Interaction of a lectin from <i>Psathyrella velutina</i> mushroom with <i>N</i>‐acetylneuraminic acid

Ueda, Haruko; Kojima, Kensuke; Saitoh, Toshihito; Ogawa, Haruko

doi:10.1016/s0014-5793(99)00334-8

Cited by 38 publications

(46 citation statements)

References 22 publications

(15 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Materials-PVL was purified from the fruiting bodies of P. velutina mushrooms collected in Japan, and PVL-Sepharose and fetuin-Sepharose were prepared by reacting amino groups of PVL (5 mg) or fetuin (40 mg) with formyl-Sepharose (2 g) by reductive amination as reported previously (23). SNA, human ␣ 1 -acid glycoprotein (orosomucoid), fetuin from fetal calf serum, and human transferrin were purchased from Sigma.…”

Section: Methodsmentioning

confidence: 99%

“…Griffonia simplicifolia lectin II (GS II) was purchased from EY Laboratories Inc. (San Mateo, CA). Biotinylation of MAL, concanavalin A, L-PHA, and GS II was carried out with N-hydroxysuccinimide biotin (Pierce) according to the previously reported method (23). For preparation of the anti-PVL antibody, 80 l of 1 mg/ml PVL was mixed with 160 l of research adjuvant (TiterMax TM Gold, CytRX Corp., Norcross, GA), and a 100-l aliquot was injected intramuscularly into each thigh of a rabbit twice with a 3-week interval.…”

Section: Methodsmentioning

confidence: 99%

“…After washing with TBS, 100 l of HRP-conjugated anti-rabbit IgG antibody diluted to 1:1,000 with 1% bovine serum albumin, TBS was added. After incubation for 3 h, the color was developed and read at 490 nm using a microplate reader as described previously (23).…”

Section: Sds-page and Binding Studies With Biotin-or Hrp-lectins On Tmentioning

confidence: 99%

“…Recently, we observed that PVL binds to several sialoglycoproteins with no GlcNAc residues exposed. We also found that PVL recognizes N-acetylneuraminic acid (NeuAc) at the same site as the GlcNAc-binding site, and displays differential binding to oligosaccharides depending on the affinity for nonreducing terminal NeuAc residues (23). In this study, the detailed binding specificity of PVL toward sialoglycoproteins was studied in comparison with other sialic acid-specific lectins.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing TerminalN-Acetylneuraminic Acid α2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans

Ueda¹,

Matsumoto²,

Takahashi³

et al. 2002

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

A lectin from the fruiting body of the Psathyrella velutina mushroom (PVL) was found to bind specifically to N-acetylneuraminic acid, as well as to GlcNAc (Ueda, H., Kojima, K., Saitoh, T., and Ogawa, H. (1999) FEBS Lett. 448, 75-80). In this study, the glycan sequences that PVL recognizes with high affinity on sialoglycoproteins were revealed. Among sialic acid-specific lectins only PVL could reveal the sialylated N-acetyllactosamine structure of glycoproteins in blotting studies, based on the dual specificity. The affinity of PVL to fetuin was measured by surface plasmon resonance to be 10 7 M ؊1 , which is an order of magnitude higher than those of Sambucus nigra agglutinin and Maackia amurensis mitogen, whereas affinity to asialofetuin was ϳ0 and to asialoagalactofetuin was 10 8 M ؊1 , suggesting that PVL exhibits remarkably high affinities toward glycoproteins possessing trisialo-or GlcNAc-exposed glycans. Transferrin was separated into fractions that correspond to the sialylation states on an immobilized PVL column. Transferrin-possessing trisialoglycans containing ␣2,3-linked N-acetylneuraminic acid on the ␤1,4-linked GlcNAc branch bound to the PVL column and eluted with GlcNAc; those containing only ␣2,6-linked sialic acids were retarded, whereas other transferrin fractions passed through the column. These results indicate that PVL is a lectin with potential for separation and detection of sialoglycoproteins because of its dual specificity toward sialoglycans and GlcNAc exposed glycans.Sialic acids play an important role as ligands in cell sociology. Sialylation of glycoproteins changes under pathological conditions as well as during developmental stages, and altered sialylation often has significant implications in the physiological role of glycoproteins (1-3). Lectins that recognize the linkages or modifications of sialic acid are therefore indispensable as reagents in biochemical research and diagnostic analyses.Among sialic acid-specific lectins purified from plants and other sources, several lectins have been employed as tools for the detection and separation of sialic acid-containing glycoconjugates (3, 4). Lectins that distinguish various linkages of sialic acid are elderberry bark lectin (SNA 1 ; Sambucus nigra agglutinin) (5), Japanese elderberry lectin (SSA; S. sieboldiana agglutinin) (6), and Polyporus squamosus lectin (7) that are specific for NeuAc␣2,6Gal/GalNAc sequences; Maackia amurensis mitogen (MAL) that reacts with greatest affinity to the trisaccharide sequence NeuAc/Gc␣2,3Gal␤1,4GlcNAc/Glc, which is usually present in N-linked oligosaccharides (8), and the hemagglutinin from the same source (MAH) that displays higher affinity for a disialylated tetrasaccharide found in the O-linked oligosaccharide, NeuAc␣2,3Gal␤1,3(NeuAc␣2,6)GalNAc␣ (9). In contrast to these sequence-specific lectins, wheat germ lectin (WGA) and Limax flavus lectin have been used as general tools to bind sialylated glycoconjugates (10, 11). A mushroom lectin from Hericum erinaceum recognizes N-glycolylneuraminic acid...

