scholarly journals Physiochemical studies on achatininH, a novel sialic acid-binding lectin

1989 ◽  
Vol 257 (1) ◽  
pp. 65-71 ◽  
Author(s):  
C Mandal ◽  
S Basu ◽  
C Mandal
Keyword(s):  
Sialic Acid ◽  
Binding Affinity ◽  
Physicochemical Characterization ◽  
Alpha Helix ◽  
Spectral Studies ◽  
Acetylneuraminic Acid ◽  
High Affinity ◽  
Sugar Binding ◽  
Sialic Acid Binding ◽  
Binding Lectin

We have purified a sialic acid-binding lectin, achatininH, in a single step by affinity chromatography, having high affinity for 9-O-acetylneuraminic acid. The physicochemical characterization of the interaction of achatininH with bivalent metal ions and sialic acid derivatives by the use of spectrofluorimetry, spectropolarimetry and precipitin reaction is reported. From fluorescence quenching studies the binding of Ca2+ (Ka = 251 +/- 9 M-1) and of Mn2+ (Ka = 86 +/- 5 M-1) was found to be weak, but their presence is absolutely necessary for sugar binding as well as biological activity. The nature and position of the substituent group play a very important role in the binding affinity. AchatininH shows a high affinity for 9-O-acetylneuraminic acid (Ka = 1.20 x 10(3) +/- 0.07 x 10(3) M-1) compared with that for the 4-O-acetyl derivative. In oligomers the binding strength increases in the order monosaccharide less than disaccharide less than trisaccharide. The binding affinity of achatininH for the disaccharide was found to reach a peak around pH 8. From c.d. spectral studies achatininH was found to have a high beta-sheet content (46%) and a low alpha-helix content (24%). From precipitin analysis at least one sugar-binding site on each of the 16 monomer subunits of the protein is indicated.

scholarly journals Porcine Arterivirus Infection of Alveolar Macrophages Is Mediated by Sialic Acid on the Virus

2004 ◽  
Vol 78 (15) ◽  
pp. 8094-8101 ◽  
Author(s):  
Peter L. Delputte ◽  
Hans J. Nauwynck
Keyword(s):  
Sialic Acid ◽  
Alveolar Macrophages ◽  
Sialic Acids ◽  
Respiratory Syndrome Virus ◽  
Specific Monoclonal Antibody ◽  
Neuraminidase Treatment ◽  
Acid Binding Protein ◽  
Sialic Acid Binding ◽  
High Mannose ◽  
Binding Lectin

ABSTRACT Recently, we showed that porcine sialoadhesin (pSn) mediates internalization of the arterivirus porcine reproductive and respiratory syndrome virus (PRRSV) in alveolar macrophages (Vanderheijden et al., J. Virol. 77:8207-8215, 2003). In rodents and humans, sialoadhesin, or Siglec-1, has been described as a macrophage-restricted molecule and to specifically bind sialic acid moieties. In the current study, we investigated whether pSn is a sialic acid binding protein and, whether so, whether this property is important for its function as a PRRSV receptor. Using untreated and neuraminidase-treated sheep erythrocytes, we showed that pSn binds sialic acid. Furthermore, pSn-specific monoclonal antibody 41D3, which blocks PRRSV infection, inhibited this interaction. PRRSV attachment to and infection of porcine alveolar macrophages (PAM) were both shown to be dependent on the presence of sialic acid on the virus: neuraminidase treatment of virus but not of PAM blocked infection and reduced attachment. Enzymatic removal of all N-linked glycans on the virus with N-glycosidase F reduced PRRSV infection, while exclusive removal of nonsialylated N-linked glycans of the high-mannose type with endoglycosidase H had no significant effect. Free sialyllactose and sialic acid containing (neo)glycoproteins reduced infection, while lactose and (neo)glycoproteins devoid of sialic acids had no significant effect. Studies with linkage-specific neuraminidases and lectins indicated that α2-3- and α2-6-linked sialic acids on the virion are important for PRRSV infection of PAM. From these results, we conclude that pSn is a sialic acid binding lectin and that interactions between sialic acid on the PRRS virion and pSn are essential for PRRSV infection of PAM.

