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1 Microbial Physiology
2 Lectin activity in mycelial extracts of Fusarium
3 species
∗
4 Q1 Ranjeeta Bhari, Bhawanpreet Kaur, Ram S. Singh
5 Q2 Carbohydrate and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala, Punjab, India
6
7 a r t i c l e i n f o a b s t r a c t
8
9 Article history: Lectins are non-immunogenic carbohydrate-recognizing proteins that bind to glycopro-
10 Received 25 February 2015 teins, glycolipids, or polysaccharides with high affinity and exhibit remarkable ability
11 Accepted 12 November 2015 to agglutinate erythrocytes and other cells. In the present study, ten Fusarium species
12 Available online xxx previously not explored for lectins were screened for the presence of lectin activity. Mycelial
extracts of F. fujikuroi, F. beomiformii, F. begoniae, F. nisikadoi, F. anthophilum, F. incarnatum,
Associate Editor: Rosana Puccia
and F. tabacinum manifested agglutination of rabbit erythrocytes. Neuraminidase treatment
13
of rabbit erythrocytes increased lectin titers of F. nisikadoi and F. tabacinum extracts,
14 Keywords:
whereas the protease treatment resulted in a significant decline in agglutination by most
15 Fusarium
of the lectins. Results of hapten inhibition studies demonstrated unique carbohydrate
16 Lectin
specificity of Fusarium lectins toward O-acetyl sialic acids. Activity of the majority of
17 Hemagglutination
Fusarium lectins exhibited binding affinity to d-ribose, l-fucose, d-glucose, l-arabinose, d-
18 Carbohydrate specificity
mannitol, d-galactosamine hydrochloride, d-galacturonic acid, N-acetyl-d-galactosamine,
19 Culture age
N-acetyl-neuraminic acid, 2-deoxy-d-ribose, fetuin, asialofetuin, and bovine submaxillary
mucin. Melibiose and N-glycolyl neuraminic acid did not inhibit the activity of any of the
Fusarium lectins. Mycelial extracts of F. begoniae, F. nisikadoi, F. anthophilum, and F. incarnatum
interacted with most of the carbohydrates tested. F. fujikuroi and F. anthophilum extracts
displayed strong interaction with starch. The expression of lectin activity as a function
of culture age was investigated. Most species displayed lectin activity on the 7th day of
cultivation, and it varied with progressing of culture age.
© 2016 Published by Elsevier Editora Ltda. on behalf of Sociedade Brasileira de
Microbiologia. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
1
molecules in cell–cell or cell–matrix interactions. Microbial 22
Introduction
lectins include various agglutinins, adhesins, precipitins, tox- 23
2
ins, and enzymes and occur widely in bacteria, protozoa, 24
20 Lectins are carbohydrate-binding proteins or glycoproteins of 3
viruses, and fungi. Lectins have applications in blood typ- 25
21 non-immune origin that play an important role as recognition
ing and are known to exert essential functions in the immune
∗
Corresponding author.
E-mail: [email protected] (R.S. Singh).
