EconPapers    
Economics at your fingertips  
 

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

Lay-Sun Ma, Lei Wang, Christine Trippel, Artemio Mendoza-Mendoza, Steffen Ullmann, Marino Moretti, Alexander Carsten, Jörg Kahnt, Stefanie Reissmann, Bernd Zechmann, Gert Bange and Regine Kahmann ()
Additional contact information
Lay-Sun Ma: Max Planck Institute for Terrestrial Microbiology
Lei Wang: Max Planck Institute for Terrestrial Microbiology
Christine Trippel: Max Planck Institute for Terrestrial Microbiology
Artemio Mendoza-Mendoza: Max Planck Institute for Terrestrial Microbiology
Steffen Ullmann: Max Planck Institute for Terrestrial Microbiology
Marino Moretti: Max Planck Institute for Terrestrial Microbiology
Alexander Carsten: Max Planck Institute for Terrestrial Microbiology
Jörg Kahnt: Max Planck Institute for Terrestrial Microbiology
Stefanie Reissmann: Max Planck Institute for Terrestrial Microbiology
Bernd Zechmann: Baylor University
Gert Bange: Philipps-Universität Marburg
Regine Kahmann: Max Planck Institute for Terrestrial Microbiology

Nature Communications, 2018, vol. 9, issue 1, 1-15

Abstract: Abstract 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 (repetitive secreted protein 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.

Date: 2018
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-018-04149-0 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04149-0

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-018-04149-0

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().

 
Page updated 2025-03-19
Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04149-0