, were incapable of binding to BCA. Thus, BCA preferentially recognized the nonreducing terminal α1-2 mannose cluster as a primary target. As predicted from carbohydrate-binding propensity, this lectin inhibited the human immunodeficiency virus (HIV)-1 entry into the host cells at an half maximal effective concentration of 8.2 nM. High affinity binding (K(A)= 3.71 ? 108 M(-1)) of BCA to the HIV envelope glycoprotein gp120 was demonstrated by surface plasmon resonance analysis. Moreover, BCA showed the potent anti-influenza activity by directly binding to viral envelope hemagglutinin against various strains including a clinical isolate of pandemic H1N1-2009 virus, revealing its potential as an antiviral reagent.
PMID: 21460211 [PubMed - as supplied by publisher]Free Article
http://www.ncbi.nlm.nih.gov/pubmed/21460211