http://dx.doi.org/10.1016/j.bjm.2016.04.024
1517-8382/© 2016 Published by Elsevier Editora Ltda. on behalf of Sociedade Brasileira de Microbiologia. This is an open access article
under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Please cite this article in press as: Bhari R, et al. Lectin activity in mycelial extracts of Fusarium species. Braz J Microbiol. (2016),
http://dx.doi.org/10.1016/j.bjm.2016.04.024 BJM 101 1–6
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26 recognition process of viral, bacteria, mycoplasmal, and par- Lectin extraction 80
27 asitic infections, as well as in fertilization, cancer metastasis,
4,5
28 and growth and differentiation several cells. After plants, The mycelium was homogenized in PBS (1:1.5, w/v) using an 81
®
29 mushrooms are the most widely studied group of organisms ultra-high speed homogenizer (Ultra-Turrax T25 basic, IKA- 82
30 for lectins, and these lectins have gained considerable atten- Werke, Staufen, Germany) and then ground in mortar and 83
6,7 19
31 tion due to their promising biological activities. Yeast lectins pestle with acidified river sand for 30 min. The extract was 84
◦
32 are known to be involved in cell–cell interactions, pathogene- centrifuged (3000 × g, 20 min, 4 C), and the supernatant was 85
8
33 sis, and cell flocculation. The mitogenic potential of microbial assayed for lectin activity. 86
34 lectins has been well established as well as their ability to
9
35 induce mitosis in lymphocytes/splenocytes. Hemagglutination assay 87
36 There are several reports regarding lectins from micro-
10 11,12 ◦
37 fungi, including Rhizopus stolonifer, Aspergillus fumigatus, Blood samples drawn in Alsever’s solution were stored at 4 C 88
13 14 15
38 A. oryzae, Penicillium marneffei, P. thomii and P. griseofulvum, until further use. Erythrocyte suspension (2%, v/v) was pre- 89
16 17
39 Sclerotium rolfsii and Fusarium solani. Additionally, micro- pared in PBS, and two-fold serially diluted mycelial extract 90
40 fungi exhibiting lectin activity and their possible functions was tested for agglutination of human, goat, pig, sheep, and 91
18 19
41 have been reviewed exhaustively by our group. Singh rabbit erythrocytes. The surfaces of human and rabbit eryth- 92
19–21
42 et al. screened 40 species of Aspergillus for the pres- rocytes were modified with the enzymes, neuraminidase and 93
27
43 ence of lectin activity and discovered wide occurrence protease, as described by Meng et al. and used in the aggluti- 94
44 of lectins in this genera. Few of them have also been nation assay. Hemagglutination was determined visually by an 95
22–24
45 evidenced to possess mitogenic and immunomodulatory appearance of mat formation as an indicative a lectin activity, 96
25
46 properties. whereas button formation was taken as an absence of lectin 97
26
47 Recently, Singh and Thakur reported lectin activity in activity. Lectin titer was defined as inverse of the highest dilu- 98
48 mycelial extracts of eight Fusarium species, namely F. acumi- tion capable of producing visible agglutination of erythrocytes. 99
49 natum, F. chlamydosporium, F. compactum, F. crookwellense, F.
50 culmorum, F. dimerum, F. decemcellulare, and F. coeruleum. The Hapten inhibition assay 100
51 present study attempted to explore lectin activity in ten
52 species of Fusarium, which have been not investigated earlier. Hapten inhibition assay was carried out against a panel of 101
53 The lectins were characterized with respect to their biological carbohydrates according to a method described by Singh 102
19
54 spectrum and carbohydrate inhibition profile. The expres- et al. Lectin was incubated for 1 h with an equal volume of 103
55 sion of lectin activity with respect to culture age was also the test solution in the wells of U-bottom microtiter plates. 104
56 investigated. The present examination could provide useful Erythrocyte suspension was added and hemagglutination was 105
57 information for cataloging lectins and prompt further research established visually following 30 min of incubation. Button for- 106
58 on the possible roles and applications of the lectins isolated mation in the presence of carbohydrates indicated specific 107
