A CLC-type @entity2865 channel gene is required for laccase activity and virulence in XXXX .

@entity1 @entity8487 @entity1328 @entity19 @entity1327 @entity2734 @entity920 @entity1129 @entity2865 @entity70546 @entity375 @entity1063
Laccase is a major virulence factor required for infection caused by the @entity1 pathogenic @entity375 @entity1327 . However, cellular processes involved in the regulation and expression of laccase remain largely unknown in @entity1327 . Here we report the identification of a @entity2865 channel gene @entity1129 which is essential for laccase activity in @entity1327 . @entity1129 shares homology to CLC-type voltage-gated @entity2865 channels from other organisms; for example, 63% homology to @entity70546 , a @entity2865 channel gene from @entity375 . A clc-a mutant, Mlac3, generated by insertional mutagenesis as well as a targeted Deltaclc-a mutant produced undetectable laccase in a liquid assay and produced no melanin on @entity2734 agar containing @entity1063 . Mlac3 was complemented with wild-type @entity1129 which restored laccase activity and melanin biosynthesis. The clc-a mutants also showed reduced synthesis of another important virulence factor, capsule, and showed reduced growth at @entity8487 . In addition, the clc-a mutation resulted in attenuated virulence in a @entity19 @entity1328 model that was restored by complementation with wild-type @entity1129 , indicating that the @entity2865 channel plays an important role in the virulence of the organism. Further analysis revealed that the basis for absent laccase expression in the clc-a mutant was a laccase transcriptional defect that could be restored by adding exogenous @entity920 . In conclusion, our findings show that @entity1129 plays a role in the expression of two important virulence factors, capsule and laccase expression, which are required for virulence of the fungal pathogen.
