Isolation and characterization of a lectin from Grifola frondosa fruiting bodies

Kawagishi, Hirokazu; Nomura, Aya; Mizuno, Takashi; Kimura, Atsuo; Chiba, Seiya

doi:10.1016/0304-4165(90)90045-x

Cited by 114 publications

(56 citation statements)

References 27 publications

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“…From these results, the presence of stage-specific lectins in G. frondosa as in P. cornucopiae 8) appears unlikely. The purification and properties of a lectin from the fruiting body of G. frondosa have been reported, 11) but the properties were different somehow from those described in this paper.…”

Section: L S V G T T T I Q T R L I G Gcontrasting

confidence: 67%

“…1,2) Many lectins have been purified from basidiomycete mushrooms belonging to Agaricales, such as Agaricus campestris, 3) Flammulina velutipes, 4) Xerocomus chrysenteron, 5) Pleurotus cornucopiae, [6][7][8][9] and so on, but few from mushrooms belonging to Aphyllophorales. 10,11) We have reported that P. cornucopiae synthesizes two types of lectins in a developmental-stage-specific manner. One, named PCL-F, occurs in the fruiting body, and is synthesized after the fruiting body starts to form.…”

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confidence: 98%

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Characterization, Occurrence, and Molecular Cloning of a Lectin fromGrifola frondosa: Jacalin-Related Lectin of Fungal Origin

Nagata

Yamashita

Honda

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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Section: L S V G T T T I Q T R L I G Gcontrasting

confidence: 67%

mentioning

confidence: 98%

Characterization, Occurrence, and Molecular Cloning of a Lectin fromGrifola frondosa: Jacalin-Related Lectin of Fungal Origin

Nagata

Yamashita

Honda

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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“…N-acetyl-D-galactosamine specificity was exhibited by lectins from A. gorakhpurensis and A. carbonarius. GalNAc specific lectins have been reported from Ciborinia camelliae (Otta et al 2002) and Grifola frondosa fruiting bodies (Kawagishi et al 1990). This supports the increase in lectin titre upon neuraminidase treatment.…”

Section: Carbohydrate Specificity Of Aspergillus Lectinsmentioning

confidence: 99%

New lectins from aspergilli and their carbohydrate specificity

2013

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Lectin activity was assessed in sixteen Aspergillius species using human A, B, O, AB, rabbit, goat, pig and sheep erythrocytes. Neuraminidase and protease treated blood group O erythrocytes were also used to evaluate lectin activity from all the cultures unable to agglutinate native red blood cells. Lectin activity was revealed from Aspergillus acristatus, A. gorakhpurensis, A. panamensis and A. carbonarius extracts, while undiluted extract of A. fischeri showed weak haemagglutination. Lectin activity was expressed after 5 days of growth by A. acristatus, A. gorakhpurensis, A. panamensis and A. carbonarius and after 8 days of cultivation a sharp decline in lectin activity was observed. Higher titres were observed from these species with enzymatically modified blood type O erythrocytes. A variety of carbohydrates were used to study their minimum inhibitory concentration capable of inhibiting haemagglutination. Porcine stomach mucin was found to be the most potent inhibitor of all the lectins. A. gorakhpurensis lectin showed high specificity for chondroitin-6-sulphate and N-acetyl-D-galactosamine. Significant specificity for L-fucose, D-arabinose and 2-deoxy-D-ribose was identified with A. panamensis lectin. Low concentrations of 0.625 mM of D-galactosamine HCl and 0.12 mg/mL of chondroitin-6-sulphate were found optimal to prevent haemagglutination of A. carbonarius extract. A. carbonarius lectin was partially purified 2.75-fold using ammonium sulphate precipitation, dialysis and ultrafiltration. It was found to be stable upto 40• C and within the pH range of 7.0-8.0. Lectin activity was not affected by guanidine-HCl, while it was reduced to half after incubation with urea and thiourea after 24 h.

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“…They are currently attracting much interest on account of their many exploitable medicinal activities. The immunomodulatory and antitumor/cytotoxic activities of lectins from Agaricus bisporus (Yu et al, 1993(Yu et al, , 1999 Boletus satanas (Ennamany et al, 1994), Flammulina velutipes (Hsu et al, 1997), Ganoderma lucidum (Van et al, 1995), Grifola frondosa (Kawagishi et al, 1990), Tricholoma mongolium (Wang et al, 1995) and Volvariell volvacea (Lin et al, 1984) have been testified. A collagen-binding protein, which inhibits the lewis lung carcinoma cell adhesion to type IV collagen was isolated from Hypsizigus marmoreus (Tsuchida et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

A Lectin with Mycelia Differentiation and Antiphytovirus Activities from the Edible Mushroom Agrocybe aegerita

Sun

Zhao²,

Tong³

et al. 2003

BMB Reports

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A lectin named AAL has been purified from the fruiting bodies of the edible mushroom Agrocybe aegerita. AAL consisted of two identical subunits of 15.8 kDa, its pI was about 3.8 determined by isoelectric focusing, and no carbohydrate was discerned. Being treated by pyrogultamate aminopeptidase, the blocked N-terminus of AAL was sequenced as QGVNIYNI. AAL agglutinated human and animal erythrocytes regardless of blood type or animal species. Its hemagglutinating activity was unaffected by acid or alkali treatment and demetalization or addition of divalent metals Mg 2+, Ca 2+ and Zn 2+. AAL was toxic to mice: its LD50 was 15.85 mg per kilogram body weight by intraperitoneal injection. In this study, two novel activities of AAL were proved. It showed inhibition activity to infection of tobacco mosaic virus on Nicotiana glutinosa. The result of IEF suggested that AAL attached to TMV particles. Mycelia differentiation promotion was the other interesting activity. AAL promoted the differentiation of fruit body primordia from the mycelia of Agrocybe aegerita and Auricularia polytricha. AAL antiserum was prepared and immunologically crossreactived with several proteins from five other kinds of mushrooms. These results suggested that AAL probably was a representative of a large protein family, which plays important physiological roles in mushroom.

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Isolation and characterization of a lectin from Grifola frondosa fruiting bodies

Cited by 114 publications

References 27 publications

Characterization, Occurrence, and Molecular Cloning of a Lectin fromGrifola frondosa: Jacalin-Related Lectin of Fungal Origin

Characterization, Occurrence, and Molecular Cloning of a Lectin fromGrifola frondosa: Jacalin-Related Lectin of Fungal Origin

New lectins from aspergilli and their carbohydrate specificity

A Lectin with Mycelia Differentiation and Antiphytovirus Activities from the Edible Mushroom Agrocybe aegerita

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