59 from Fusarium sp. interaction, while mat formation was taken an absence of 108
interaction between the lectin and the carbohydrate. The min- 109
imum inhibitory concentration (MIC) of each of the specific 110
Materials and methods carbohydrates was determined by serial double dilution of the 111
test solution. MIC was defined as the lowest concentration of 112
60 Maintenance, growth and harvesting of microbial cultures the carbohydrate capable of inducing complete inhibition of 113
lectin-mediated hemagglutination. 114
61 Ten Fusarium species, namely F. fujikuroi (MTCC 9930), F. beomi- The carbohydrates tested as inhibitors were: d-ribose, 115
62 formii (MTCC 9946), F. diaminii (MTCC 9937), F. annulatum (MTCC l-rhamnose, xylose, l-fucose, d-glucose, d-mannose, d- 116
63 9951), F. begoniae (MTCC 9929), F. nisikadoi (MTCC 9948), F. arabinose, l-arabinose, d-galactose, d-fructose, d-mannitol, 117
d
64 staphyleae (MTCC 9911), F. anthophilum (MTCC 10129), F. incar- -sucrose, d-maltose, d-lactose, melibiose, d-trehalose 118
65 natum (MTCC 10292), and F. tabacinum (MTCC 10131) were dihydrate, d-raffinose, maltotriose, inositol, meso-inositol, d- 119
66 procured from Microbial Type Culture Collection (MTCC), Insti- glucosamine hydrochloride, d-galactosamine hydrochloride, 120
67 tute of Microbial Technology, Chandigarh, India. All strains d-glucuronic acid, d-galacturonic acid, N-acetyl-d- 121
68 were maintained on potato dextrose agar slants contain- glucosamine, N-acetyl-d-galactosamine, 2-deoxy-d-glucose, 122
69 ing potato 20.0%, dextrose 2.0%, and agar 2.0%; pH of the 2-deoxy-d-ribose, porcine stomach mucin, bovine submaxil- 123
70 medium was adjusted to 5.6. Agar slants were stored at lary mucin, fetuin, asialofetuin, inulin, pullulan, starch, 124
◦
±
71 4 1 C, until further use and were subcultured regularly chondroitin-6-sulphate, N-acetyl neuraminic acid, and N- 125
72 at an interval of two weeks. The cultures were grown in glycolyl neuraminic acid. Simple sugars were tested at a 126
73 Erlenmeyer’s flasks (250 mL) containing 100 mL of mainte- final concentration of 100 mM, whereas glycoproteins and 127
◦
74 nance medium without agar and were incubated at 25 C polysaccharides were analyzed at a final concentration of 128
75 under stationary conditions for 7 and 10 days, respectively. 1 mg/mL. 129
76 Mycelium was harvested by filtration, washed thoroughly
77 with phosphate buffered saline (PBS, 0.1 M, pH 7.2), and Lectin activity as a function of culture age 130
78 briefly pressed between the folds of filter paper. The culture
79 supernatant was separately collected and assayed for lectin The activity of lectin-positive cultures was determined as a 131
28
activity. function of the mycelial growth, as described by Singh et al. 132
Please cite this article in press as: Bhari R, et al. Lectin activity in mycelial extracts of Fusarium species. Braz J Microbiol. (2016),
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133 Erlenmeyer flasks (250 mL) containing 50 mL medium were 140
Native erythrocytes
134 inoculated with culture discs of 5 mm diameter (containing 120
135 Neuraminidase treated erythrocytes mycelium and agar) and incubated over a period of 5–12 days 100
◦
136 at 30 C, under stationary condition. Mycelium was recov-
80 Protease treated erythrocytes
137 ered at 24 h intervals, homogenized in PBS (1:1.5, w/v), and
60
138 then ground in mortar and pestle with acidified river sand for
40
139 30 min. Lectin titer in the extracts was determined. For each
Lectin activity (Titre)
140 fungal culture, an identical amount of biomass was invariably 20
141 taken in same quantity of PBS over the days to determine the 0
142 comparative hemagglutination as a function of culture age.
F. fujikuroi F. begoniae F. nisikadoi F. tabacinum F. incarnatum F. beomiformii F. anthophilum
Results
Fig. 1 – Effect of enzyme-treatment on agglutination of
rabbit erythrocytes by Fusarium spp. Erythrocytes were
143 Screening of fungal cultures for the presence of lectin
treated with protease (2 mg/mL) or neuraminidase
144 activity
(0.2 IU/mL) and suspensions were used in
hemagglutination assay.
