Mycologia
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DOI: 10.3852/mycologia.98.2.167
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Mycologia, 98(2), 2006, pp. 167-171.
© 2006 by The Mycological Society of America

An agglutinin with mitogenic and antiproliferative activities from the mushroom Flammulina velutipes


T.B. Ng 1
Patrick H.K. Ngai

     Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China

Lixin Xia

     Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China, and College of Life Science, Shenzhen University, Shenzhen, China

   ABSTRACT
TOP
 ABSTRACT
INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 LITERATURE CITED
 

A hemagglutinin with a molecular mass of 12 kDa was isolated from the fruiting bodies of the mushroom Flammulina velutipes. Its molecular mass is similar to that of the fungal immunomodulatory protein isolated from F. velutipes (FIP-fve) with ice-cold 5% acetic acid and 50 mM 2-mercaptoethanol as extraction medium and to that of the larger 12 kDa subunit of F. velutipes lectin isolated with phosphate buffer as extraction medium. Its hemagglutinating activity cannot be inhibited by a variety of carbohydrates tested. The activity is stable between pH 4 and pH 11. Loss in activity occurred when the temperature is raised to 60 C and 70 C. Activity is indiscernible at and above 80 C. Its N-terminal sequence shows differences from that of FIP-fve. F. velutipes hemagglutinin stimulates [3H-methyl] thymidine uptake by mouse splenocytes. It inhibits proliferation of leukemia L1210 cells with an IC50 of 13 µM.

Key words: Agglutinin, Flammulina velutipes, isolation, mushroom


   INTRODUCTION
TOP
 ABSTRACT
 INTRODUCTION
MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 LITERATURE CITED
 
Flammulina velutipes is a common edible mushroom popular in the Orient. From it a ß-(1->3)-glucan with antitumor activity (Ikekawa et al 1982Go), a similar polysaccharide with antitumor activity (Leung et al 1997Go), and a protein-bound polysaccharide that can prolong the lifespan of mice challenged with leukemic cells (Otagiri et al 1983Go) have been isolated.

Several ribosome inactivating proteins have been purified from F. velutipes including flammulin (40 kDa) (Wang and Ng 2000Go), velutin (13.8 kDa) (Wang and Ng 2001Go), flammin (30 kDa) (Ng and Wang 2004Go) and velin (19 kDa) (Ng and Wang 2004Go). Velutin has been shown to inhibit HIV-1 reverse transcriptase (Wang and Ng 2001Go).

Other than the polysaccharides, protein-bound polysaccharides and ribosome inactivating proteins mentioned above, a lectin and a fungal immunomodulatory protein (FIP-fve) have been reported. The lectin, which has a molecular mass of 20 kDa, is composed of a 12 kDa subunit and a small 8 kDa subunit. Only the 12 kDa subunit exhibits hemagglutinating and mitogenic activities (Tsada 1979). The fungal immunomodulatory protein, which displays a molecular mass of 12 kDa, is similar to the 12 kDa subunit of the lectin in possessing hemagglutinating activity that cannot be inhibited by simple sugars and mitogenic activity toward lymphocytes (Ko et al 1995Go). Because the lectin was isolated with a procedure that involved extraction with phosphate buffer, whereas the purification protocol for FIP-fve entailed extraction with ice-cold 5% acetic acid and 50 mM 2-mercaptoethanol, it is possible that FIP-fve is in fact the 12 kDa subunit of F. velutipes lectin.

The purpose of the present study was to attempt to isolate and characterize a hemagglutinin/lectin from F. velutipes and compare its characteristics with similar proteins previously reported from the same mushroom species. Lectins have been purified from a number of mushroom species (Sage and Vazquez 1967Go; Tsuda 1979Go; Eifeer and Ziska 1980; Kawagishi et al 1988Go, 1990Go, 1994Go, 1997Go; Ko et al 1995Go; Wang et al 1995Go, 1996aGo, 1996bGo, 1997bGo, 1998bGo, 2002bGo, 2003Go; Zhuang et al 1996Go; Hsu et al 1997Go; Yagi et al 1997Go; She et al 1998Go; Wang et al 2000Go; Yu et al 2000Go; Kent et al 2003Go). The isolated F. velutipe lectin/hemagglutinin also will be compared with these mushroom lectins.


   MATERIALS AND METHODS
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
RESULTS
 DISCUSSION
 LITERATURE CITED
 
Isolation of hemagglutinin.— – Fresh fruiting bodies of needle mushroom (3 kg) were homogenized (3 mL/g) in 10 mM NH4OAc buffer (pH 4.6) with a Waring blender. The homogenate was centrifuged at 14 000 rpm for 30 min at 4 C. The supernatant was collected and loaded to a CM-cellulose column (2.5 x 20 cm) (Sigma). After removal of unabsorbed proteins, adsorbed proteins were fractionated with 0.2 M NaCl and then with 1.0 M NaCl in the same buffer. Fraction C2 containing hemagglutinating activity was collected and dialyzed against distilled water overnight.

