Advanced

Purification and characterization of a surface lectin from the nematode-trapping fungus Arthrobotrys oligospora

Rosen, S. LU ; Ek, Bo ; Rask, L. and Tunlid, A. LU (1992) In Journal of General Microbiology 138(12). p.2663-2672
Abstract

Several studies have indicated that the capture of nematodes by the nematophagous fungus Arthrobotrys oligospora is mediated by a lectin on the fungal surface. One of the major surface proteins of this fungus showed haemagglutinating activity and was isolated by affinity chromatography using a mucin Sepharose column. Biochemical analysis showed that the protein was a dimeric glycoprotein with a molecular mass of 36 kDa and an isoelectric point of pH 6.5, and contained no sulphur amino acids. The protein was N-terminally blocked; four internal peptides were sequenced, and showed no significant similarity to sequences in the Swiss-Prot or PIR databases. The haemagglutinating activity of the isolated protein was not inhibited by any of the... (More)

Several studies have indicated that the capture of nematodes by the nematophagous fungus Arthrobotrys oligospora is mediated by a lectin on the fungal surface. One of the major surface proteins of this fungus showed haemagglutinating activity and was isolated by affinity chromatography using a mucin Sepharose column. Biochemical analysis showed that the protein was a dimeric glycoprotein with a molecular mass of 36 kDa and an isoelectric point of pH 6.5, and contained no sulphur amino acids. The protein was N-terminally blocked; four internal peptides were sequenced, and showed no significant similarity to sequences in the Swiss-Prot or PIR databases. The haemagglutinating activity of the isolated protein was not inhibited by any of the mono- or disaccharides tested, but it was inhibited by the glycoproteins fetuin and mucin. The haemagglutinating activity changed after incubating the protein in buffers of different pH, with maximal activity at pH 11.0 and no activity at pH 2.8. The lectin was tested for different enzymic activities but none were detected. Analysis of the haemagglutinating activity in various cell fractions indicated that the protein was associated with extracellular polymer layers and with the cell wall of the fungus. About the same amount of the haemagglutinating protein was recovered from samples of vegetative mycelium and of mycelium containing nematode-trapping cells.

(Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of General Microbiology
volume
138
issue
12
pages
2663 - 2672
publisher
MAIK Nauka/Interperiodica
external identifiers
  • pmid:1487732
  • scopus:0027102486
ISSN
0022-1287
DOI
10.1099/00221287-138-12-2663
language
English
LU publication?
yes
id
dc1d2e75-7c6a-4e98-be60-ff44eb07e873
date added to LUP
2019-10-23 17:16:17
date last changed
2020-01-13 02:28:31
@article{dc1d2e75-7c6a-4e98-be60-ff44eb07e873,
  abstract     = {<p>Several studies have indicated that the capture of nematodes by the nematophagous fungus Arthrobotrys oligospora is mediated by a lectin on the fungal surface. One of the major surface proteins of this fungus showed haemagglutinating activity and was isolated by affinity chromatography using a mucin Sepharose column. Biochemical analysis showed that the protein was a dimeric glycoprotein with a molecular mass of 36 kDa and an isoelectric point of pH 6.5, and contained no sulphur amino acids. The protein was N-terminally blocked; four internal peptides were sequenced, and showed no significant similarity to sequences in the Swiss-Prot or PIR databases. The haemagglutinating activity of the isolated protein was not inhibited by any of the mono- or disaccharides tested, but it was inhibited by the glycoproteins fetuin and mucin. The haemagglutinating activity changed after incubating the protein in buffers of different pH, with maximal activity at pH 11.0 and no activity at pH 2.8. The lectin was tested for different enzymic activities but none were detected. Analysis of the haemagglutinating activity in various cell fractions indicated that the protein was associated with extracellular polymer layers and with the cell wall of the fungus. About the same amount of the haemagglutinating protein was recovered from samples of vegetative mycelium and of mycelium containing nematode-trapping cells.</p>},
  author       = {Rosen, S. and Ek, Bo and Rask, L. and Tunlid, A.},
  issn         = {0022-1287},
  language     = {eng},
  month        = {01},
  number       = {12},
  pages        = {2663--2672},
  publisher    = {MAIK Nauka/Interperiodica},
  series       = {Journal of General Microbiology},
  title        = {Purification and characterization of a surface lectin from the nematode-trapping fungus Arthrobotrys oligospora},
  url          = {http://dx.doi.org/10.1099/00221287-138-12-2663},
  doi          = {10.1099/00221287-138-12-2663},
  volume       = {138},
  year         = {1992},
}