145 Ten species of Fusarium were screened for their ability to
146 agglutinate rabbit, goat, sheep, pig, and human (A, B, AB,
147 and O) erythrocytes. No lectin activity in the culture super-
148 natant was displayed by these Fusarium species, whereas of lectins from other Fusarium spp. was reduced after protease 168
149 mycelial extracts of seven species, namely F. fujikuroi, F. treatment. 169
150 beomiformii, F. begoniae, F. nisikadoi, F. anthophilum, F. incarna-
151
tum, and F. tabacinum were found to agglutinate only rabbit Carbohydrate inhibition assay 170
152 erythrocytes (Table 1); and no agglutination was observed
153
with other erythrocytes. Hemagglutination assay was also Carbohydrate specificity profile of Fusarium lectins is pre- 171
154
performed using neuraminidase and protease-treated rabbit sented in Table 2. Few Fusarium lectins displayed exceedingly 172
155
and human erythrocytes. None of the extracts agglutinated rare carbohydrate specificities. Lectin activity of the majority 173
156
even the enzyme-treated human erythrocytes. Agglutination of Fusarium species was inhibited by d-ribose, l-fucose, d- 174
157
of enzyme-treated rabbit erythrocytes with Fusarium lectins glucose, l-arabinose, d-mannitol, d-galactosamine hydrochlo- 175
158
showed a variable response. Lectin extracts of F. anthophilum ride, d-galacturonic acid, N-acetyl-d-galactosamine, N-acetyl 176
159
exhibited a 4-fold increase in the titer with neuraminidase- neuraminic acid, 2-deoxy-d-ribose, fetuin, and asialofetuin. 177
160
treated erythrocytes, whereas that of F. nisikadoi and F. tabac- F. begoniae, F. anthophilum, and F. incarnatum extracts inter- 178
161
inum showed only a 2-fold increase (Fig. 1). However, the titer acted with most of the sugars tested. d-Mannose could 179
162
of F. incarnatum mycelial extracts was substantially reduced slightly inhibit the activity of F. nisikadoi lectins. d-Galactose 180
163
d
by neuraminidase-modified erythrocytes. Lectin titers of F. and -trehalose dihydrate suppressed the activity of F. bego- 181
164
fujikuroi, F. beomiformii, and F. begoniae extracts manifested no niae lectin. Porcine stomach mucin was inhibitory to F. 182
165
effect of the treatment with neuraminidase on erythrocytes. anthophilum and F. begoniae lectins. However, activity of all 183
166
F. fujikuroi and F. tabacinum extracts displayed titers similar to of the Fusarium lectins was inhibited by bovine submaxil- 184
167
those of native and protease-treated erythrocytes. The activity lary mucin. Melibiose and N-glycolyl neuraminic acid did 185
not suppress the action of any of the lectins. F. fujikuroi, F. 186
beomiformii, and F. tabacinum lectins interacted with only few 187
of the carbohydrates examined. The activity of F. fujikuroi 188
lectin was inhibited by d-galacturonic acid, d-galactosamine 189
Table 1 – Lectin activity of Fusarium spp. with rabbit
erythrocytes. hydrochloride, fetuin, and asialofetuin with respective MICs of 190
3.12 mM, 1.56 mM, 31.25 g/mL, and 250 g/mL. The lectins of 191
Species Lectin activity (Titer)
F. fujikuroi and F. anthophilum strongly interacted with starch, 192
7 days 10 days
and MICs of 1.95 g/mL and 3.90 g/mL, respectively, were 193
observed. 194
F. fujikuroi 0 4
F. beomiformii 8 16
F. begonia 8 16 Lectin activity of Fusarium sp. as a function of growth 195
F. nisikadoi 8 32
F. tabacinum 32 4
Lectin activity was determined over a period of 5–12 days to 196
F. anthophilum 16 2
determine the influence of culture age on lectin expression. 197
F. incarnatum 8 32
Lectin activity was expressed by 7-day old cultures of all Fusa- 198
F. diaminii 0 0
199
F. annulatum 0 0 rium lectins except for F. fujikuroi, where lectin activity was
F. staphyleae 0 0 expressed only by 9–10 days old cultures (Fig. 2). F. anthophilum 200
and F. tabacinum lectins displayed maximum activity after 7–8 201
Lectin activity was determined by hemagglutination assay. The
days of cultivation. F. incarnatum expressed a consistently high 202
mycelial extracts were prepared from 7 day and 10 day-old cultures.
titer in 8–10 days old cultures.
