Linked Life Data

8012587

Source:http://linkedlifedata.com/resource/pubmed/id/8012587

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1994-7-25
pubmed:abstractText
A novel lectin was isolated and purified from the culture filtrate of the soilborne plant pathogenic fungus Sclerotium rolfsii by anion-exchange chromatography using a DEAE-Sepharose column. The lectin came through the column with the flow-through, whereas all the non-agglutinating proteins present in the crude preparation remained bound to the column until elution in a NaCl gradient. SDS-PAGE analysis of the agglutinating fraction revealed a single band corresponding to a protein with a molecular mass of approximately 45 kDa. Agglutination of Escherichia coli cells by the purified lectin was not inhibited by any of the mono- or disaccharides tested, whereas the glycoproteins mucin and asialomucin did inhibit agglutination. Proteases, as well as 1,3-beta-glucanase, were found to be totally destructive to agglutination activity, indicating that both protein and 1,3-beta-glucan are necessary for agglutination. Using a biomimetic system based on binding of the lectin to the surface of inert nylon fibres revealed that the presence of the purified agglutinin on the surface of the fibres specifically induced mycoparasitic behaviour in Trichoderma harzianum. Trichoderma formed tightly adhering coils, which were significantly more frequent with the purified agglutinin-treated fibres than with untreated ones or with those treated with non-agglutinating extracellular proteins from S. rolfsil. Other mycoparasite-related structures, such as appressorium-like bodies and hyphal loops, were only observed in the interaction between T. harzianum and the purified agglutinin-treated fibres.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
140 ( Pt 3)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
651-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
A newly isolated lectin from the plant pathogenic fungus Sclerotium rolfsii: purification, characterization and role in mycoparasitism.
pubmed:affiliation
Otto Warburg Center for Agricultural Biotechnology, Hebrew University of Jerusalem, Faculty of Agriculture, Rehovot, Israel.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't