Characterization of the Binding Affinity of Siglec-1 to gp120, gp145, and V2 Loop via Sialic Acid Binding Motif

2014 ◽  
Vol 30 (S1) ◽  
pp. A119-A120
Author(s):  
Hung V. Trinh ◽  
Ousman Jobe ◽  
Guofen Gao ◽  
Carl R. Alving ◽  
Venigalla Rao ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Binding Affinity ◽  
Binding Motif ◽  
Sialic Acid Binding

scholarly journals Involvement of ER stress in apoptosis induced by sialic acid-binding lectin (leczyme) from bullfrog eggs

2013 ◽  
Vol 43 (6) ◽  
pp. 1799-1808 ◽  
Author(s):  
TAKEO TATSUTA ◽  
MASAHIRO HOSONO ◽  
YUKI MIURA ◽  
SHIGEKI SUGAWARA ◽  
YUKIKO KARIYA ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Er Stress ◽  
Sialic Acid Binding ◽  
Binding Lectin

A sialic acid-binding lectin from the legume Maackia fauriei: comparison with lectins from M. amurensis

Plant Science ◽  
2004 ◽  
Vol 167 (6) ◽  
pp. 1315-1321 ◽  
Author(s):  
Bum Soo Kim ◽  
Kyung Taik Oh ◽  
Due Hyeon Cho ◽  
Yun Jung Kim ◽  
Wan Mo Koo ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Sialic Acid Binding ◽  
Binding Lectin

scholarly journals Sialic acid-binding lectin from bullfrog eggs inhibits human malignant mesothelioma cell growth in vitro and in vivo

PLoS ONE ◽  
2018 ◽  
Vol 13 (1) ◽  
pp. e0190653 ◽  
Author(s):  
Takeo Tatsuta ◽  
Toshiyuki Satoh ◽  
Shigeki Sugawara ◽  
Akiyoshi Hara ◽  
Masahiro Hosono
Keyword(s):  
Sialic Acid ◽  
Cell Growth ◽  
Malignant Mesothelioma ◽  
Sialic Acid Binding ◽  
Mesothelioma Cell ◽  
Binding Lectin

Chemical Synthesis of a Synthetic Analogue of the Sialic Acid-Binding Lectin Siglec-7

ChemBioChem ◽  
2014 ◽  
Vol 15 (17) ◽  
pp. 2503-2507 ◽  
Author(s):  
Masayuki Izumi ◽  
Akihisa Otsuki ◽  
Mika Nishihara ◽  
Ryo Okamoto ◽  
Yasuhiro Kajihara
Keyword(s):  
Sialic Acid ◽  
Chemical Synthesis ◽  
Synthetic Analogue ◽  
Sialic Acid Binding ◽  
Binding Lectin

scholarly journals The structure of siglec-7 in complex with sialosides: leads for rational structure-based inhibitor design

2006 ◽  
Vol 397 (2) ◽  
pp. 271-278 ◽  
Author(s):  
Helen Attrill ◽  
Hirokazu Takazawa ◽  
Simone Witt ◽  
Soerge Kelm ◽  
Rainer Isecke ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Binding Sites ◽  
Cellular Interactions ◽  
Inhibitor Design ◽  
Binding Assays ◽  
Rational Structure ◽  
Transmembrane Receptors ◽  
Acetylneuraminic Acid ◽  
Sialic Acid Binding ◽  
Inhibition Data

Siglecs (sialic acid binding Ig-like lectins) are transmembrane receptors for sialylated glycoconjugates that modulate cellular interactions and signalling events in the haematopoietic, immune and nervous systems. Siglec-7 is a structural prototype for the recently described family of immune inhibitory CD33-related siglecs and is predominantly expressed on natural killer cells and monocytes, as well as subsets of CD8 T-cells. Siglec-specific inhibitors are desired for the detection of masked and unmasked forms of siglecs, to aid in dissection of signalling pathways and as tools to investigate siglecs as potential therapeutic targets. As a first step towards this end, we present the crystal structure of siglec-7 in complex with a sialylated ligand, the ganglioside analogue DSLc4 [α(2,3)/α(2,6) disialyl lactotetraosyl 2-(trimethylsilyl)ethyl], which allows for a detailed description of the binding site, required for structure-guided inhibitor design. Mutagenesis and binding assays were used to demonstrate a key structural role for Lys131, a residue that changes conformation upon sialic acid binding. Differences between the binding sites of siglec family members were then exploited using α-methyl Neu5Ac (N-acetylneuraminic acid) as a basic scaffold. A co-crystal of siglec-7 in complex with the sialoside inhibitor, oxamido-Neu5Ac [methyl α-9-(amino-oxalyl-amino)-9-deoxy-Neu5Ac] and inhibition data for the sialosides gives clear leads for future inhibitor design.

Sign in / Sign up

Export Citation Format

Share Document