Fraction C2 was dissolved in 10 mM NH4OAc buffer (pH 4.6) and loaded to a 1 mL Mono S column (Amersham). After the unbound fraction had been removed, the proteins were eluted with a linear gradient of 0.0–1.0 M NaCl in the same buffer. Fraction M4 containing hemagglutinating activity was collected and dialyzed against distilled water overnight.

Fraction M4 then was lyophilized and dissolved in 20 mM NH4HCO3 buffer (pH 9.0). It was purified further by gel filtration on a Superdex 75 HR 10/30 column (Amersham Biosciences) in the same buffer. The purified protein, which resided in fraction S1, was collected and stored at –70 C until further analysis.

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).— – SDS-PAGE was conducted according to the method of Laemmli and Favre (1973)Go. After electrophoresis the gel was stained with Coomassie brilliant blue. The molecular mass of the purified hemagglutinin was determined by comparison of its electrophoretic mobility with those of molecular mass marker proteins from Amersham Biosciences.

Amino acid sequence analysis.— – The N-terminal amino acid sequence of the purified hemagglutinin (ca. 500 picomoles) was analyzed by means of automated Edman degradation. Microsequencing was carried out with a Hewlett Packard 1000A protein sequencer equipped with an HPLC system. The initial and repetitive yields of the sequencing experiments exceeded 95% and 90%, respectively (Wang et al 2000Go).

Assay for hemagglutinating activity.— – In the assay for lectin (hemagglutinating) activity, a serial twofold dilution of the lectin solution in microtiter U-plates (50 µL) was mixed with 50 µL of a 2% suspension of rabbit red blood cells in phosphate buffered saline (pH 7.2) at 20 C. The results were read after about 1 h when the blank had fully settled into sediment. The hemagglutination titer, defined as the reciprocal of the highest dilution exhibiting hemagglutination, was reckoned as 1 hemagglutination unit or 1 titer. Specific activity is the number of hemagglutination units or titer per mg protein (Wang et al 2002Go).

Assay for mitogenic activity on mouse splenocytes.— – This assay was performed as described by Wang et al (Wang et al 2002Go). Splenocytes were isolated from BALB/c mice. The cells were diluted with RPMI medium containing 10% fetal bovine serum and seeded (2 x 106 cells/0.2 mL/well) in 96-well microplates. The hemagglutinin was added at various concentrations. Cells cultured in the absence of the lectin served as control. The cells wee incubated at 37 C in a humidified atmosphere of 5% carbon dioxide for 24 h. The cells were viable after 24 h. During the last 6 h, cells in one well were pulsed with 0.5 µCi of [3H-methyl]-thymidine (specific activity 5 µCi/mmol, Amersham Biosciences, England) in 10 µL and were harvested onto a glass fiber filter with a cell harvester. The radioactivity was determined with a Beckman scintillation counter. The proliferative (mitogenic) response was expressed as mean counts per min (cpm).

Assay of antiproliferative activity on tumor cell lines.— – The possible antiproliferative activity of the hemagglutinin was determined as follows. The cell lines HepG2 and L1210 were purchased from American Tissue Culture Collection. The lines were maintained in RPMI medium supplemented with 10% v/v fetal bovine serum (FBS), 100 mg/L streptomycin, and 100 IU/mL penicillin at 37 C in a humidified atmosphere of 5% (v/v) CO2. Cells (1 x 104) in their exponential growth phase were seeded in each well of a 96-well culture plate (Nunc, Denmark) and incubated 12 h before addition of the hemagglutinin. Incubation was carried out another 48 h. Radioactive precursor, 1 µCi ([methyl-3H]thymidine, Amersham Biosciences) was added to each well and incubated 12 h. The cultures were collected by a cell harvester. The incorporated radioactivity was determined by liquid scintillation counting (Wang et al 1995Go).


   RESULTS
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
DISCUSSION
 LITERATURE CITED
 
When the crude extract 173.5 mg protein with 147.6 hemagglutination titer/mg prepared from 3 kg fresh fruiting bodies of the mushroom Flammulina velutipes was subjected to ion exchange chromatography on a CM-cellulose column, three fractions were obtained, a large unadsorbed fraction C1 (92 mg) and two small adsorbed fractions eluted with 0.2 M and 1.0 M NaCl, named C2 (65 mg) and C3 (18 mg) respectively. C2 was the only fraction with hemagglutinating activity (1960 titer/mg). C2 then was chromatographed on a Mono S column, and 10 mM NH4OAc buffer (pH 4.6) was used to elute the column yielding a large unabsorbed fraction M1 (20 mg). The column was eluted with 0.0–1.0 NaCl in the same buffer. Three smaller adsorbed fractions, M2 (9.6 mg), M3 (13.6 mg) and M4 (17.5 mg) were obtained. Only the most tightly bound fraction M4 contained hemagglutinating activity (5885 titer/mg). Gel filtration of fraction M4 yielded a single sharp peak, S1 (11.3 mg, 88/3 titer/mg). SDS-PAGE revealed that the molecular mass of the hemagglutinin was below 14.4 kDa. The molecular mass was estimated to be 12 kDa by gel filtration on Superdex 75 column which had been calibrated with molecular markers. The sequence of the first 10 N-terminal amino acids was determined (TABLE IGo). It showed similarity to fungal immunomodulatory proteins from the mushrooms Flammulina velutipes, Volvariella volvacea and Ganodema lucidum, a hemagglutinin-like protein from Xylella fastidiosa Temecula1 and a disease-resistant protein from Oryza sativa (japonica cultivar-group).


