the botrytis cinerea xylanase xyn11a contributes to virulence with its necrotizing activity, not with its catalytic activity葡萄孢菌的木聚糖酶xyn11a导致毒性坏死的活动,而不是它的催化活性.pdfVIP
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the botrytis cinerea xylanase xyn11a contributes to virulence with its necrotizing activity, not with its catalytic activity葡萄孢菌的木聚糖酶xyn11a导致毒性坏死的活动,而不是它的催化活性
Noda et al. BMC Plant Biology 2010, 10:38
/1471-2229/10/38
RESEARCH ARTICLE Open Access
The Botrytis cinerea xylanase Xyn11A contributes
to virulence with its necrotizing activity, not with
its catalytic activity
*
Judith Noda, Nélida Brito, Celedonio González
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 cel
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