Deletion of a lectin gene does not affect the phenotype of the nematode-trapping fungus Arthrobotrys oligospora

Balogh, Johanna; Tunlid, Anders; Rosén, Stefan

doi:10.1016/s1087-1845(03)00023-9

Cited by 44 publications

(29 citation statements)

References 33 publications

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“…Similarly, expression of SRL is much higher in sclerotia than in vegetative mycelium (Swamy et al 2004). Using respective knockout mutants, TAP1 and AOL 2 were shown not to be essential for the formation of fruiting bodies (Nowrousian and Cebula 2005) or the function of nematode traps, respectively (Balogh et al 2003).…”

Section: Actinoporin-type Lectinsmentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

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Section: Actinoporin-type Lectinsmentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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“…Later, a gene encoding such a lectin was characterized from A. oligospora (60). However, deletion of the gene did not affect the ability to infect nematodes (61), which suggests that the fungus might express other lectins mediating attachment to nematodes. Indeed, in the recently published ge- nome of A. oligospora, seven lectins with different sugar specificities were identified (10).…”

Section: Cell Surface Proteins (I) Proteins Containing the Wsc Domaimentioning

confidence: 99%

Proteome of the Nematode-Trapping Cells of the Fungus Monacrosporium haptotylum

Andersson

Meerupati

Levander

et al. 2013

Appl Environ Microbiol

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Many nematophagous fungi use morphological structures called traps to capture nematodes by adhesion or mechanically. To better understand the cellular functions of adhesive traps, the trap cell proteome of the fungus Monacrosporium haptotylum was characterized. The trap of M. haptotylum consists of a unicellular structure called a knob that develops at the apex of a hypha. Proteins extracted from knobs and mycelia were analyzed using SDS-PAGE and liquid chromatography-tandem mass spectrometry (LC-MS-MS). The peptide sequences were matched against predicted gene models from the recently sequenced M. haptotylum genome. In total, 336 proteins were identified, with 54 expressed at significantly higher levels in the knobs than in the mycelia. The upregulated knob proteins included peptidases, small secreted proteins with unknown functions, and putative cell surface adhesins containing carbohydrate-binding domains, including the WSC domain. Phylogenetic analysis showed that all upregulated WSC domain proteins belonged to a large, expanded cluster of paralogs in M. haptotylum. Several peptidases and homologs of experimentally verified proteins in other pathogenic fungi were also upregulated in the knob proteome. Complementary profiling of gene expression at the transcriptome level showed poor correlation between the upregulation of knob proteins and their corresponding transcripts. We propose that the traps of M. haptotylum contain many of the proteins needed in the early stages of infection and that the trap cells can tightly control the translation and degradation of these proteins to minimize the cost of protein synthesis. N ematode-trapping fungi have the unique ability to capture and infect free-living nematodes (1). Given their potential use as biological control agents for plant-and animal-parasitic nematodes (2), there is much interest in studying their infection biology. To enter the parasitic stage, nematode-trapping fungi develop a unique morphological structure called traps. These traps develop from hyphal branches, either spontaneously or in response to signals from the environment, such as peptides or other compounds released by the host nematode (3). Molecular phylogeny studies have shown that the majority of nematode-trapping fungi belong to a monophyletic group in the order Orbiliales (Ascomycota). Within this clade, the trapping mechanisms have evolved along two major lineages, one leading to species with constricting rings and the other to species with adhesive traps, including three-dimensional networks, knobs, and branches (4-6).Despite large variation in their morphology, adhesive traps share a unique ultrastructure that clearly separates them from vegetative hyphae (3). One feature that is common to all traps is the presence of numerous cytosolic organelles called dense bodies. These organelles have catalase and D-amino acid oxidase activities, which indicates that they are peroxisome-like organelles (3). However, the function of these organelles is not yet fully understood. Another feature of th...

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“…This approach offers the opportunity to infer the fitness consequence for both the fungus and the fungivore when the expression of genes involved in secondary metabolite formation is impaired or enhanced but the genetic background remains unaltered. To date, however, only few studies have used mutant fungi in fungus-fungivore experiments ( Table 9.1, [77][78][79][80][81][82][83][84][85][86][87][88]). A series of studies have demonstrated that knocking out the gene laeA in Aspergillus sp.…”

Section: What Does Genetic Manipulation Of Fungal Secondary Metabolismentioning

confidence: 99%

“…In contrast, confrontation assays with such gene deletion strains even enhanced mortality of D. melanogaster larvae [84] and fungivorous springtails [98] Balogh et al [88] ko candidate gene(s) was/were knocked out, oe candidate gene was overexpressed, -, ↑, ↓ neutral, positive, or negative influence on organismic traits, n.q. organismic traits were not quantified Table 9.1 Fungal genes tested for their involvement in mediating resistance to fungivores 9 Fungal Secondary Metabolism in the Light of Animal-Fungus Interactions other metabolites or metabolite combinations are more efficient against fungivores, provided that sterigmatocystin biosynthesis is blocked.…”

Section: What Does Genetic Manipulation Of Fungal Secondary Metabolismentioning

confidence: 99%

“…Rather, the presence of the chemical shield depends on the presence of fungivores and is built de novo or secondary metabolites are synthesized to a significantly larger amount. Central to an inducible response is the activation of regulatory and biosynthetic genes involved in determining a fungus' capacity to resist fungivory (see Table 9.1, [77][78][79][80][81][82][83][84][85][86][87][88]). Such changes in gene expression are usually mediated by the combined action of cell surface receptors and intra-cellular signaling cascades.…”

Section: Induced Fungal Responses Toward Fungivore Grazers?mentioning

confidence: 99%

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Fungal Secondary Metabolism in the Light of Animal–Fungus Interactions: From Mechanism to Ecological Function

Rohlfs

2015

Fungal Biology

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Deletion of a lectin gene does not affect the phenotype of the nematode-trapping fungus Arthrobotrys oligospora

Cited by 44 publications

References 33 publications

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Proteome of the Nematode-Trapping Cells of the Fungus Monacrosporium haptotylum

Fungal Secondary Metabolism in the Light of Animal–Fungus Interactions: From Mechanism to Ecological Function

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