title: The sugarcane defense protein SUGARWIN2 causes cell death in Colletotrichum falcatum but not in non-pathogenic fungi.
abstract: Plants respond to pathogens and insect attacks by inducing and accumulating a large set of defense-related proteins. Two homologues of a barley wound-inducible protein (BARWIN) have been characterized in sugarcane, SUGARWIN1 and SUGARWIN2 (sugarcane wound-inducible proteins). Induction of SUGARWINs occurs in response to Diatraea saccharalis damage but not to pathogen infection. In addition, the protein itself does not show any effect on insect development; instead, it has antimicrobial activities toward Fusarium verticillioides, an opportunistic fungus that usually occurs after D. saccharalis borer attacks on sugarcane. In this study, we sought to evaluate the specificity of SUGARWIN2 to better understand its mechanism of action against phytopathogens and the associations between fungi and insects that affect plants. We used Colletotrichum falcatum, a fungus that causes red rot disease in sugarcane fields infested by D. saccharalis, and Ceratocystis paradoxa, which causes pineapple disease in sugarcane. We also tested whether SUGARWIN2 is able to cause cell death in Aspergillus nidulans, a fungus that does not infect sugarcane, and in the model yeast Saccharomyces cerevisiae, which is used for bioethanol production. Recombinant SUGARWIN2 altered C. falcatum morphology by increasing vacuolization, points of fractures and a leak of intracellular material, leading to germling apoptosis. In C. paradoxa, SUGARWIN2 showed increased vacuolization in hyphae but did not kill the fungi. Neither the non-pathogenic fungus A. nidulans nor the yeast S. cerevisiae was affected by recombinant SUGARWIN2, suggesting that the protein is specific to sugarcane opportunistic fungal pathogens.
authors.affiliation: Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, SP, Brazil.
authors.forename: Flávia P
authors.initials: FP
authors.lastname: Franco
authors.affiliation: Departamento de Genética e Evolução, Universidade Federal de São Carlos, São Carlos, SP, Brazil.
authors.forename: Adelita C
authors.initials: AC
authors.lastname: Santiago
authors.affiliation: Departamento de Genética e Evolução, Universidade Federal de São Carlos, São Carlos, SP, Brazil.
authors.forename: Flávio
authors.initials: F
authors.lastname: Henrique-Silva
authors.affiliation: Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
authors.forename: Patrícia Alves
authors.initials: PA
authors.lastname: de Castro
authors.affiliation: Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Ribeirão Preto, SP, Brazil; Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE), Campinas, SP, Brazil.
authors.forename: Gustavo H
authors.initials: GH
authors.lastname: Goldman
authors.affiliation: Departamento de Ciências Biológicas, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, SP, Brazil.
authors.forename: Daniel S
authors.initials: DS
authors.lastname: Moura
authors.affiliation: Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, SP, Brazil.
authors.forename: Marcio C
authors.initials: MC
authors.lastname: Silva-Filho
mesh_terms: D001230:Aspergillus / Q000166:cytology / Q000187:drug effects; D016923:Cell Death / Q000187:drug effects; D020231:Colletotrichum / Q000166:cytology* / Q000187:drug effects; D025282:Mycelium / Q000166:cytology / Q000187:drug effects; D010940:Plant Proteins / Q000494:pharmacology*; D011994:Recombinant Proteins / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000187:drug effects; D031786:Saccharum / Q000378:metabolism* / Q000382:microbiology
chemical_list: D010940:Plant Proteins; D011994:Recombinant Proteins