TY - JOUR
T1 - Lectin of Sclerotium rolfsii
T2 - its purification and possible function in fungal‐fungal interaction
AU - Barak, R.
AU - Chet, I.
PY - 1990/7
Y1 - 1990/7
N2 - The soil‐borne plant pathogenic fungus, Sclerotium rolfsii, produces a lectin which is strongly associated with the fungal β‐1,3‐glucan. The chitin synthetase inhibitors, polyoxin D and nikkomycin decrease the production of β‐1,3‐glucan by the fungus but increase the titre of the excreted lectin. On the other hand, the competitive inhibitor of glucose, 2‐deoxyglucose, decreases the production of both β‐1,3‐glucan and the lectin. The inhibition of glucan synthesis by polyoxin D was used for separation of the lectin from the glucan. For purification, the fungus was grown in synthetic medium supplemented with 5 × 10−6 mol/l polyoxin D and the crude lectin was puried on a column of Sephadex G‐75. SDS‐PAGE of the purified lectin showed two protein bands with the molecular weights of 55 000 and 60 000. The location of the lectin on S. rolfsii hyphae and its adsorption to conidia of Tri‐choderma were determined by indirect imrnunofluorescence, with antiserum raised against the purified lectin. The possible role of this lectin in S. rolfsii‐Trichoderma cell interaction is discussed.
AB - The soil‐borne plant pathogenic fungus, Sclerotium rolfsii, produces a lectin which is strongly associated with the fungal β‐1,3‐glucan. The chitin synthetase inhibitors, polyoxin D and nikkomycin decrease the production of β‐1,3‐glucan by the fungus but increase the titre of the excreted lectin. On the other hand, the competitive inhibitor of glucose, 2‐deoxyglucose, decreases the production of both β‐1,3‐glucan and the lectin. The inhibition of glucan synthesis by polyoxin D was used for separation of the lectin from the glucan. For purification, the fungus was grown in synthetic medium supplemented with 5 × 10−6 mol/l polyoxin D and the crude lectin was puried on a column of Sephadex G‐75. SDS‐PAGE of the purified lectin showed two protein bands with the molecular weights of 55 000 and 60 000. The location of the lectin on S. rolfsii hyphae and its adsorption to conidia of Tri‐choderma were determined by indirect imrnunofluorescence, with antiserum raised against the purified lectin. The possible role of this lectin in S. rolfsii‐Trichoderma cell interaction is discussed.
UR - http://www.scopus.com/inward/record.url?scp=0025148354&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2672.1990.tb02917.x
DO - 10.1111/j.1365-2672.1990.tb02917.x
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AN - SCOPUS:0025148354
SN - 0021-8847
VL - 69
SP - 101
EP - 112
JO - Journal of Applied Bacteriology
JF - Journal of Applied Bacteriology
IS - 1
ER -