A cytoplasmic lectin produced by the fungus Arthrobotrys oligospora functions as a storage protein during saprophytic and parasitic growth
(1997) In Microbiology 143(8). p.2593-2604- Abstract
It was recently shown that the nematode-infecting fungus Arthrobotrys oligospora contains a saline-soluble lectin (designated AOL) that is a member of a novel family of fungal lectins sharing similar primary sequences and binding specificities. During saprophytic growth in liquid cultures, levels of AOL and AOL mRNA were found to vary depending on the growth phase of the mycelium and the carbon/nitrogen (C/N) ratio of the medium. AOL was not detected in young mycelium. In older mycelium (stationary growth phase) grown in media with low UN ratios (1 or 6), AOL comprised 5-20% of the total amount of saline-soluble proteins present in the mycelium. Neither the lectin nor its transcript was detected in mycelia grown in medium with higher... (More)
It was recently shown that the nematode-infecting fungus Arthrobotrys oligospora contains a saline-soluble lectin (designated AOL) that is a member of a novel family of fungal lectins sharing similar primary sequences and binding specificities. During saprophytic growth in liquid cultures, levels of AOL and AOL mRNA were found to vary depending on the growth phase of the mycelium and the carbon/nitrogen (C/N) ratio of the medium. AOL was not detected in young mycelium. In older mycelium (stationary growth phase) grown in media with low UN ratios (1 or 6), AOL comprised 5-20% of the total amount of saline-soluble proteins present in the mycelium. Neither the lectin nor its transcript was detected in mycelia grown in medium with higher C/N ratios (≤ 150). Under conditions of nitrogen starvation, AOL was preferentially degraded in relation to the total amount of saline-soluble proteins present in the mycelium. During the infection of nematodes, the level of AOL protein and AOL mRNA increased significantly once the nematodes had been penetrated and digested. Large amounts of AOL accumulated in the trophic hyphae growing inside the nematode as visualized by immunofluorescence microscopy. Later, AOL labelling was detected outside the digested nematodes, preferentially in strands of aggregated hyphae and in newly developed trap cells. Electron microscopy showed that AOL was localized to the cytoplasm and the nucleus-of both vegetative mycelium and trap cells, and in the trophic hyphae growing inside the infected nematodes. These results indicate that AOL functions as a storage protein during both saprophytic and parasitic growth.
(Less)
- author
- Rosén, Stefan LU ; Sjollema, Klaas ; Veenhuis, Marten and Tunlid, Anders LU
- organization
- publishing date
- 1997-01-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Immunolocalization, Lectin, Nematophagous fungus, Storage protein
- in
- Microbiology
- volume
- 143
- issue
- 8
- pages
- 2593 - 2604
- publisher
- MAIK Nauka/Interperiodica
- external identifiers
-
- scopus:0030765765
- ISSN
- 1350-0872
- DOI
- 10.1099/00221287-143-8-2593
- language
- English
- LU publication?
- yes
- id
- 0671592a-40ab-44ef-9005-0439f44c0407
- date added to LUP
- 2019-10-23 17:04:25
- date last changed
- 2024-01-01 22:29:21
@article{0671592a-40ab-44ef-9005-0439f44c0407,
abstract = {{<p>It was recently shown that the nematode-infecting fungus Arthrobotrys oligospora contains a saline-soluble lectin (designated AOL) that is a member of a novel family of fungal lectins sharing similar primary sequences and binding specificities. During saprophytic growth in liquid cultures, levels of AOL and AOL mRNA were found to vary depending on the growth phase of the mycelium and the carbon/nitrogen (C/N) ratio of the medium. AOL was not detected in young mycelium. In older mycelium (stationary growth phase) grown in media with low UN ratios (1 or 6), AOL comprised 5-20% of the total amount of saline-soluble proteins present in the mycelium. Neither the lectin nor its transcript was detected in mycelia grown in medium with higher C/N ratios (≤ 150). Under conditions of nitrogen starvation, AOL was preferentially degraded in relation to the total amount of saline-soluble proteins present in the mycelium. During the infection of nematodes, the level of AOL protein and AOL mRNA increased significantly once the nematodes had been penetrated and digested. Large amounts of AOL accumulated in the trophic hyphae growing inside the nematode as visualized by immunofluorescence microscopy. Later, AOL labelling was detected outside the digested nematodes, preferentially in strands of aggregated hyphae and in newly developed trap cells. Electron microscopy showed that AOL was localized to the cytoplasm and the nucleus-of both vegetative mycelium and trap cells, and in the trophic hyphae growing inside the infected nematodes. These results indicate that AOL functions as a storage protein during both saprophytic and parasitic growth.</p>}},
author = {{Rosén, Stefan and Sjollema, Klaas and Veenhuis, Marten and Tunlid, Anders}},
issn = {{1350-0872}},
keywords = {{Immunolocalization; Lectin; Nematophagous fungus; Storage protein}},
language = {{eng}},
month = {{01}},
number = {{8}},
pages = {{2593--2604}},
publisher = {{MAIK Nauka/Interperiodica}},
series = {{Microbiology}},
title = {{A cytoplasmic lectin produced by the fungus Arthrobotrys oligospora functions as a storage protein during saprophytic and parasitic growth}},
url = {{http://dx.doi.org/10.1099/00221287-143-8-2593}},
doi = {{10.1099/00221287-143-8-2593}},
volume = {{143}},
year = {{1997}},
}