Fungal attachment to nematodes

Tunlid, Anders; Jansson, Hans; Nordbring‐Hertz, Birgit

doi:10.1016/s0953-7562(09)81082-4

Cited by 95 publications

(30 citation statements)

References 55 publications

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“…Tyrosinases also oxidize protein-and peptide-bound tyrosyl residues, resulting in the formation of inter-and intramolecular cross-links between peptides, proteins, and carbohydrates (84). Cross-linking between proteins and polymers present in the extracellular layer might have a role in mediating binding between the trap of nematode-trapping fungi and the nematode cuticle (85).…”

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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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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“…The extracellular fibrillar polymers of trap cell walls contain mainly proteins and carbohydrates (Tunlid, Johansson & Nordbring-Hertz, 1991). The adhesion of nematodes to the surface of the traps is considered as just one step in the infection (Tunlid et al, 1992), during which the fibrils become more dense and oriented in one direction (Veenhuis et al, 1985a).…”

Section: Diversity Of Trapping Structures In Arthrobotrysmentioning

confidence: 99%

Morphogenesis in the nematode-trapping fungus Arthrobotrys oligospora - an extensive plasticity of infection structures

Nordbring‐Hertz

2004

Mycologist

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“…(Jones, 1994 ;Nicholson & Kunoh, 1995 ;Nicholson, 1996). ECM has been found in a wide range of fungi, including aquatic, nematophagous, plant pathogenic and wood-decaying species (Tunlid, Jansson & Nordbring-Hertz, 1992 ;Nicole et al, 1993 ;Jones, 1994). Not much is known about the functions or importance of extracellular matrix.…”

Section: Introductionmentioning

confidence: 99%

Visualization and characterization of the extracellular matrix of Bipolaris sorokiniana

Apoga

Jansson

2000

Mycological Research

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Extracellular matrix (ECM) surrounding conidia and germlings of B. sorokiniana was studied using light microscopy (LM), scanning (SEM) and transmission electron microscopy (TEM). Conidial ECM surrounding dry-inoculated, ungerminated conidia was fluid-like and observed only using a cryo-preparation technique, suggesting that the material was water soluble. ECM enveloping germlings appeared fibrillar in LM, TEM and SEM but amorphous in cryo-SEM, indicating that the structure of the ECM is dependent on the water content of the matrix. Fibrillar ECM formed thread-like structures that extended over long distances on the substrate or towards neighbouring conidia and hyphae. TEM of germlings negatively stained with uranyl acetate revealed the presence of fungal fimbriae. The strong resemblance between the extending organization of fibrillar thread-like ECM structures and fimbriae suggested that fimbriae constitute a basic structural component of the ECM and serve as the aggregation centre for the other ECM components. Histochemical labelling revealed significant differences between ECM surrounding the fungus at different morphological stages. The germ tube ECM was labelled for both proteins and polysaccharides whereas germling ECM consisted of two layers : an inner rich in proteins and an outer composed mainly of polysaccharides. Furthermore, the newly released ECM localized on germ tubes and hyphal tips showed affinity for microspheres carrying any type of surface properties while hyphal ECM had affinity only for negatively charged microspheres. This together suggests that ECM after its release is subjected to structural changes.

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Fungal attachment to nematodes

Cited by 95 publications

References 55 publications

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

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

Morphogenesis in the nematode-trapping fungus Arthrobotrys oligospora - an extensive plasticity of infection structures

Visualization and characterization of the extracellular matrix of Bipolaris sorokiniana

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