The β-1,3-glucanosyltransferases (Gels) affect the structure of the rice blast fungal cell wall during appressorium-mediated plant infection

Marketa Samalova, Hugo Melida, Francisco Vilaplana, Vincent Bulone, Darren M. Soanes, Nicholas J. Talbot, Sarah J. Gurr

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Abstract

The fungal wall is pivotal for cell shape and function, and in interfacial protection during host infection and environmental challenge. Here, we provide the first description of the carbohydrate composition and structure of the cell wall of the rice blast fungus Magnaporthe oryzae. We focus on the family of glucan elongation proteins (Gels) and characterize five putative β‐1,3‐glucan glucanosyltransferases that each carry the Glycoside Hydrolase 72 signature. We generated targeted deletion mutants of all Gel isoforms, that is, the GH72+, which carry a putative carbohydrate‐binding module, and the GH72 Gels, without this motif. We reveal that M. oryzae GH72+ GELs are expressed in spores and during both infective and vegetative growth, but each individual Gel enzymes are dispensable for pathogenicity. Further, we demonstrated that a Δgel1Δgel3Δgel4 null mutant has a modified cell wall in which 1,3‐glucans have a higher degree of polymerization and are less branched than the wild‐type strain. The mutant showed significant differences in global patterns of gene expression, a hyper‐branching phenotype and no sporulation, and thus was unable to cause rice blast lesions (except via wounded tissues). We conclude that Gel proteins play significant roles in structural modification of the fungal cell wall during appressorium‐mediated plant infection.

Original languageEnglish
Article number12659
Number of pages14
JournalCellular Microbiology
Volume19
Issue number3
Early online date29 Aug 2016
DOIs
Publication statusPublished - Mar 2017

Keywords

  • MAGNAPORTHE-GRISEA
  • SACCHAROMYCES-CEREVISIAE
  • ASPERGILLUS-FUMIGATUS
  • CANDIDA-ALBICANS
  • MOLECULAR-ORGANIZATION
  • EXPRESSION ANALYSIS
  • PATHOGENIC FUNGUS
  • HOST PENETRATION
  • PLASMA-MEMBRANE
  • PROTEIN GAS1P

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