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

Andersson, Karl-Magnus (author)
Lund University,Lunds universitet,MEMEG,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science
Meerupati, Tejashwari (author)
Lund University,Lunds universitet,MEMEG,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science
Levander, Fredrik (author)
Lund University,Lunds universitet,Institutionen för immunteknologi,Institutioner vid LTH,Lunds Tekniska Högskola,Department of Immunotechnology,Departments at LTH,Faculty of Engineering, LTH
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Friman, Eva (author)
Lund University,Lunds universitet,MEMEG,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science
Ahrén, Dag (author)
Lund University,Lunds universitet,MEMEG,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science
Tunlid, Anders (author)
Lund University,Lunds universitet,MEMEG,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science
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 (creator_code:org_t)
2013
2013
English.
In: Applied and Environmental Microbiology. - 0099-2240. ; 79:16, s. 4993-5004
  • Journal article (peer-reviewed)
Abstract Subject headings
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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 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.

Subject headings

NATURVETENSKAP  -- Biologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences (hsv//eng)

Publication and Content Type

art (subject category)
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