Aspergillus flavus VelB acts distinctly from VeA in conidiation and may coordinate with FluG to modulate sclerotial production

The proteins VeA, VelB and LaeA of Aspergillus nidulans form a heterotrimeric complex (the velvet complex) in the dark to coordinate sexual development and production of some secondary metabolites. VeA and VelB of A. nidulans and Aspergillus fumigatus also are repressors of conidiation, but VeA of Aspergillus flavus in studied strains acts positively on conidiation. In the present study, we show via yeast-two hybrid assays that interactions among A. flavus VeA, VelB, and LaeA are conserved as in the A. nidulans velvet complex. We found that FluG, which is required for conidiophore formation in A. nidulans but whose deletion in A. flavus delays onset of conidiation, was probably an interacting partner of VelB. Deletion of velB in A. flavus CA14 severely impaired conidiation in the dark although to a lesser extent than deletion of veA. In both mutants fluG deletion resulted in further decreased conidiation even in the light. Deletion of fluG in the Delta laeA strain, however, did not affect conidiation. All mutant types were unable to produce aflatoxin and sclerotia. Cross-complementation of the Delta velB strain with gpdA::veA restored conidiation but not aflatoxin production although aflR, the aflatoxin pathway regulatory gene, was expressed at a normal level. Cross-complementation of the Delta veA strain with gpdA::velB failed to restore conidiation and aflatoxin production. The Delta velB strain complemented with or a wild type transformed by gpdA::velB had elevated sclerotial production as the Delta fluG strain. Concerted interactions of A. flavus VeA and VelB with LaeA are critical for conidiation and aflatoxin biosynthesis. VelB may have a dual role and likely coordinates with FluG to modulate sclerotial production. Published by Elsevier Inc.