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Table 2 – Carbohydrate specificity of Fusarium spp. lectins.
Carbohydrate F. fujikuroi F. beomiformii F. begoniae F. nisikadoi F. anthophilum F. tabacinum F. incarnatum
d-Ribose – – 25 mM 3.12 mM 12.5 mM 6.25 mM 6.25 mM
l-Rhamnose – – 3.12 mM 6.25 mM 3.12 mM – –
Xylose – – 50 mM 3.12 mM 25 mM – –
l-Fucose – – 12.5 mM 3.12 mM 12.5 mM – 12.5 mM
d
-Glucose – – 50 mM 1.56 mM 3.12 mM – 3.12 mM
d
-Mannose – – – 25 mM – – –
d-Arabinose – – – 25 mM 12.5 mM – 12.5 mM
l-Arabinose – – 12.5 mM 12.5 mM 50 mM – 50 mM
d-Galactose – – 12.5 mM – – – 50 mM
d-Fructose – – 1.56 mM – – 50 mM 12.5 mM
d-Mannitol – – 3.12 mM – 50 mM 0.78 mM 25 mM
d-Sucrose – – 12.5 mM – 6.25 mM – –
d-Maltose – – 3.12 mM – 1.56 mM – –
d-Lactose – 3.12 mM 50 mM – – – –
Melibiose – – – – – – –
d-Trehalose dehydrate – – 1.56 mM – – – –
d-Raffinose – – 3.12 mM – – 3.12 mM 0.78 mM
Maltotriose – – 12.5 mM – 12.5 mM – –
Inositol – – 12.5 mM – – – 12.5 mM
Meso-inositol – – 6.25 mM – – – 25 mM
d
-Glucosamine – – 25 mM 6.25 mM – – – hydrochloride
d
-Galactosamine 3.12 mM 12.5 mM 25 mM 12.5 mM 6.25 mM – 6.25 mM hydrochloride
d
-Glucuronic acid – – 12.5 mM – 3.12 mM – 25 mM
d-Galacturonic acid 1.56 mM 1.56 mM 6.25 mM – 50 mM – 50 mM
N-acetyl-d-glucosamine – – 12.5 mM 25 mM – – –
N-acetyl-d-galactosamine – 12.5 mM 6.25 mM 25 mM 12.5 mM – 12.5 mM
2-Deoxy-d-glucose – – 25 mM 12.5 mM – 250 g/mL –
2-Deoxy-d-ribose – – 25 mM 125 g/ml 25 mM – 12.5 mM
N-acetyl neuraminic acid – 12.5 mM 0.195 mM 12.5 mM 3.90 mM – –
N-glycolyl neuraminic acid – – – – – – –
Bovine submaxillary mucin 31.25 g/mL 0.975 g/mL 0.06 g/mL 0.487 g/mL 0.12 g/mL 62.5 g/mL 31.25 g/mL
Porcine stomach mucin – – 0.975 g/mL – 0.975 g/mL – –
Fetuin 125 g/mL 500 g/mL 0.243 g/mL – 0.121 g/mL 500 g/mL –
Asialofetuin 250 g/mL 250 g/mL 0.487 g/mL 125 g/mL 0.975 g/mL – 31.25 g/mL
Chondroitin-6-sulphate – – 500 g/mL – 15.62 g/mL – 31.25 g/mL
Inulin – – 125 g/mL – 125 g/mL – 500 g/mL
Pullulan – – 500 g/mL – – 15.62 g/mL 62.5 g/mL
Starch 1.95 g/mL – 500 g/mL – 3.90 g/mL – –
Note: –, non-inhibitory carbohydrates.