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Sds-page and Binding Studies With Biotin-or Hrp-lectins On Tmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing TerminalN-Acetylneuraminic Acid α2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans

Ueda¹,

Matsumoto²,

Takahashi³

et al. 2002

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…Homodimer 4 Gal na Entomotoxic (Hamshou et al 2013;Hamshou et al 2010b;Hamshou et al 2012;Skamnaki et al 2013) Bleuler-Martinez et al 2011;Fujihashi et al 2003;Fukumori et al 1990;Kochibe and Furukawa 1980;Olausson et al 2010;Olausson et al 2008;Tateno et al 2009;Wimmerova et al 2003) GlcNAc-β1,4-X na nd (Cioci et al 2006;Ueda et al 1999a;Ueda et al 2002;Ueda et al 1999b;Ueda et al 2003) Entomotoxic (Birck et al 2004;Bleuler-Martinez et al 2011;Damian et al 2005;Francis et al 2003;Jaber et al 2008;Jaber et al 2007;…”

Section: β-Trefoilmentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

show abstract

Vitronectins produced by human cirrhotic liver and CCl₄‐treated rats differ in their glycosylation pattern and tissue remodeling activity

et al. 2019

Self Cite

View full text Add to dashboard Cite

Liver cirrhosis (LC) is a disease characterized by pathological accumulation and alteration of extracellular matrix (ECM) proteins; the interaction between two such proteins, collagen and vitronectin (VN), is considered to be the key to controlling ECM remodeling in liver cirrhosis. If it is possible to control the modification of oligosaccharides on VN, it may be possible to retard progression of liver cirrhosis. In this study, we examined the relationship between changes in VN glycosylation and activity related to the remodeling of hepatic tissue in human LC and a rat model of LC generated using carbon tetrachloride (CCl4). Plasma concentrations of VN in human LC declined to approximately two‐thirds that in normal plasma, but the ratio of active VN, which has collagen‐binding activities, increased 2.8 times in LC plasma. In contrast, purified LC‐VN exhibited similar binding activities toward type I, IV, and V collagens to those of normal VN. Lectin reactivities and carbohydrate analyses of LC‐VN revealed that branching, fucosylation, and sialylation of N‐glycans were higher than those of normal VN. On the other hand, the plasma level of rat CCl4‐VN increased and the ratio of active molecules to collagen in plasma decreased. Increased fucosylation of LC‐VN was not detected in carbohydrates of CCl4‐VN. The changes in rat VN due to CCl4 treatment did not correspond to the changes in plasma levels of human VN caused by LC, the ratio of active molecules, or carbohydrate composition, thereby indicating that CCl4‐treated rats are not an appropriate model for studying VNs in human LC. Glycosidase treatment of VNs supported the hypothesis that the collagen‐binding activity of VN is modulated by alterations of glycosylation during LC, which may contribute to (a) the matrix incorporation of VN and (b) tissue fibrosis.

show abstract

Interaction of a lectin from Psathyrella velutina mushroom with N‐acetylneuraminic acid

Cited by 38 publications

References 22 publications

Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing TerminalN-Acetylneuraminic Acid α2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans

Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing TerminalN-Acetylneuraminic Acid α2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Vitronectins produced by human cirrhotic liver and CCl₄‐treated rats differ in their glycosylation pattern and tissue remodeling activity

Contact Info

Product

Resources

About

Interaction of a lectin from Psathyrella velutina mushroom with N‐acetylneuraminic acid

Cited by 38 publications

References 22 publications

Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing TerminalN-Acetylneuraminic Acid α2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans

Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing TerminalN-Acetylneuraminic Acid α2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Vitronectins produced by human cirrhotic liver and CCl4‐treated rats differ in their glycosylation pattern and tissue remodeling activity

Contact Info

Product

Resources

About

Vitronectins produced by human cirrhotic liver and CCl₄‐treated rats differ in their glycosylation pattern and tissue remodeling activity