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To cause disease in maize, the biotrophic fungus  Ustilago maydis  secretes a large arsenal of effector proteins. Here, we functionally characterize the repetitive effector Rsp3 ( r epetitive  s ecreted  p rotein 3), which shows length polymorphisms in field isolates and is highly expressed during biotrophic stages. Rsp3 is required for virulence and anthocyanin accumulation. During biotrophic growth, Rsp3 decorates the hyphal surface and interacts with at least two secreted maize DUF26-domain family proteins (designated AFP1 and AFP2). AFP1 binds mannose and displays antifungal activity against the  rsp3  mutant but not against a strain constitutively expressing  rsp3 . Maize plants silenced for AFP1 and AFP2 partially rescue the virulence defect of  rsp3  mutants, suggesting that blocking the antifungal activity of AFP1 and AFP2 by the Rsp3 effector is an important virulence function. Rsp3 orthologs are present in all sequenced smut fungi, and the ortholog from  Sporisorium reilianum  can complement the  rsp3  mutant of  U. maydis , suggesting a novel widespread fungal protection mechanism.

The Ustilago maydis repetitive effector Rsp3 blocks the antifungal activity of mannose-binding maize proteins