title: Identification of botryticidal proteins with similarity to NBS-LRR proteins in rosemary pepper (Lippia sidoides Cham.) flowers.
abstract: Heavy agricultural losses are closely related to attacks by insect-pests and phytopathogens such as bacteria and fungi. Among them, the fungus Botrytis cinerea can cause gray mold in more than 200 different species of plants, and is considered a challenging problem for agribusiness. Fungicides are commonly used to control this pathogen because they are fast-working and easy to apply. However, the continuous use of fungicides may promote the selection of resistant fungi and can also cause profound contamination in ecosystems. Aiming to find alternative strategies to solve these problems, several studies have focused on searching for plant proteins and peptides with antifungal activities (AFPs). With this in mind, this report shows the isolation and characterization of two novels antifungal proteins from flowers of rosemary pepper (Lippia sidoides Cham.) with 10 and 15 kDa. Isolation was performed by using an Octyl-Sepharose hydrophobic column. In vitro bioassays indicated that isolated proteins were able to inhibit B. cinerea development, but were not effective against all bacteria tested. Moreover, N-termini sequences indicate that both proteins showed sequence homology with NBS-LRR R proteins with a lower molecular mass, suggesting possible protein fragmentation. Data reported here could help in the development of biotechnological products for crop protection against phytopathogenic fungi in the near future.
authors.affiliation: Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, SGAN Quadra 916, Módulo B, Av. W5 Norte 70. 790-160 Asa Norte, Brasília, DF-Brazil. josuender@gmail.com
authors.forename: João S
authors.initials: JS
authors.lastname: Moreira
authors.forename: Renato G
authors.initials: RG
authors.lastname: Almeida
authors.forename: Letícia S
authors.initials: LS
authors.lastname: Tavares
authors.forename: Marcelo O
authors.initials: MO
authors.lastname: Santos
authors.forename: Lyderson F
authors.initials: LF
authors.lastname: Viccini
authors.forename: Ilka M
authors.initials: IM
authors.lastname: Vasconcelos
authors.forename: José T A
authors.initials: JT
authors.lastname: Oliveira
authors.forename: Nádia R B
authors.initials: NR
authors.lastname: Raposo
authors.forename: Simoni C
authors.initials: SC
authors.lastname: Dias
authors.forename: Octavio L
authors.initials: OL
authors.lastname: Franco
mesh_terms: D000249:Adenosine Monophosphate / Q000031:analogs & derivatives / Q000737:chemistry / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000818:Animals; D020171:Botrytis; D001938:Brazil; D035264:Flowers / Q000737:chemistry; D005659:Fungicides, Industrial / Q000737:chemistry* / Q000302:isolation & purification*; D032411:Lippia / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D013873:Thionucleotides / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D005659:Fungicides, Industrial; D010455:Peptides; D010940:Plant Proteins; D013873:Thionucleotides; C557284:antimicrobial peptide 1, Lippia sidoides; C557285:antimicrobial peptide 2, Lippia sidoides; C014308:adenosine 5'-phosphorothioate; D000249:Adenosine Monophosphate