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  		TABLE I. Comparison of N-terminal sequence of hemagglutinin from the golden needle mushroom Flammulina velutipes (FVA) with proteins from other sources (results of BLAST search)

 
Flammulina velutipes hemagglutinin was stable in the temperature range 25–50 C. Loss in activity was observed when the temperature was increased to 60 C and beyond. Activity was undetectable at and above 80 C. The activity was stable at pH 4–11, 25 C for 30 min. It was reduced at pH 3 and pH 12. Trypsin treatment (1 : 1, w : w, 37 C for 30 min) enhanced the hemagglutinating activity of FVA from a hemagglutination titer of 3–5. The hemagglutinin elicited a weaker mitogenic response than Con A from mouse splenocytes (FIG. 1Go). It inhibited proliferation of L1210 cells with an IC50 of 13 µM (FIG. 2Go).


Figure 1
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  		FIG. 1. Induction of mitogenic response from mouse splenocytes by Flammulina velutipes hemagglutinin as reflected by incorporation of [3H-methyl]thymidine. Results represent mean ± SD (n = 3).

 

Figure 2
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  		FIG. 2. Antiproliferative activity of Flammulina velutipes hemagglutinin (FVA) toward tumor cells. Results represent mean ± SD (n = 3).

 

   DISCUSSION
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
LITERATURE CITED
 
Hemagglutinin obtained in this study, designated as F. velutipes hemagglutinin (FVA), was isolated with a procedure (Ko et al 1995Go) that did not involve acids such as acetic acid and reducing agents such as 2-mercaptoethanol. It is a single-chain 12 kDa protein like FIP-fve (Tsuda 1979Go) and unlike the dimeric 20 kDa lectin prepared with ice-cold 5% acetic acid and 50 mM 2-mercaptoethanol in the extraction medium. Thus it is unlikely that FVA is a subunit formed in an acidic medium from an initially dimeric molecule. Its N-terminal sequence however does not closely resemble that of FIP-fve. Like both F. velutipes lectin and FIP-fve its hemagglutinating activity is not inhibited by simple sugars and it stimulates the mitogenic response of lymphocytes/splenocytes. The discrepancy between the sequence data from the present study and those from the earlier reports may be due to the different strains of F. velutipes used in the different studies.

It is shown in this investigation that the hemagglutinating activity of FVA, like that of red kidney bean hemagglutinin (Ye and Ng 2001Go), can be inhibited by lactoferrin, a milk glycoprotein. FVA is a fairly stable hemagglutinin with regard to pH variation. However it can withstand heat treatment only up to 50 C without loss of hemagglutinating activity, indicating a low thermostability.

The results of the trypsinization experiment indicate that the hemagglutinating activity of FVA is not adversely affected. Because after trypsin treatment of the hemagglutinin the enzyme was not inactivated or removed before incubation with erythrocytes, the enzyme might have exposed some cryptic sites on the red cells and thus enhanced the hemagglutinating activity of FVA.

A potentially exploitable activity of FVA, other than its mitogenic activity toward splenocytes, is its antiproliferative activity toward leukemia (L1210) cells. The latter activity is achieved at micromolar concentration. The antiproliferative (Kawagishi et al 1990Go, Yu et al 1993Go, Parslew et al 1999Go, Wang et al 2000Go, Yu et al 2000Go, Battery et al 2002, Mahajan et al 2002Go, Kent et al 2003Go, Ngai and Ng 2004Go) and antitumor (Wang et al 1996Go, 1997Go; Zhao et al 2003) activities of some mushroom lectins have been reported. Some lectins demonstrate antifungal activity (Gozia et al 1993Go, Ciopraga et al 1999Go, Ye et al 2001Go). Others may show anti-HIV-1 activity (Hansen et al 1991Go, Corbean et al 1994, Charan et al 2000Go, Lopez et al 2003Go). Yet FVA exhibits neither antifungal nor HIV-1 reverse transcriptase inhibitory activity.

The previously reported FIP-fve and F. velutipes lectin were not tested for pH stability, thermostability, antiproliferative activity against tumor cells and antifungal activity. The present study served to fill these gaps in knowledge about F. velutipes agglutinin.

F. velutipes lectin isolated in this study has fairly high pH stability and trypsin stability. Hence its mitogenic activity toward splenocytes and antiproliferative activity toward tumor cells add to the health promoting value of F. velutipes, a popular edible mushroom.


   ACKNOWLEDGMENTS
 
The expert secretarial assistance of Miss Fion Yung is deeply appreciated.


   FOOTNOTES
 
Accepted for publication January 1, 2006.

1 Corresponding author. E-mail: b021770{at}mailserv.cuhk.edu.hk


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 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 LITERATURE CITED
 
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