title: The Botrytis cinerea xylanase Xyn11A contributes to virulence with its necrotizing activity, not with its catalytic activity.
abstract: BACKGROUND
  The Botrytis cinerea xylanase Xyn11A has been previously shown to be required for full virulence of this organism despite its poor contribution to the secreted xylanase activity and the low xylan content of B. cinerea hosts. Intriguingly, xylanases from other fungi have been shown to have the property, independent of the xylan degrading activity, to induce necrosis when applied to plant tissues, so we decided to test the hypothesis that secreted Xyn11A contributes to virulence by promoting the necrosis of the plant tissue surrounding the infection, therefore facilitating the growth of this necrotroph.
  
  
  RESULTS
  We show here that Xyn11A has necrotizing activity on plants and that this capacity is conserved in site-directed mutants of the protein lacking the catalytic activity. Besides, Xyn11A contributes to the infection process with the necrotizing and not with the xylan hydrolyzing activity, as the catalytically-impaired Xyn11A variants were able to complement the lower virulence of the xyn11A mutant. The necrotizing activity was mapped to a 30-amino acids peptide in the protein surface, and this region was also shown to mediate binding to tobacco spheroplasts by itself.
  
  
  CONCLUSIONS
  The main contribution of the xylanase Xyn11A to the infection process of B. cinerea is to induce necrosis of the infected plant tissue. A conserved 30-amino acids region on the enzyme surface, away from the xylanase active site, is responsible for this effect and mediates binding to plant cells.
authors.affiliation: Departamento de Bioquímica y Biología Molecular, Universidad de La Laguna, Tenerife, Spain.
authors.forename: Judith
authors.initials: J
authors.lastname: Noda
authors.forename: Nélida
authors.initials: N
authors.lastname: Brito
authors.forename: Celedonio
authors.initials: C
authors.lastname: González
mesh_terms: D000595:Amino Acid Sequence; D020171:Botrytis / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D003001:Cloning, Molecular; D043364:Endo-1,4-beta Xylanases / Q000235:genetics / Q000378:metabolism*; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D018551:Solanum lycopersicum / Q000382:microbiology; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010935:Plant Diseases / Q000382:microbiology*; D016415:Sequence Alignment; D014026:Nicotiana / Q000382:microbiology; D014774:Virulence
chemical_list: D005656:Fungal Proteins; D043364:Endo-1,4-beta Xylanases