scholarly journals Elderberry Bark Lectins Evolved to Recognize Neu5Ac 2,6Gal/GalNAc Sequence from a Gal/GalNAc Binding Lectin Through the Substitution of Amino-Acid Residues Critical for the Binding to Sialic Acid

2007 ◽  
Vol 143 (1) ◽  
pp. 143-143
Author(s):  
H. Kaku ◽  
H. Kaneko ◽  
N. Minamihara ◽  
K. Iwata ◽  
E. T. Jordan ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Binding Lectin

scholarly journals Chemical-modification studies of a unique sialic acid-binding lectin from the snail Achatina fulica. Involvement of tryptophan and histidine residues in biological activity

1988 ◽  
Vol 254 (1) ◽  
pp. 195-202 ◽  
Author(s):  
S Basu ◽  
C Mandal ◽  
A K Allen
Keyword(s):  
Biological Activity ◽  
Sialic Acid ◽  
Amino Acid ◽  
Fluorescence Emission ◽  
Amino Acid Residues ◽  
Achatina Fulica ◽  
Histidine Residues ◽  
Sialic Acid Binding ◽  
Arginine Residues ◽  
Binding Lectin

A unique sialic acid-binding lectin, achatininH (ATNH) was purified in single step from the haemolymph of the snail Achatina fulica by affinity chromatography on sheep submaxillary-gland mucin coupled to Sepharose 4B. The homogeneity was checked by alkaline gel electrophoresis, immunodiffusion and immunoelectrophoresis. Amino acid analysis showed that the lectin has a fairly high content of acidic amino acid residues (22% of the total). About 1.3% of the residues are half-cystine. The glycoprotein contains 21% carbohydrate. The unusually high content of xylose (6%) and fucose (2.7%) in this snail lectin is quite interesting. The protein was subjected to various chemical modifications in order to detect the amino acid residues and carbohydrate residues present in its binding sites. Modification of tyrosine and arginine residues did not affect the binding activity of ATNH; however, modification of tryptophan and histidine residues led to a complete loss of its biological activity. A marked decrease in the fluorescence emission was found as the tryptophan residues of ATNH were modified. The c.d. data showed the presence of an identical type of conformation in the native and modified agglutinin. The modification of lysine and carboxy residues partially diminished the biological activity. The activity was completely lost after a beta-elimination reaction, indicating that the sugars are O-glycosidically linked to the glycoprotein's protein moiety. This result confirms that the carbohydrate moiety also plays an important role in the agglutination property of this lectin.

scholarly journals Molecular Interactions of the Polysialytransferase Domain (PSTD) in ST8Sia IV with CMP-Sialic Acid and Polysialic Acid Required for Polysialylation of the Neural Cell Adhesion Molecule Proteins: An NMR Study

2020 ◽  
Vol 21 (5) ◽  
pp. 1590 ◽  
Author(s):  
Si-Ming Liao ◽  
Bo Lu ◽  
Xue-Hui Liu ◽  
Zhi-Long Lu ◽  
Shi-Jie Liang ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Sialic Acid ◽  
Amino Acid ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Polysialic Acid ◽  
Neural Cell ◽  
Amino Acid Residues ◽  
Neural Cell Adhesion

Polysialic acid (polySia) is an unusual glycan that posttranslational modifies neural cell adhesion molecule (NCAM) proteins in mammalian cells. The up-regulated expression of polySia-NCAM is associated with tumor progression in many metastatic human cancers and in neurocognitive processes. Two members of the ST8Sia family of α2,8-polysialyltransferases (polySTs), ST8Sia II (STX) and ST8Sia IV (PST) both catalyze synthesis of polySia when activated cytidine monophosphate(CMP)-Sialic acid (CMP-Sia) is translocate into the lumen of the Golgi apparatus. Two key polybasic domains in the polySTs, the polybasic region (PBR) and the polysialyltransferase domain (PSTD) areessential forpolysialylation of the NCAM proteins. However, the precise molecular details to describe the interactions required for polysialylation remain unknown. In this study, we hypothesize that PSTD interacts with both CMP-Sia and polySia to catalyze polysialylation of the NCAM proteins. To test this hypothesis, we synthesized a 35-amino acid-PSTD peptide derived from the ST8Sia IV gene sequence and used it to study its interaction with CMP-Sia, and polySia. Our results showed for the PSTD-CMP-Sia interaction, the largest chemical-shift perturbations (CSP) were in amino acid residues V251 to A254 in the short H1 helix, located near the N-terminus of PSTD. However, larger CSP values for the PSTD-polySia interaction were observed in amino acid residues R259 to T270 in the long H2 helix. These differences suggest that CMP-Sia preferentially binds to the domain between the short H1 helix and the longer H2 helix. In contrast, polySia was principally bound to the long H2 helix of PSTD. For the PSTD-polySia interaction, a significant decrease in peak intensity was observed in the 20 amino acid residues located between the N-and C-termini of the long H2 helix in PSTD, suggesting a slower motion in these residues when polySia bound to PSTD. Specific features of the interactions between PSTD-CMP-Sia, and PSTD-polySia were further confirmed by comparing their 800 MHz-derived HSQC spectra with that of PSTD-Sia, PSTD-TriSia (DP 3) and PSTD-polySia. Based on the interactions between PSTD-CMP-Sia, PSTD-polySia, PBR-NCAM and PSTD-PBR, these findingsprovide a greater understanding of the molecular mechanisms underlying polySia-NCAM polysialylation, and thus provides a new perspective for translational pharmacological applications and development by targeting the two polysialyltransferases.

Amino acid sequence of sialic acid binding lectin from frog (Rana catesbeiana) eggs

Biochemistry ◽  
1987 ◽  
Vol 26 (8) ◽  
pp. 2189-2194 ◽  
Author(s):  
Koiti Titani ◽  
Koji Takio ◽  
Manabu Kuwada ◽  
Kazuo Nitta ◽  
Fusao Sakakibara ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rana Catesbeiana ◽  
Sialic Acid Binding ◽  
Binding Lectin

Identification of amino acid residues of influenza A virus H3 HA contributing to the recognition of molecular species of sialic acid

FEBS Letters ◽  
2009 ◽  
Vol 583 (19) ◽  
pp. 3171-3174 ◽  
Author(s):  
Tadanobu Takahashi ◽  
Asako Hashimoto ◽  
Mami Maruyama ◽  
Hideharu Ishida ◽  
Makoto Kiso ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Influenza A Virus ◽  
Molecular Species ◽  
Influenza A ◽  
Amino Acid Residues
Sign in / Sign up

Export Citation Format

Share Document