Javascript is not activated in your browser. This website needs javascript activated to work properly.
You are here

Proteome of the nematode-trapping cells of the fungus Monacrosporium haptotylum.

  • Karl-Magnus Andersson
  • Tejashwari Meerupati
  • Fredrik Levander
  • Eva Friman
  • Dag Ahrén
  • Anders Tunlid
Publishing year: 2013
Language: English
Pages: 4993-5004
Publication/Series: Applied and Environmental Microbiology
Volume: 79
Issue: 16
Document type: Journal article
Publisher: American Society for Microbiology

Abstract english

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 knob that develops at the apex of a hyphae. Proteins extracted from knobs and mycelia were analyzed using SDS-PAGE and 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 being expressed at significantly higher levels in the knobs than in the mycelia. The upregulated knob proteins included peptidases, small secreted proteins with unknown function 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 to 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.


  • Biological Sciences


  • ISSN: 0099-2240
Anders Tunlid
E-mail: anders [dot] tunlid [at] biol [dot] lu [dot] se

Pro dean

Faculty of Science

+46 70 314 00 67


Sölvegatan 27, Lund




+46 46 222 37 57


Sölvegatan 37, Lund