Simple sugars were tested at a final concentration of 100 mM, while glycoproteins and polysaccharides were tested at a concentration of
1 mg/mL. The test solutions were as two-fold serially diluted across the wells of microtiter plates and incubated with appropriately diluted
lectin to determine minimum inhibitory concentration of specific carbohydrate.
lectins mostly agglutinate human and rabbit erythrocytes, 217
Discussion
and only a few of them could agglutinate sheep, goat, and 218
17,30
porcine erythrocytes. Khan et al. found that Fusarium solani 219
203 The present study reports lectin activity from seven Fusa-
lectin agglutinated only pronase- or neuraminidase-treated 220
204 rium species, namely, F. fujikuroi, F. beomiformii, F. begoniae, F.
human erythrocytes. Considering these findings, the hemag- 221
205 nisikadoi, F. anthophilum, F. incarnatum, and F. tabacinum, the
glutination activity of each extract was also tested against 222
206 presence of lectins in these species has not been explored
neuraminidase- or protease-treated human erythrocytes, but 223
207 previously. Our results and those of previous investigations
26 lectins failed to agglutinate even the enzyme-modified human 224
208 conducted by Singh and Thakur demonstrate a wide pres-
erythrocytes. 225
209 ence of mycelial lectins in Fusarium species. In the present
Neuraminidase removes sialic acid from the surface of 226
210 study, lectins from all the seven species were found to agglu-
erythrocytes and exposes subterminal galactosyl residues, 227
211 tinate only rabbit erythrocytes, and no agglutination with
thus reducing the net negative charge on the surface of 228
212 human, goat, sheep, and pig erythrocytes was observed.
31
29 erythrocytes and increasing their agglutination ability. The 229
213 Ishikawa and Oishi reported agglutination of chick, horse
decrease in agglutination of erythrocytes after the protease 230
214 and rabbit erythrocytes by culture filtrate of Fusarium sp.,
treatment indicates the removal of the preferred binding 231
215 whereas the cell extract was capable of agglutinating human
26 sites for Fusarium lectins. The treatment of erythrocytes with 232
216 erythrocytes. Singh and Thakur evidenced that Fusarium
Please cite this article in press as: Bhari R, et al. Lectin activity in mycelial extracts of Fusarium species. Braz J Microbiol. (2016),
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35 F. fujikuroi However, inhibition by asialofetuin corroborates the earlier 261
findings, where lectins specific for sialic acid also manifested 262 30 F. beomiformii
34,35
F. begonia inhibition by the asialo form glycoproteins. 263
25
F. tabacinum The results of the present investigation suggest an affin- 264
20 ity of Fusarium lectins to O-acetyl neuraminic acid, which is 265
also reflected in the erythrocyte specificity. The lectins bound 266
15
to rabbit erythrocytes, which contain N-O-acetyl neuraminic 267
10 acid. Human A, O, sheep, and goat erythrocytes have sur- 268
Lectin activity (Titre) 32
face glycoconjugates rich in N-acetyl neuraminic acid, which 269
5
might have been responsible for the failure of lectins to agglu- 270
0 tinate these erythrocytes. However, the augmentation of lectin 271
5 6 7 8 9 10 11 12
titer after the neuraminidase treatment and the fine speci- 272
Culture age (Days)
ficity of Fusarium lectins cannot be completely explained at 273
this point. These might be due to the presence of more than 274
35
F. nisikadoi one lectin in the extracts tested. 275
30 F. anthophilum Fusarium lectins were found to be developmentally reg- 276
ulated. There was no increase in lectin activity with the 277
25 F. incarnatum
progressing culture age and a corresponding rise in the protein 278
20
content of mycelia, indicating that the lectin activity was not 279
280
15 a function of growth rate alone. The developmental regulation
of Fusarium lectins corroborates to earlier reports on Fusarium 281
10 26 15,21,28,36,37
sp. and other microfungi. 282
Lectin activity (Titre)
5 In the present study, the large number of lectin-positive 283
species capable of agglutinating only rabbit erythrocytes indi- 284
0
5 6 7 8 9 10 11 12 cates a high incidence of sialic acid-specific lectins amongst 285
Culture age (Days) the members of this genus. Although hemagglutinating activ- 286
ity is not a powerful tool to define minor differences in affinity 287
Fig. 2 – Effect of culture age on lectin activity of Fusarium
between different molecules, recognition of different glycan 288
spp. The mycelia were recovered after 24 h intervals over a
structures suggests the widespread occurrence of receptors 289
period of 5–12 days and disrupted to assay lectin activity.
