Claim · model-written summary
A time-dependent core exoproteome was shared among isolates regardless of virulence.
- Taxon
- Peach
Prunus persicat0 - Outcome
- core-exoproteome among isolatese0
- Qualifier
- independently of their virulence but time-dependente0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValue
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“A core-exoproteome among isolates independently of their virulence but time-dependent was also described”
t0“Peach Tissue”
Title
Proteomic Studies to Understand the Mechanisms of Peach Tissue Degradation by Monilinia laxa
Silvia Rodríguez-Pires; Paloma Melgarejo; Antonieta De Cal; et al. Frontiers in Plant Science 2020. doi:10.3389/fpls.2020.01286
Other claims from this paper (14)
- Observation Isolate 8L was the most aggressive on nectarine fruit.
- Observation Isolate 33L had intermediate virulence on nectarine fruit.
- Observation Isolate 5L was weakly aggressive on nectarine fruit.
- Observation Nectarine colonization by isolate 5L was strongly delayed.
- Observation The 8L exoproteome contained 181 identified proteins at 3 dpi.
- Observation The 33L exoproteome contained 289 identified proteins at 3 dpi.
- Observation The 5L exoproteome contained 206 identified proteins at 7 dpi.
- Observation Most identified exoproteins belonged to the metabolism OG group.
- Observation Carbohydrate transport and metabolism was represented in isolate 5L.
- Observation Energy production and conversion was most represented in isolates 8L and 33L.
- Observation Carbohydrate-active enzymes and peptidases showed different alternatives with the same function among isolates.
- Association Secreted MlPG1, MlPME3, NEP-like and endoglucanase proteins were proposed as markers of higher virulence.
- Observation The core exoproteome included cutinase, pectin lyases and acid proteases.
- Mechanism Secretion patterns supported an extensive M. laxa protein repertoire facilitating host infection and colonization.