for Fusarium lectins. Normal tissues have N-acetyl neuraminic 290
32
acid, whereas malignant cells contain O-acetyl sialic acid. 291
These lectins can be a valuable tool for localization and assess- 292
233 neuraminidase was also reported to increase the titers of ment of glycoconjugates containing O-acetyl sialic acid. The 293
234 Fusarium lectins, whereas no such effect was established after unique carbohydrate specificity of Fusarium lectins invites fur- 294
26
235 protease treatments. ther research on this genus. The carbohydrate specificities and 295
236 In the present study, the majority of lectins were inhibited hemagglutination profiles indicate that more than one lectin 296
237 by d-galactosamine hydrochloride, N-acetyl-d-galactosamine, may be present in the extracts. However, further investigations 297
238 asialofetuin, and fetuin. Most of the lectins manifested inhibi- are required to establish the subtle saccharide specificity of 298
239 tion by free sialic acid, which was contrary to earlier findings Fusarium lectins reported herein. 299
26 30
240 of Singh and Thakur. Khan et al. reported specificity of
241 Fusarium solani lectin to N-linked glycans. The lectins in this
Q3
Conflicts of interest
242 study did not interact with N-glycolyl neuraminic acid, which
243 explains the failure of lectins to agglutinate porcine eryth-
The authors declare no conflicts of interest. 300
244 rocytes. Bovine submaxillary mucin is a potent inhibitor of
245 Fusarium lectins, whereas porcine stomach mucin is a weak
246 inhibitor. The former contains N-acetyl neuraminic acid, N- Acknowledgement
247 glycolyl neuraminic acid, N-acetyl 9-O-acetyl neuraminic acid,
248
and 8,9-di-O-acetyl neuraminic acid. On the other hand, Authors are thankful to Head, Department of Biotechnology, 301
249
mucin from porcine stomach contains 90% N-glycolyl neu- Punjabi University, Patiala for providing the necessary labora- 302
250
raminic acid, 10% N-acetyl neuraminic acid, and traces of tory facilities during the whole course of the study. 303
32
251 N-acetyl 9-O-acetyl neuraminic acid. Free N-acetyl neu-
304
252 raminic acid could inhibit the activity of few Fusarium lectins,
r e f e r e n c e s
253 but N-glycolyl neuraminic acid had no inhibitory effect, which
305
254 justifies the strong inhibitory potential of N-acetyl neuraminic
255 acid containing glycoprotein bovine submaxillary mucin and
1. Sharon N, Lis H, eds. Lectins. Amsterdam: Kluwer Scientific 306
256 weak binding with porcine stomach mucin. Fetuin mainly con-
Publishers; 2003. 307
33
257 tains N-glycolyl neuraminic acid, and most of the lectins
2. Lakhtin VM. Molecular organization of lectins. Mol Biol 308
258
discovered in representative Fusarium species showed only (Moscow). 1994;28:245–273. 309
259 weak interaction with fetuin. The results depict the inhibition 3. Singh RS, Tiwary AK, Kennedy JF. Lectins: sources, activities, 310
311
260 of lectin activity of Fusarium extracts by sialoglycoconjugates. and applications. Crit Rev Biotechnol. 1999;19:145–178.
Please cite this article in press as: Bhari R, et al. Lectin activity in mycelial extracts of Fusarium species. Braz J Microbiol. (2016),
http://dx.doi.org/10.1016/j.bjm.2016.04.024 BJM 101 1–6
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characterization of a mucin-binding mycelial lectin from
Please cite this article in press as: Bhari R, et al. Lectin activity in mycelial extracts of Fusarium species. Braz J Microbiol. (2016),
http://dx.doi.org/10.1016/j.bjm.2016.04.024 BJM 101 1–6